(data stored in ACNUC7421 zone)

SWISSPROT: GPDA_AERHH

ID   GPDA_AERHH              Reviewed;         334 AA.
AC   A0KF08;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394};
DE            EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394};
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394};
GN   Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394};
GN   OrderedLocusNames=AHA_0296;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.94;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + H(+) + NADPH; Xref=Rhea:RHEA:11096,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.94;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00394};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism. {ECO:0000255|HAMAP-Rule:MF_00394}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}.
DR   EMBL; CP000462; ABK36018.1; -; Genomic_DNA.
DR   RefSeq; WP_011704301.1; NC_008570.1.
DR   RefSeq; YP_854826.1; NC_008570.1.
DR   SMR; A0KF08; -.
DR   STRING; 380703.AHA_0296; -.
DR   EnsemblBacteria; ABK36018; ABK36018; AHA_0296.
DR   GeneID; 4490454; -.
DR   KEGG; aha:AHA_0296; -.
DR   PATRIC; fig|380703.7.peg.284; -.
DR   eggNOG; ENOG4105CSF; Bacteria.
DR   eggNOG; COG0240; LUCA.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; WLCKGFE; -.
DR   BioCyc; AHYD380703:G1G7B-297-MONOMER; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 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; 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   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KF08.
DR   SWISS-2DPAGE; A0KF08.
KW   Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW   NAD; Oxidoreductase; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome.
FT   CHAIN         1    334       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_1000049479.
FT   NP_BIND      11     16       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   REGION      258    259       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   ACT_SITE    194    194       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     109    109       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     109    109       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     142    142       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     258    258       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     284    284       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   334 AA;  35341 MW;  15A503C9F6BF750A CRC64;
     MADQIAISVL GAGSYGSALA ISLARNGHPT LLWGHDPAHV AELEQDRCNK AFLPDVPFPA
     DLQLTADLQQ AVQAAPVLLL VVPSHVFGQV LAQVKPFLRP DTRIAWATKG LEPDSGRLLQ
     DVAREVLGDE MPLAVISGPT FAKELAAGLP TAISVASTHD DFADDLSLLL HCGRSFRVYT
     NPDFIGLQLG GAVKNVIAIG AGLSDGLGFG ANARTALITR GLVEMQRLGA ALGADAKTFM
     GMAGLGDLVL TCTDNQSRNR RFGLALGAGK DVNTAMAEIG QVVEGYRNTK EVHLLAARCG
     VEMPICEQIF KVLYEGKNPK EAAIALLSRD KKDE
//

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