CAZyme Information: TPX50376.1

Basic Information

• Species: Synchytrium endobioticum
• Lineage: Chytridiomycota; Chytridiomycetes; ; Synchytriaceae; Synchytrium; Synchytrium endobioticum
• CAZyme ID: TPX50376.1
• CAZy Family: GT2
• CAZyme Description: glucan endo-1,3-beta-D-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578		64467.23	7.9669

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SendobioticumMB42	8031	N/A	0	8031

Full Sequence      

MECFGRTHVTRYTNSDNWNFEMSRNQNPKAALVLEILVMSKHGAPKDMIKIAVFGGTQGV
GKHVVIKALECHHFVTVLARSPKKLADVVVNRHKLKIIQGDILHDPAAVDQVVDGQDVVI
VSLGTTGVKKGPQAKVCSFGQKVINDAMKARGVKRLIVVTSIGVGDSIKHVSYSAYFFIK
FVIYKAIADKEVQEDLVKSSGLDWTILRPTGLLDQPPRSLRYDYGEDLNGSSIARAHVAE
ICLEVIPKPHYGRIYALTLLHTLHFRHGQDMYAHCISLILLLICCSQVKPDLYGINYSPR
RSLFACPTHAMITSDLQLLRNMTTRIKTFSLIDSGSGQASATCNFGETILKAAVPLGFRV
TLGMEFRGADIDAMFQREVRELERLSYAYPNLFTVVEAIVVGSETLYRGEETQQTLSQRV
TTVRTILHSKNLRVPITAADIPPPFYGDILIAAVDFIMINVYPYWEGHAVASAPYSQMAA
VHALRERTSKNVVLGECGWPTAGSTNTDAEASIQNLEWYYKQWVCTARKNGVEYFLFEAF
DEDWKSDEHAGVEKHWGLFDLNRQPKSTVFLNPVDCSP

Enzyme Prediction     

EC	3.2.1.-:2	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH17	385	566	7.4e-34	0.7331189710610932

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
227625	Scw11	8.57e-53	294	563	47	305	Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism].
404360	NAD_binding_10	4.73e-47	55	249	1	183	NAD(P)H-binding.
187555	BVR-B_like_SDR_a	7.83e-43	50	239	1	188	biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs. Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
187554	SDR_a5	4.44e-32	50	244	1	185	atypical (a) SDRs, subgroup 5. This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
366033	Glyco_hydro_17	9.21e-20	450	566	171	304	Glycosyl hydrolases family 17.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLQ77781.1|GH17	QLQ77781.1|GH17	2.39e-29	281	572	10	307
CCD23099.1|GH17	CCD23099.1|GH17	2.60e-29	281	569	13	307
ABP48761.2|GH17	ABP48761.2|GH17	8.87e-29	306	559	39	297
CCE61637.1|GH17	CCE61637.1|GH17	8.87e-29	306	559	39	297
QLL30211.1|GH17	QLL30211.1|GH17	1.56e-28	281	569	10	304

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4WTP_A	4WTP_A	4.23e-33	293	569	38	294	Crystal structure of glycoside hydrolase family 17 beta-1,3-glucanosyltransferase from Rhizomucor miehei [Rhizomucor miehei CAU432]
4WTR_A	4WTR_A	2.81e-32	293	569	38	294	Active-site mutant of Rhizomucor miehei beta-1,3-glucanosyltransferase in complex with laminaribiose [Rhizomucor miehei CAU432],4WTS_A Active-site mutant of Rhizomucor miehei beta-1,3-glucanosyltransferase in complex with laminaritriose [Rhizomucor miehei CAU432]
3QVO_A	3QVO_A	3.19e-10	51	249	26	211	Structure of a Rossmann-fold NAD(P)-binding family protein from Shigella flexneri. [Shigella flexneri 2a str. 2457T]
4JGB_A	4JGB_A	7.61e-10	45	225	2	172	Crystal Structure of Putative exported protein from Burkholderia pseudomallei [Burkholderia pseudomallei K96243],4JGB_B Crystal Structure of Putative exported protein from Burkholderia pseudomallei [Burkholderia pseudomallei K96243]
5FFQ_A	5FFQ_A	9.39e-07	143	214	89	155	ChuY: An Anaerobillin Reductase from Escherichia coli O157:H7 [Escherichia coli O157:H7],5FFQ_B ChuY: An Anaerobillin Reductase from Escherichia coli O157:H7 [Escherichia coli O157:H7]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B2W4|BGL2_ARTBC	sp|D4B2W4|BGL2_ARTBC	9.59e-32	272	566	3	296	Glucan 1,3-beta-glucosidase ARB_02797 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02797 PE=1 SV=1
sp|O13990|BGL2_SCHPO	sp|O13990|BGL2_SCHPO	5.76e-28	314	566	63	313	Glucan 1,3-beta-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=bgl2 PE=2 SV=4
sp|P15703|BGL2_YEAST	sp|P15703|BGL2_YEAST	1.25e-27	306	559	40	298	Glucan 1,3-beta-glucosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=BGL2 PE=1 SV=1
sp|P43070|BGL2_CANAX	sp|P43070|BGL2_CANAX	1.15e-23	306	569	35	303	Glucan 1,3-beta-glucosidase OS=Candida albicans OX=5476 GN=BGL2 PE=3 SV=1
sp|Q5AMT2|BGL2_CANAL	sp|Q5AMT2|BGL2_CANAL	1.56e-23	306	569	35	303	Glucan 1,3-beta-glucosidase BGL2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=BGL2 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000079	0.000000

TMHMM  Annotations     

There is no transmembrane helices in TPX50376.1.