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Database: UniProt
Entry: Q5X2Y0
LinkDB: Q5X2Y0
Original site: Q5X2Y0 
ID   GPDA_LEGPA              Reviewed;         329 AA.
AC   Q5X2Y0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   19-FEB-2014, entry version 75.
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=lpp2257;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F.,
RA   Etienne J., Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of
RT   host cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628336; CAH13410.1; -; Genomic_DNA.
DR   RefSeq; YP_124568.1; NC_006368.1.
DR   ProteinModelPortal; Q5X2Y0; -.
DR   STRING; 297246.lpp2257; -.
DR   EnsemblBacteria; CAH13410; CAH13410; lpp2257.
DR   GeneID; 3118553; -.
DR   KEGG; lpp:lpp2257; -.
DR   PATRIC; 22325073; VBILegPne27771_2575.
DR   LegioList; lpp2257; -.
DR   eggNOG; COG0240; -.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; RNHTAGR; -.
DR   OrthoDB; EOG6JDWF4; -.
DR   ProtClustDB; PRK00094; -.
DR   BioCyc; LPNE297246:GCO9-2911-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    329       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_0000137978.
FT   NP_BIND      10     15       NAD (By similarity).
FT   REGION      253    254       Substrate binding (By similarity).
FT   ACT_SITE    189    189       Proton acceptor (By similarity).
FT   BINDING     105    105       NAD; via amide nitrogen (By similarity).
FT   BINDING     105    105       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   329 AA;  35435 MW;  21BF1B6FD9430557 CRC64;
     MNKKTIAMLG AGSWGTAVAI HLAKIGHKTL LWSHNPQHVA LMAEQHSNPA YLPGIPFPEN
     LIPSDDLIEC VQLADYVIIA VPSHAFAEII NKIPKPTQGL AWLTKGVDPA SHQLLSQLVA
     SRFGVDFPIA VISGPSFAKE VARFLPTALT LASNNTNYQK KMHQLFHHDN IRVYLSDDLI
     GVQLCGAVKN ILAIACGISD GLGYGANAKA ALITRGLAEM TRLGLSMGAR QDTFLGLAGV
     GDLVLTCTDD QSRNRRFGLL LGREVPIPEA EHQIGQVVEG KHNAAQICAI ANKNKVEMPI
     CEQINALLHG IVHAQQAVNN LMSRPAKEE
//
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