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