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Database: UniProt
Entry: Q476J3
LinkDB: Q476J3
Original site: Q476J3 
ID   GPDA_CUPPJ              Reviewed;         347 AA.
AC   Q476J3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   14-MAY-2014, entry version 70.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+];
DE            EC=1.1.1.94;
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
GN   Name=gpsA; OrderedLocusNames=Reut_A0308;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia
OS   eutropha (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) =
CC       glycerone phosphate + NAD(P)H.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; CP000090; AAZ59690.1; -; Genomic_DNA.
DR   RefSeq; YP_294534.1; NC_007347.1.
DR   ProteinModelPortal; Q476J3; -.
DR   STRING; 264198.Reut_A0308; -.
DR   EnsemblBacteria; AAZ59690; AAZ59690; Reut_A0308.
DR   GeneID; 3609853; -.
DR   KEGG; reu:Reut_A0308; -.
DR   PATRIC; 20226057; VBIRalEut24049_0906.
DR   eggNOG; COG0240; -.
DR   HOGENOM; HOG000246853; -.
DR   KO; K00057; -.
DR   OMA; MPISTAV; -.
DR   OrthoDB; EOG6JDWF4; -.
DR   BioCyc; CPIN264198:GIW3-309-MONOMER; -.
DR   UniPathway; UPA00940; -.
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-HAMAP.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0036439; F:glycerol-3-phosphate dehydrogenase [NADP+] 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-HAMAP.
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-HAMAP.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; DH_multihelical.
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; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR11728; PTHR11728; 1.
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   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW   NAD; Oxidoreductase; Phospholipid biosynthesis;
KW   Phospholipid metabolism.
FT   CHAIN         1    347       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_0000255350.
FT   NP_BIND      16     21       NAD (By similarity).
FT   REGION      271    272       Substrate binding (By similarity).
FT   ACT_SITE    207    207       Proton acceptor (By similarity).
FT   BINDING     118    118       NAD; via amide nitrogen (By similarity).
FT   BINDING     118    118       Substrate (By similarity).
FT   BINDING     156    156       NAD; via amide nitrogen (By similarity).
FT   BINDING     271    271       NAD (By similarity).
FT   BINDING     297    297       NAD (By similarity).
SQ   SEQUENCE   347 AA;  35750 MW;  6CAF630AF8D85F01 CRC64;
     MRRSTVRAAM KLTFLGAGAW GTALASHAAA NHDVVLWGRD PAQLAAIAAT GSNEAYLPGV
     PLSPRLRVEA DFEQAVGHAA DDPDGLVVVA TPVSGLREMT RRLAGRGNGH VRMLWLCKGF
     EAGTHALPHQ MVREELDAAG RTSGFDYGVL TGPSFAREVA LGLPCALTVA GSVPTLADCA
     QAAFHHHAMR IYGSDDLTGV EVGGAVKNVL AIATGASDGL GLGLNARAAL VTRGLAEMTR
     LGLALGGRAE TFMGLAGVGD LILTATGDLS RNRKVGQQLA AGQSLDQILA SLGHVAEGVR
     CAQAVAALAE ACKIEMPITR AVCAVLFEGL SAADAVAQLL QRDARDE
//
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