Hgt id 1-34 (Figs 1- 30) GenBank Acc. / Jgi database protein id




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HGT ID 1-34 (Figs S1.1-S1.30)

GenBank Acc. / JGI database protein ID

Reported in Richards et al 2006

Annotation

Evidence of Signal peptide and Secretion

1 (S1.1)

EEY57756

Yes (named AraJ)

Annotation by similarity search (1-3) suggests that this HGT encodes a major facilitator superfamily (MFS) transporter. The MFS transporters are single-polypeptide secondary carriers capable of transporting small solutes in response to chemi-osmotic ion gradients. The MFS is a large and diverse group of secondary transporters and can facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides (1, 2). KASS analysis suggests this protein sequence has the highest affinity with saccharide monomer transporters.

N

2 (S1.2)

82760 (P.ramorum)

Yes (named esterase/lipase – see Fig. S3B (4))

This HGT candidate encodes an extracellular protein with a putative esterase/lipase domain. The functional role of esterases and lipase enzymes is difficult to decipher based on homology searches because substrate specificity often depends upon small changes in amino acid sequences and these enzyme families have relatively few functional studies compared to the complexity of the protein families (5, 6). However, the amino acid sequence has strong sequence similarity to carotenoid ester lipase enzymes of the fungus Pleurotus sapidus which have been shown to perform efficient hydrolysis of xanthophyll esters (7) and are therefore potentially important for processing xanthophyll caretenoids found in plant tissues.
KASS database analysis also demonstrated that this gene has strong similarity to enzymes that function in sterol and lipid degradation. Interestingly, many oomycetes depend on extracellular sources of sterol and fatty acids, and the supply of these metabolites play a role in determining the transition of oomycetes through different lifecycle stages (8, 9). Although these putative extracellular enzymes may have a number of roles in releasing long chain fatty acids and terpenoids from a range of plant derived substrates (e.g. carotenoids, suberin, cutin).
This is one of four separate putative HGTs of esterase/lipase domain-containing extracellular proteins. It is difficult to predict the function of these proteins, but extracellular lipases have been shown to be important pathogenic phenotypes involved in the detection and breakdown of plant waxy cuticle (10-12) which may represent an important metabolic resource for sterol and long chain fatty acids for oomycete plant pathogens.

Y

3 (S1.3)

AAM48174.1

Yes (named GalM)

This HGT putatively encodes an aldose 1-epimerase (EC 5.1.3.3). This enzyme catalyses conversion of -D-glucose to -D-glucose and -D-galactose to -D-galactose (13) which can both be fed into glycolysis. Both -D-glucose and -D-galactose are major components of the plant cell wall with -D-galactose (-D-galactan) being a major component of pectin. The enzyme may therefore be involved in plant cell wall degradation by oomycete pathogens.
This HGT gene was recovered in a gene dense 10.8 kb BamHI fragment of the P. sojae genome project tightly linked to three gene copies of a necrosis inducing protein-encoding gene which is also a fungal derived HGT (see HGT 20 below) (14).

N

4 (S1.4)

71178

(P.ramorum)






This HGT putatively encodes an α-ketoglutarate dependent xanthine dioxygenase (XanA), an enzyme function only previously known from fungi and involved in hydroxylation of xanthine to uric acid (15)). The fungi and oomycete genes form a discrete clade, distantly related to the prokaryotic homologues (Fig. S1.4) which are of the TauD protein family. TauD from E. coli is an α-ketoglutarate-dependent taurine dioxygenase (EC 1.14.11.17). This enzyme catalyses the oxygenolytic release of sulfite from taurine. In fungi, XanA knock-out experiments in different fungal species have demonstrated that this gene encodes a protein important for xanthine utilization because these knock-out strains fail to convert xanthine to uric acid when xanthine dehydrogenase activity is also deleted or inhibited (15, 16) and when these fungi are grown on xanthine as a sole source of nitrogen. No alternative purines effectively substitute for xanthine as a substrate for this enzyme reaction, suggesting that the enzyme is highly substrate-specific (17). Xanthine is present in plant and animal cells and is a product of purine degradation. Interestingly this represents an alternative pathway for xanthine breakdown to that commonly found in other taxa, where xanthine is broken down by a pathway composed of unrelated protein families containing the molybdopterin cofactor Moco (15). The predicted function and taxon distribution of this HGT candidate family suggests that the enzyme may represent an important adaptation for nitrogen scavenging in fungal and oomycete osmotrophs.

