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GPD_CANTR
ID   GPD_CANTR               Reviewed;         391 AA.
AC   Q4PNS1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)];
DE            EC=1.1.1.8;
GN   Name=GPD;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   He F., Chen Y.;
RT   "Isolation of the glycerol-3-phosphate dehydrogenase gene from Candida
RT   tropicalis and its application to gene expression in Saccharomyces
RT   cerevisiae.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.8;
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; DQ064595; AAY63996.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4PNS1; -.
DR   SMR; Q4PNS1; -.
DR   VEuPathDB; FungiDB:CTMYA2_011940; -.
DR   VEuPathDB; FungiDB:CTRG_02011; -.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..391
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]"
FT                   /id="PRO_0000138088"
FT   ACT_SITE        250
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         46..51
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         315..316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         315
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         344
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
SQ   SEQUENCE   391 AA;  42536 MW;  B409DA55F000945D CRC64;
     MCTSANNRLD QLTQILHPEN LLNPTNASHP ESSLRPDHPF KIAVVGSGNW GTTIAKIVSE
     NAVARPHLFS HFVNMWVFEE KIDGTNLTEI INTRHENIKY LPGVKLPKNL IAVPDIVKAV
     KGADLIVFNL PHQFLPRILK QLKGHVPKTT RAISCLKGLE VNANGCKLLS TVIEEELGIA
     CGALSGANLA PEIARGNWSE TTVAYRVPAD YRGPGKDIDK LVLKALFHRP YFHVNVIDDV
     AGVSIAGALK NVVALAVGFV EGLGWGDNAK AAVMRVGLLE TIKFAKLFFN DAEIDTFTGE
     SAGVADLITT CSGGRNVKVG RYMAETGCAA EEAEKKLLNG QSSQGIVTTK EVHEFLTNVN
     KLEEFPLFEA TYQITFGSES IENLPNLLNN Y
 
 
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