CAZyme Information: AGR57_1889T0-p1

Basic Information

• Species: Phanerochaete chrysosporium
• Lineage: Basidiomycota; Agaricomycetes; ; Phanerochaetaceae; Phanerochaete; Phanerochaete chrysosporium
• CAZyme ID: AGR57_1889T0-p1
• CAZy Family: GH152
• CAZyme Description: Glycosyltransferase Family 2 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
943	PchrRP-78_SC002|CGC5	105603.86	6.6669

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PchrysosporiumRP-78	13602	273507	0	13602

• Gene Location: location=PchrRP-78_SC002:778851-781934(+)

Full Sequence      

MPPEQELVAVTGGNGFIGSHVAERLMSLGYSVRVIDLARRSLLENNPGIEVVVGDLRKRD
FAHRACRGAKYVLHFAANMGGMGTIHEDNEAIIYQDNHTMLLNVLQACKDLGVKKFLFAS
SACVYPESRQGLYGLEKLCSELVILRGAPLSLRTYIARFHNIYGPHGSWRDGREKVPAAV
LRKAIAAKVSGEQEIELWGDGTQRRSFCYIDDAVEGVLKLLASEYHGPVNIGSEEAVTIR
ELTEMAAEAVGLQDFTIRSLEGMPIGVASRNSNNTLVRRVLGWEPRISLREGLRRTGVWI
EGEMDRLLLGFEDSKREEALHALKTSVILRLRPRGTVFGILLPVTSRCTTDNFTGWAESL
RNFAQSLARTTDGETQTREFSYRIYLAVDEQDEPILANGNAAERILREEGVVDVVTLVRN
YPRGRVCSLWRDCARKAWEEGADYFVLMGDDVTLHTVGWMSTVHRAFLSMAQETGTPFGL
GCVAFKDTTFPGMPTFPVVHRTHMEIFDGRVVPDVFVNQDGDPFLFQLYRRFGCSRMVDC
EIRNAVGGSDDARYEKEPVKDWTFGTLSEATAIVETFLRDASSTRRIVRKLTIDVIVPCY
RVMLPYLDTFLGLQPSPSCSVMFIIIVDDPNSPNIAELKAKYEERLDVRIRVNKANLGAS
ASRNRGLRESAAEWVLFLDDDVTPRPDILEKLEKVIRDHPRAAGFVGNTTFPLAETVFTT
AVHLAGVTFFWNIASKMPNEEDVPWGVTANLAARRDVPDGVVYDVSFPKTGGGEDIDYCR
KKREYSVAHGGTGFVAAPEVGAVHPYWNAGRRSYWRFYMLYPEHMFLFSISWIAVPECIR
LLGFRAIVAVLVVNVLHDCYRHLWRDADRTNAIQTNVGGVRWVLAVLESSLIRIFSETGR
VVGLVERGEVGLLYGPKDDERRNSTQRLVLSGALLFLWVALTI

Enzyme Prediction     

No EC number prediction in AGR57_1889T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	594	716	2e-17	0.7176470588235294

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
178298	PLN02695	7.97e-96	2	306	17	335	GDP-D-mannose-3',5'-epimerase
187581	GME-like_SDR_e	1.40e-92	8	306	3	318	Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs. This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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.
223528	WcaG	2.36e-61	8	300	3	308	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].
187566	UDP_AE_SDR_e	5.02e-54	8	300	2	304	UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs. This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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.
187541	UGD_SDR_e	5.57e-45	8	299	3	303	UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs. UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV90438.1|GT2	7.06e-316	7	930	18	1007
QRV75675.1|GT2	5.47e-310	7	930	18	1007
QRW04585.1|GT2	1.36e-295	7	930	19	1011
QRW23776.1|GT2|GT8	1.50e-270	2	901	8	924
QXV65791.1|GT2	7.82e-25	592	847	4	259

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C59_A	6.83e-64	2	306	26	344	gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), with gdp-alpha-d-mannose and gdp-beta-l-galactose bound in the active site. [Arabidopsis thaliana],2C59_B gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), with gdp-alpha-d-mannose and gdp-beta-l-galactose bound in the active site. [Arabidopsis thaliana]
2C54_A	1.78e-63	2	306	26	344	gdp-mannose-3', 5' -epimerase (arabidopsis thaliana),k178r, with gdp-beta-l-gulose and gdp-4-keto-beta-l-gulose bound in active site. [Arabidopsis thaliana],2C54_B gdp-mannose-3', 5' -epimerase (arabidopsis thaliana),k178r, with gdp-beta-l-gulose and gdp-4-keto-beta-l-gulose bound in active site. [Arabidopsis thaliana]
2C5A_A	2.45e-63	2	306	26	344	GDP-mannose-3', 5' -epimerase (Arabidopsis thaliana),Y174F, with GDP-beta-L-galactose bound in the active site [Arabidopsis thaliana],2C5A_B GDP-mannose-3', 5' -epimerase (Arabidopsis thaliana),Y174F, with GDP-beta-L-galactose bound in the active site [Arabidopsis thaliana]
2C5E_A	4.65e-63	2	306	26	344	gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), k217a, with gdp-alpha-d-mannose bound in the active site. [Arabidopsis thaliana],2C5E_B gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), k217a, with gdp-alpha-d-mannose bound in the active site. [Arabidopsis thaliana]
3ICP_A	2.48e-28	8	304	3	310	Crystal Structure of UDP-galactose 4-epimerase [Pyrobaculum calidifontis JCM 11548],3KO8_A Crystal Structure of UDP-galactose 4-epimerase [Pyrobaculum calidifontis JCM 11548]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A3C4S4|GME1_ORYSJ	2.03e-65	2	306	26	343	GDP-mannose 3,5-epimerase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=GME-1 PE=1 SV=1
sp|Q2R1V8|GME2_ORYSJ	4.36e-65	2	306	19	336	GDP-mannose 3,5-epimerase 2 OS=Oryza sativa subsp. japonica OX=39947 GN=GME-2 PE=2 SV=2
sp|A2Z7B3|GME1_ORYSI	1.39e-64	2	306	26	343	GDP-mannose 3,5-epimerase 1 OS=Oryza sativa subsp. indica OX=39946 GN=OsI_032456 PE=2 SV=1
sp|Q93VR3|GME_ARATH	3.33e-63	2	306	24	342	GDP-mannose 3,5-epimerase OS=Arabidopsis thaliana OX=3702 GN=At5g28840 PE=1 SV=1
sp|O49213|FCL1_ARATH	1.09e-25	1	299	12	315	GDP-L-fucose synthase 1 OS=Arabidopsis thaliana OX=3702 GN=GER1 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000062	0.000000

TMHMM  Annotations     

There is no transmembrane helices in AGR57_1889T0-p1.