N

5 (S1.5)

EEY56552




Our annotation suggests this HGT candidate encodes a dehydrogenase/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family protein. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. This is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR) (1). Phylogenetic analysis of other alcohol dehydrogenase-encoding genes has demonstrated multiple HGT events, suggesting that other alcohol dehydrogenase enzymes have replaceable functional roles and have undergone numerous replacements by HGT (18, 19).

N

6 (S1.6)

72257

(P.ramorum)






Annotation suggests this HGT candidate protein has strong similarity to the extracellular quercetin 2,3-dioxygenase (EC 1.13.11.24) identified from filamentous ascomycetes (e.g. (20, 21)). Quercetin 2,3-dioxygenase is a type 2 copper-dependent enzyme, which is able to disrupt the O-heteroaromatic ring of flavonols, yielding the corresponding depside (phenolic carboxylic acid ester – i.e. 2-protocatechuoyl-phlorogucinol carboxylic acid) and carbon monoxide (22). Quercetin is a naturally occurring flavonoid compound found in most plant tissues and also a product of rutin breakdown. Quercetin 2,3-dioxygenase is produced by various filamentous fungi when grown on the complex aromatic compound rutin as sole carbon and energy source (20, 21, 23) suggesting this enzyme is part of an important pathway for breakdown of plant tissues.

Y

7 (S1.7)

EEY52979




Annotation by similarity search (1-3) suggests this HGT candidate encodes an extracellular α-L-rhamnosidase (EC 3.2.1.40 – glycosyl hydrolase family 78 (24)). This putative enzyme catalyses the hydrolysis of terminal non-reducing α-L-rhamnose i.e. hydrolyzing α-1,2 and α-1,6 linkages (25, 26). L-rhamnose is an abundant monosaccharide, a common constituent of glycolipids (e.g. rhamnolipids found in some bacteria) and glycosides, such as plant pigments, pectin, gums or biosurfactants. Pectin from plant cell walls, contains rhamnogalacturonan, consisting of rhamnose and galacturonate as the main-chain and therefore this enzyme is important to many plant- associated fungi for modifying and/or degrading rhamnose-related compounds, including the plant cell wall (25, 26). Metabolic reconstruction based on the published oomycete genomes demonstrates that there is no identifiable rhamnose utilization pathway, suggesting that oomycetes do not normally metabolize rhamnose for energy. The HGT acquisition may function as a plant cell wall degrading enzyme.
Analysis of P. infestans microarray data (27) suggests that one gene from this HGT family showed up-regulation after five days infection of plant tissue (t-test; P value at <0.1 - borderline).

Y

8 (S1.8)

EEY63463




This HGT candidate family encodes a member of lactonohydrolase/gluconolactonase. Lactonohydrolases are intramolecular ester bond-hydrolyzing enzymes. Lactone compounds are cyclic compounds possessing intra-molecular ester bonds and are widely distributed in nature (28). Lactonohydrolases have been implicated in ascorbate biosynthesis and also the breakdown of dihydrocoumarin and other plant-associated aromatic lactones (20).

N

9 (S1.9)

EEY64355





Annotation suggests this HGT candidate encodes an extracellular glucooligosaccharide oxidase (EC 1.1.99.B3) which putatively catalyses carbohydrate oxidation to the corresponding lactones. A similar gluco-oligosaccharide oxidase (GOOX) from the fungus Acremonium strictum has been shown to perform oxidization of a variety of carbohydrates with the concomitant reduction of molecular oxygen to hydrogen peroxide. This enzyme was shown to use D-glucose, maltose, lactose, malto- and cello-oligosaccharides, cellobiose as substrates. Demonstrating a broad substrate specificity of GOOX, particularly toward oligosaccharides (29, 30).

