CAZyme Information: CC1G_15736-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_15736-t26_1-p1
• CAZy Family: PL42
• CAZyme Description: NAD-dependent epimerase/dehydratase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
959	AACS02000011|CGC2	106949.93	7.2508

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinereaokay7-130	13657	240176	301	13356

• Gene Location: location=AACS02000011:1592971-1596046(-)

Full Sequence      

MVSLLGSHFAKRLISSGEYRVRIIDQSPKPTFPEGDLCHELIIGNLCDPSTCRSAVDGVS
IVCHFAANMGGMGTIHEANEFRIYAENHFMTLHLLQAAIEAGVKRFLYASTACVYPLHLQ
QSVEPATPLSLSEDDVYRDATSESPPCPQGLYGLEKLSTELLLHQASSKVSVRIARLHNV
YGPGGTWNSGREKAPAAMLRKALALKRLGAGSSHSFEIWGDGQQQRSFLYIDDAVDTLLK
LLASDYSSPLNIGSDTSVSILRLSKLALRVARADSGRVSFSFDTTKPVGVASRNSNNERV
SRVLGWRPSTSLDVGMAKTCAWMEKEMERLLSQRESGLARETLLLQCLSSKVVDLKEEAT
VFAILLPITSRGGTSPQSCLSNLGKFAQSLSDTTWRDLHSLGGKRYRVAIYLAIDHDDEF
LLADQGPNKAEALLRSHGFSDVTSLICDYPRGHVCSLWRDCAARAFDDCCDYYGLFGDDV
SILDEGWMRKMDESSTESPSTKVSLLLYRRWNASRMVDLRLSNSIGGSDDARYAKQRARD
WTFDTLTNAVSSVDSHIRSFNPSISPTLTLDVVIPCYRVDLAIISNILALQHSPTLTIMF
IIIVDNPSSPQILKLETLYGRRPDVRIRVNSVNLGASASRNRGMSESSAEWVYFLDDDIV
PDADLLFEAEKVIREHPDAAGFVGNTVFPKSETIFQAAVHLAGVTYFWDIATKIEDDVPW
GVTANLIARRNIKDGIEYDLRYPKTGGGEDIDFCRLKREVSIKRGGSGFGAAPLVRVTHP
YWNNGKRSYWRFYMWAYGDGMLVARFPELTYRDYAPNSAEYLLLAIALPFIVLPLGDNLL
SSLYLTAYLIAKGLSSVVLANVLHDIYRHLWQHPERDAGLNSSIKSGPRFWLALVESSFI
RMSSELGRLKGAVDRKQWYCIGKRFDWFAGREGDGPKREERWNNVQRLVCIVLIFRFVL

Enzyme Prediction     

No EC number prediction in CC1G_15736-t26_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187581	GME-like_SDR_e	3.22e-87	3	329	10	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.
178298	PLN02695	4.76e-79	5	329	33	335	GDP-D-mannose-3',5'-epimerase
223528	WcaG	8.21e-43	5	329	12	314	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].
187566	UDP_AE_SDR_e	3.38e-36	6	323	12	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.
187574	UDP_G4E_5_SDR_e	2.32e-35	5	322	11	299	UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs. This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. 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	2.19e-316	5	954	28	1011
QRW04585.1|GT2	7.76e-310	4	953	28	1014
QRV75675.1|GT2	5.46e-309	5	953	28	1010
QRW23776.1|GT2|GT8	8.75e-236	5	910	23	925
UFH56504.1|GT2	2.56e-34	569	957	25	384

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C59_A	3.86e-56	5	329	41	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	9.87e-56	5	329	41	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	1.35e-55	5	329	41	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	2.53e-55	5	329	41	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]
6WJB_A	7.41e-17	5	318	15	305	UDP-GlcNAc C4-epimerase from Pseudomonas protegens in complex with NAD and UDP-GlcNAc [Pseudomonas protegens Pf-5],6WJB_B UDP-GlcNAc C4-epimerase from Pseudomonas protegens in complex with NAD and UDP-GlcNAc [Pseudomonas protegens Pf-5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A3C4S4|GME1_ORYSJ	1.26e-57	5	333	41	347	GDP-mannose 3,5-epimerase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=GME-1 PE=1 SV=1
sp|Q2R1V8|GME2_ORYSJ	2.69e-57	5	329	34	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	8.35e-57	5	333	41	347	GDP-mannose 3,5-epimerase 1 OS=Oryza sativa subsp. indica OX=39946 GN=OsI_032456 PE=2 SV=1
sp|Q93VR3|GME_ARATH	1.88e-55	5	329	39	342	GDP-mannose 3,5-epimerase OS=Arabidopsis thaliana OX=3702 GN=At5g28840 PE=1 SV=1
sp|Q5SFA6|CHMD_STRBI	2.11e-19	2	322	17	320	dTDP-4-dehydro-6-deoxy-D-allose reductase OS=Streptomyces bikiniensis OX=1896 GN=chmD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000067	0.000000

TMHMM  Annotations     

There is no transmembrane helices in CC1G_15736-t26_1-p1.