(data stored in ACNUC7421 zone)

SWISSPROT: GPDA_ANADE

ID   GPDA_ANADE              Reviewed;         332 AA.
AC   Q2IMY8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 90.
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=Adeh_0396;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC80172.1; -; Genomic_DNA.
DR   RefSeq; WP_011419455.1; NC_007760.1.
DR   SMR; Q2IMY8; -.
DR   STRING; 290397.Adeh_0396; -.
DR   EnsemblBacteria; ABC80172; ABC80172; Adeh_0396.
DR   KEGG; ade:Adeh_0396; -.
DR   eggNOG; ENOG4105CSF; Bacteria.
DR   eggNOG; COG0240; LUCA.
DR   HOGENOM; HOG000246853; -.
DR   KO; K00057; -.
DR   OMA; WLCKGFE; -.
DR   BioCyc; ADEH290397:G1G5W-406-MONOMER; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001935; 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.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMY8.
DR   SWISS-2DPAGE; Q2IMY8.
KW   Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW   NAD; Oxidoreductase; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome.
FT   CHAIN         1    332       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_0000255277.
FT   NP_BIND       7     12       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   REGION      255    256       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   ACT_SITE    191    191       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     105    105       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     105    105       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     140    140       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     255    255       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     281    281       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   332 AA;  35016 MW;  4B713C7CF0A73824 CRC64;
     MRATVLGAGS WGTALASLLA GKGYTVTSWD KDAAVLDDIA RNHRNERYLP GLHLPPTLHA
     SAEVAKALEG AELVVLAVPS HAVRPVVIEA KRHVHAGTPI VCVAKGIELD TLMTMTEVVE
     DVLPVPLHPY LAVLSGPSFA KEVAKGLPTA VTVAARWERI AKQVQDAFHT KTFRPYTSGD
     VVGCEIGGCV KNVVAIAAGI SDGMGFGANA MAALVTRGLA EITRLAVRKG ANPLTLSGLA
     GLGDLVLTCS SDLSRNRTVG RGLAEGKTAD AIQRELGQVA EGVRNARSAR ELAKRLGVEM
     PITEAIYRVL YEGLAPREAV TALMMRETKP EL
//

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