Y

10 (S1.10)

EEY59160




Our annotations suggests this HGT candidate encodes an extracellular unsaturated rhamnogalacturonyl hydrolase (glycosyl hydrolase family 88 - EC:3.2.1.-). This enzyme catalyses the random hydrolysis of (1→4)-α-D-galactosiduronic linkages in pectate and other galacturonans e.g. hydrolysis of unsaturated rhamnogalacturonan disaccharide to yield unsaturated D-galacturonic acid and L-rhamnose. Potentially an important component of pectin and plant cell wall degradation. Metabolic reconstruction based on the three Phytophthora genome projects demonstrates that a standard galactouronide utilisation pathway was absent. Further searches identified a partial alternative (fungal) galactouronide metabolic pathway, a four enzyme pathway found in some fungi utilized to break down plant cell walls (31, 32),
Analysis of P. infestans microarray data (27) suggests that one gene from this HGT family showed up -regulation after five days infection of plant tissue (t-test, P value at <0.1 - borderline).

Y

11 (S1.11)

83543

(P.ramorum)






Annotation by similarity search (1-3) suggests this HGT encodes a putative transcription factor (pfam04299). In Bacillus subtilis, family member PAI 2/ORF-2 was found to be essential for growth encoding a novel transcriptional-regulator involved in glucose repression (33).

N

12 (S1.12)

85044

(P.ramorum)






Our annotations suggests this HGT candidate is a member of a large protein family including: 1) 3-octaprenyl-4-hydroxybenzoate carboxy-lyase which catalyzes the third step in the biosynthesis of ubiquinone, and 2) Phenylphosphate carboxylase, a carbon-carbon lyase which eliminates or adds carboxy-groups to phenols (34). Metabolic modeling in the three Phytophthora genomes suggests that ubiquinone pathway is performed by the alternative eukaryotic synthesis pathways – suggesting this prokaryote-like UbiD protein seems to be redundant in relation to ‘prokaryote’ ubiquinone synthesis as the other pathway enzyme steps are missing. The enzyme may participate in production of precursors and scavenging intermediates for ubiquinone synthesis and may therefore be involved in degradation of phenylpropanoids (lignino-stilbene) which are bi-products of lignin and suberin breakdown from plant cell walls.

N

13 (S1.13)

EEY53137




Annotation by similarity search (1-3) suggests this HGT candidate encodes a phosphatidylinositol transfer protein, involved in transport of phospholipids from their site of synthesis in the endoplasmic reticulum and Golgi to other cell membranes (35).

N

14 (S1.14)

133521

(P. sojae)






Annotation suggests this HGT candidate encodes an extracellular hypothetical protein with sequence similarity to prokaryote secretory lipases. It is difficult to predict the function of this protein, as the esterase/lipase family is a highly complex gene family. Interestingly, many oomycetes depend on extracellular sources of sterol and fatty acids, and the supply of these metabolites plays a role in determining the transition of oomycetes through different lifecycle stages (8, 9). Although these putative extracellular enzymes may have a number of roles in releasing long chain fatty acids and terpenoids from a range of substrates (e.g. carotenoids, suberin, cutin).
This is one of four separate transfers of esterase/lipase domain containing extracellular proteins. It is difficult to predict the function of these proteins but extracellular lipases have been shown to be important pathogenic phenotypes involved in the detection and breakdown of plant waxy cuticle (10-12), which may represent an important metabolic resource for sterol and long chain fatty acids for oomycete plant pathogens.

