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Database: UniProt
Entry: Q1QUM1
LinkDB: Q1QUM1
Original site: Q1QUM1 
ID   GPDA_CHRSD              Reviewed;         356 AA.
AC   Q1QUM1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   14-MAY-2014, entry version 66.
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=Csal_2490;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) 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; CP000285; ABE59837.1; -; Genomic_DNA.
DR   RefSeq; YP_574536.1; NC_007963.1.
DR   ProteinModelPortal; Q1QUM1; -.
DR   STRING; 290398.Csal_2490; -.
DR   EnsemblBacteria; ABE59837; ABE59837; Csal_2490.
DR   GeneID; 4026628; -.
DR   KEGG; csa:Csal_2490; -.
DR   PATRIC; 21448828; VBIChrSal113723_2502.
DR   eggNOG; COG0240; -.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; IGVEMAG; -.
DR   OrthoDB; EOG6JDWF4; -.
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    356       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_0000255299.
FT   NP_BIND      12     17       NAD (By similarity).
FT   REGION      257    258       Substrate binding (By similarity).
FT   ACT_SITE    193    193       Proton acceptor (By similarity).
FT   BINDING     110    110       NAD; via amide nitrogen (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     142    142       NAD; via amide nitrogen (By similarity).
FT   BINDING     257    257       NAD (By similarity).
FT   BINDING     283    283       NAD (By similarity).
SQ   SEQUENCE   356 AA;  38575 MW;  FA7B28E2F3024B69 CRC64;
     MTDERPKVAV LGGGSFGTAI ASIAADNGAR VNQWLRDPAL IEQINREHRN ARYLPDYAIN
     PAVVASGDMQ EVLRDAELVF IAIPSSAFLT VVRQALPWLK PTQILVSTTK GIQEDGFKLM
     SQILEEETGF PHIGVLSGPN LASEIAQKHL TATVIASDDP LTRARVQSAL GCDYFRVYAS
     NDRYGVELGG ALKNIYAIAA GMAAALGMGE NTRSMLMTRA LAEMSRFAVA LGANPLTFIG
     LAGVGDLIVT CSSKLSRNYR VGFALGEDKT LEEAVTALGQ VAEGVNTVSL VREKARREHI
     YMPLAEGLYQ VLFNGVPARQ MAQMLMQQEQ SSDVEFILSR QDVFEARRLE PGAEET
//
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