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Database: UniProt
Entry: Q0TPK0
LinkDB: Q0TPK0
Original site: Q0TPK0 
ID   GPDA_CLOP1              Reviewed;         331 AA.
AC   Q0TPK0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   14-MAY-2014, entry version 65.
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=CPF_2007;
OS   Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / NCTC 8237 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000246; ABG82368.1; -; Genomic_DNA.
DR   RefSeq; YP_696440.1; NC_008261.1.
DR   ProteinModelPortal; Q0TPK0; -.
DR   STRING; 195103.CPF_2007; -.
DR   EnsemblBacteria; ABG82368; ABG82368; CPF_2007.
DR   GeneID; 4202431; -.
DR   KEGG; cpf:CPF_2007; -.
DR   PATRIC; 19486266; VBICloPer106549_1952.
DR   eggNOG; COG0240; -.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; MPISTAV; -.
DR   OrthoDB; EOG6JDWF4; -.
DR   BioCyc; CPER195103:GHAW-2023-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    331       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_1000049497.
FT   NP_BIND       8     13       NAD (By similarity).
FT   REGION      253    254       Substrate binding (By similarity).
FT   ACT_SITE    189    189       Proton acceptor (By similarity).
FT   BINDING     106    106       NAD; via amide nitrogen (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
FT   BINDING     138    138       NAD; via amide nitrogen (By similarity).
FT   BINDING     253    253       NAD (By similarity).
FT   BINDING     279    279       NAD (By similarity).
SQ   SEQUENCE   331 AA;  35649 MW;  2A372299389E91A2 CRC64;
     MSKVAFLGAG SFGTSLGILL GNKGVTVSLW DRDENVINDI NVNRKNDKYI KDLTIPTNVT
     AYKDLDEALN GAEYVVLAVP SHVIRTACKN LKGKINDDVI IINIAKGIEE GTNLRLSQVI
     NQELPNNKVV VLSGPSHAEE VSKGIPTTLV ASSECMECAE KVQDLFMDKN FRIYTNDDII
     GVEIGGAVKN IIALAAGVCD GIGYGDNSKA ALMTRGMAEI ARIGIKMGGK AETFFGLTGM
     GDLIVTCTSM HSRNRRAGIL IGQGKTAEEA IEEVGMVVEG IKACKAFYEL KEKEGVTMPI
     TDIAYKVLFE GAKAENAVSL LMERDKKKEE I
//
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