Y

15 (S1.15)

142730

(P.sojae)






Our annotations suggests this HGT candidate encodes a conserved hypothetical protein with sequence similarity to the esterase/lipase protein domain family. A putative gene family that may play roles in releasing long chain fatty acids and terpenoids from a range of plant derived substrates (e.g. carotenoids, suberin, cutin).
One of four separate transfers of esterase/lipase domain containing proteins

N

16 (S1.16)

EEY68514




Annotation suggests this HGT encodes a xylitol dehydrogenase / sorbitol dehydrogenase (EC 1.1.1.9/ EC 1.1.1.14). This gene family includes broad-spectrum reversible oxidoreductases of sugar alcohols e.g. sorbitol to fructose, with NAD reduction (36, 37). Interestingly in fungi, sugar alcohols, such as mannitol, arabitol, and glycerol, accumulate and have a number of different cellular functions. These include maintaining osmotic balance, generating turgor in appressoria, and quenching reactive oxygen species (38). Sugar alcohols may form in plant-pathogenic fungi when -fructosidases convert plant-derived sucrose to fructose, which is converted to sorbitol by sorbitol dehydrogenase. It is unclear what function this enzyme plays in Phytophthora because oomycetes are thought not to accumulate sugar alcohols, such as sorbitol (39), and therefore a number of alternative roles are suggested (38). Oomycete gene expression patterns and enzyme activity have been shown to be associated with sporulation. Furthermore, the enzyme displayed similar activities when sorbitol, xylitol, sorbitol, or glycerol was used as a substrate (38) suggesting that this HGT represents a useful enzyme for reconfiguring a range of sugars which can then ultimately be fed into glycolysis.

N

17 (S1.17)

EEY55544




Annotation suggests that this HGT candidate encodes an extracellular arabinan-endo-1,5-α-L-arabinosidase (glycosyl hydrolases family 43), which catalyses endohydrolysis of (1→5)-α-arabinofuranosidic linkages. Arabinans are found in hemicellulose and consist of a backbone of -1,5-linked L-arabinofuranosyl residues, some of which are substituted with -1,2- and -1,3-linked side chains. This enzyme catalyses breakdown of the arabinan backbone (40, 41) and therefore is a critical acquisition for digestion of plant cell wall because it acts synergistically with a number of other plant cell wall degrading enzymes.
Metabolic reconstruction based on the oomycete genomes demonstrates that no identifiable arabinose utilization pathway suggesting the oomycetes analysed here do not metabolise arabinose for energy and classical culture-based studies have demonstrated that arabinose is a poor sugar source for Phytophthora species (39). We therefore hypothesise that this HGT acquisition functions as a secreted enzyme for the breakdown of plant cell walls.

Y

18 (S1.18)

EEY59913

Yes (named CodB)

Our annotations suggests this HGT encodes a transporter protein. This family consists of bacterial and fungal transporters for purines and pyrimidines. In filamentous fungi, apart from their direct use in nucleic acid or nucleotide biosynthesis, purines can also be used (through their oxidation to ureides and eventually to urea and ammonium) as nitrogen sources. The expression of fungal genes encoding purine-specific transporters or enzymes involved in purine catabolism is usually induced by purines and repressed when a primary nitrogen source, such as ammonium or glutamine, is available (42, 43). This result is intriguing because Phytophthora metabolic network analysis demonstrated that all three oomycetes have retained a functional purine and pyrimidine biosynthesis pathway, suggesting that these parasitic oomycetes do not need to acquire nucleobases from the environment. This suggests that the transporter has additional transport functions or is used to acquire purines from plant breakdown to provide nitrogen.
Interestingly, BLASTp (ref_seq database) suggest that this transporter also has homology to a pyridoxine transport protein in Saccharomycotina yeast species. Metabolic network analysis demonstrated that the Phytophthora species analysed lack pyridoxal 5'-phosphate synthase (EC 1.4.3.5), an integral step in the synthesis of sterols, suggesting that this sub-set of the oomycetes are sterol auxotrophs, consistent with previous reports which argue that oomycetes belonging to the peronosporales, such as Phytophthora sp. cannot synthesise their own sterols (44). Fungi in anaerobic conditions or when the function of pyridoxal 5'-phosphate synthase (EC 1.4.3.5) has been perturbed, also become sterol auxotrophs and must obtain sterols from the environment using a transportation mechanism (45). This HGT derived oomycete gene has a 3e-61 BLAST similarity score to the vitamin B6 pyridoxal phosphate transporter of Saccharomyces cerevisiae (46). These observations lead us to suggest (tentatively) that this transporter may also be used to scavenge Pyridoxine (pyridoxal or pyridoxamine) in order to obtain vitamin precursors and sterols in addition to transporting nucleobases as a source of nitrogen.

N

19 (S1.19)

141189

(P. sojae)






Annotation by similarity search (1-3) suggests this HGT candidate encodes an extracellular protein with an esterase/lipase domain. The functional role of esterases and lipase enzymes is difficult to decipher based on homology searches because substrate specificity often depends upon small changes in the amino acid sequences and these enzyme families have relatively few functional studies compared to the complexity of the protein families (5, 6). The amino acid sequence has strong sequence similarity to carotenoid ester lipase enzymes of the fungus Pleurotus sapidus which have been shown to perform efficient hydrolysis of xanthophyll esters (7) and therefore important for processing xanthophyll metabolites found in plant tissues.
This is one of four separate transfers of esterase/lipase domain containing extracellular proteins. It is difficult to predict the function of these proteins but extracellular lipases have been shown to be important pathogenic phenotypes involved in the detection and breakdown of plant waxy cuticle (10-12) which may represent an important metabolic resource for sterol and long chain fatty acids for oomycete plant pathogens.

Y

20 (1.20)

EEY58144




Annotation suggests this HGT candidate encodes an extracellular protein that is a member of the NPP1 like necrosis inducing protein also known as necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLPs). This protein family is found exclusively in oomycetes, fungi and some bacteria. Infiltration of NPP1 into leaves of Arabidopsis thaliana plants results in transcript accumulation of pathogenesis-related genes, production of ROS and ethylene, callose apposition, and hypersentative response (localized cell death in plant cells to evade invasion) (47). Furthermore, NLPs trigger leaf necrosis that is genetically distinct from immunity-associated programmed cell death and stimulate immunity-associated defenses. Hence, NLPs were proposed to have dual functions in plant pathogen interactions, acting both as triggers of immunity responses and as toxin-like virulence factors (47). NLP protein analyses revealed that identical structural properties were required to cause plasma membrane permeabilization and cytolysis in plant cells, as well as to restore bacterial virulence (48). Interestingly, this protein family demonstrates a large expansion in oomycetes genomes by gene duplication compared to fungi from where the gene family originated.
Analysis of P. infestans microarray data (27) demonstrated that one gene from this HGT family showed significant up-regulation after five days infection of plant tissue (t-test; P value at <0.01).

Y

21 (1.21)

EEY64154




Annotation suggests this putative HGT candidate encodes a conserved hypothetical protein with weak sequence similarity to a prokaryotic antibiotic biosynthesis monooxygenase. Analysis of P. infestans microarray data (27) demonstrated that one gene from this HGT family showed significant up regulation after five days infection of plant tissue (t-test; P value at <0.01).

Y

22 (1.22)

EEY62062




Annotation by similarity search (1-3) suggests this HGT is a putative pectate lyase (EC 4.2.2.2). Pectate lyase is known plant virulence factor (49) and is an enzyme involved in the maceration and soft rotting of plant tissue. It functions by cleavage of (1->4)-α-D-galacturonan polysaccharides to give oligosaccharides with 4-deoxy-α-D-galact-4-enuronosyl groups at their non-reducing ends (50). Pectin is a major structural component of the plant cell wall and abundant source of sugars in terrestrial environments.
Analysis of P. infestans microarray data (27) demonstrated that one gene from this HGT family showed significant up regulation after five days infection of plant tissue (t-test; P value at <0.05).

Y

23 (1.23)

EEY67135

Yes (named PcaH)

This HGT candidate putatively encodes an extracellular intradiol dioxygenase. These enzymes catalyze the critical ring-cleavage step in conversion of catecholate derivatives (breaking the catechol C1-C2 bond – ring cleavage) to citric acid cycle intermediates. The family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases (EC 1.13.1.3) and are predicted to be important in breakdown of aromatic compounds including lignin (51). Lignin is an important structural molecule reinforcing plant tissues, is the second most abundant biopolymer in nature and is a significant source of aromatic groups in natural environments.

Y

24 (1.24)

ABB22031




Annotation by similarity search (1-3) suggests this HGT candidate encodes an extracellular member of endoglucanase family classified as glycosyl hydrolase family 12, formerly known as cellulase family H (24) and responsible for endohydrolysis of (1→4)-β-D-glucosidic linkages in cellulose, lichenin and cereal β-D-glucans. It has been shown to be an important enzyme in breakdown and remodeling of the plant cell wall (52).

Y

25 (1.25)

EEY67552




Annotation by similarity search (1-3) suggests this HGT candidate encodes an extracellular protein containing a histidine phosphatase domain found in phytase proteins. The GenBank sequences with the highest sequence similarity and which has been investigated with functional experiments is the phytase B family of ascomycetes. Phytase (inositol hexakisphosphate phosphohydrolase – E.C. 3.1.3.8) is capable of hydrolyzing phytic acid (myo-inositol hexakisphosphate) as well as other organophosphate substrates (53). Phytic acid (myo-inositol 1,2,3,4,5,6-hexakis dihydrogen phosphate) is the primary storage form of phosphate and inositol in plants and constitutes 3–5% of the dry weight of seeds in cereal grains and legumes (54). Phytases catalyze phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (55, 56).
Analysis of P. infestans microarray data (27) demonstrated that one gene from this HGT family showed significant up regulation after five days infection of plant tissue (t-test; P value at <0.05).

Y

26 (1.26)

EEY65395




This putative HGT candidate encodes an extracellular endo-1,4--xylanase of the glycosyl hydrolase family 10, formerly known as cellulase family F (24). The enzyme is an endo--1, 4-xylanase (EC 3.2.1.8), which catalyzes the endohydrolysis of 1,4--D-xylosidic linkages in xylan to short xylo-oligosaccharides of varying length (24, 57) from starch and hemicellulose. Hemicellulose is the second most abundant natural polysaccharide after cellulose and is also an integral structural component of the plant cell wall. Hemicellulose is made up of a number of different monomers with xylan as the majority sugar. Extracellular endo-1,4--xylanases have been shown to be efficient degraders of plant derived xylan (58) suggesting that this enzyme family is important breakdown of plant tissues.

Y

27 (1.27)

75147

(P.ramorum)






Our annotation suggests this HGT encodes a member of Zinc metalloprotease proteins which include archaemetzincin, a family of metalloproteases characterized by a conserved motif (HEXXHXXGX3CX4CXMX17CXXC) that contains an archetypal zinc-binding site and four Cys residues. Enzymatic assays performed with human recombinant AMZs have demonstrated evidence that these proteins are catalytically active metalloproteases that exhibit substrate specificity and sensitivity to inhibitors and act predominantly as aminopeptidases (59). Previous phylogenetic analysis, which did not include gene sampling from the oomycetes, suggests that HGT has played a role in the evolution of this gene family (59).

N

28 (1.28)

EEY56384




Annotation by similarity search (1-3) suggests this HGT candidate encodes an extracellular arabinogalactan endo-1,4-β-galactosidase (glycosyl hydrolase family 53, GalA, - EC:3.2.1.89). Enzymes from this protein family encode endohydrolysis of (1→4)-β-D-galactosidic linkages in arabinogalactans a polymer of arabinose and galactose monosaccharides. Two classes of arabinogalactans are found in nature: plant arabinogalactan and microbial arabinogalactan. Pectin consists of “smooth” regions of α-1,4-linked galacturonic acid and “hairy” regions of rhamnogalacturonan. Endo-1,4--galactosidase hydrolyze the galactan side chains that are part of “hairy” region of pectin (60, 61). Members of protein family has been linked to fungal pathogenesis of plants (e.g. (61)).

Y

29 (1.29)

77558

(P.ramorum)






This HGT putatively encodes an aliphatic nitrilase (CN hydrolase family - EC 3.5.5.1). Nitrilases belong to a subfamily of the carbon-nitrogen hydrolase enzyme superfamily and catalyze the conversion of nitriles to the corresponding carboxylic acids and ammonia, and are represents a highly diverse protein family with many distinct sub-families discovered from uncultured microbes (62). Within the protein family and with strong sequence similarity to the oomycete HGT genes, are the cyanide hydratases. These enzymes are encoded by many plant pathogenic fungi and the acquisition of this gene family would theoretically allow oomycetes to infect plants that synthesize large amounts of defensive alkenyl glucosinates, which break down into isothiocyanates and nitriles. Isothiocyanates and nitriles, including hydrogen cyanide, are often present in plant tissues and are toxic to fungi (63). In the ascomycete plant pathogenic fungus Leptosphaeria maculans this enzyme catalyses the breakdown of hydrogen cyanide to a less toxic compound, formamide which can be used as a nitrogen source.

N

30 (1.30)

EEY68947




Annotation by similarity search (1-3) suggests this HGT candidate encodes an extracellular α-L-rhamnosidase (EC 3.2.1.40 – glycosyl hydrolase 78 (24)). This putative enzyme catalyses hydrolysis of terminal non-reducing α-L-rhamnose i.e. hydrolyzing α-1,2 and α-1,6 linkages (25, 26). L-Rhamnose is an abundant monosaccharide, a common constituent of glycolipids and glycosides, such as plant pigments, pectin, gums or biosurfactants. Pectin from plant cell walls, contains rhamnogalacturonan, consisting of rhamnose and galacturonate as the main-chain and therefore this enzyme is important to many plant associated fungi for modifying and/or degrading rhamnose-related compounds including the plant cell wall (25, 26). This represents a separate extracellular α-L-rhamnosidase transfer to HGT number 7 discussed above.

Y

31

76863

(P.ramorum)






Annotation suggests this HGT encodes an extracellular protein containing sequence similarity to LysM domains. LysM domains are found in a variety of enzymes involved in bacterial cell wall degradation and may have a general peptidoglycan binding function (64). Recently, the first characterization of an interaction of a LysM domain with its ligand was published and demonstrated these protein domains binding of oligomers of N-acetylglucosamine a monosaccharide derivative of glucose that is a building block for bacterial peptidoglycan and fungal chitin (65). During Colletotrichum lindemuthianum infection on bean, members of this protein family have been shown to accumulate in the walls of intracellular hyphae and the interfacial matrix, which separates the hyphae from the invaginated host plasma membrane (66). While in Cladosporium fulvum, the causal agent of leaf mold of tomato, this gene family has an expression pattern consistent with other secreted C. fulvum effector proteins while RNAi knockdown experiments demonstrate significant reduction in growth of the fungus on host plants (67). LysM proteins are implicated in evasion of chitin triggered plant immunity by fungal pathogens (68). The data suggest that this HGT may act as an effector.

Y

32

EEY55495




Our annotations suggest that this HGT is an extracellular conserved hypothetical protein.

Y

33

134308

(P.sojae)






Annotation by similarity search (1-3) suggests this HGT has strong similarity to a fungal transcription factor NmrA. NmrA is a negative transcriptional regulator involved in the post-translational modification controlling nitrogen metabolite repression in fungi (69). Nmr1 is implicated in fungal pathogenicity by its interaction with fungal Tps1 in Magnaporthe oryzae (70).

N

34

EEY58177




Annotation by similarity search (1-3) suggests this HGT encodes a conserved hypothetical protein with sequence similarity to Melampsora laricis-populin and Puccinia graminis encoded proteins.

Y

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10. Feng J, et al. (2009) Analysis of a Blumeria graminis-secreted lipase reveals the importance of host epicuticular wax components for fungal adhesion and development. Mol Plant Microbe Interact 22(12):1601-1610.

11. Voigt CA, Schafer W, & Salomon S (2005) A secreted lipase of Fusarium graminearum is a virulence factor required for infection of cereals. Plant J 42(3):364-375.

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