ID GPDA_BACAH Reviewed; 340 AA.
AC A0RBW0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 29-MAY-2013, entry version 56.
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=BALH_1360;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/JB.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK84703.1; -; Genomic_DNA.
DR RefSeq; YP_894210.1; NC_008600.1.
DR ProteinModelPortal; A0RBW0; -.
DR STRING; 412694.BALH_1360; -.
DR EnsemblBacteria; ABK84703; ABK84703; BALH_1360.
DR GeneID; 4546108; -.
DR KEGG; btl:BALH_1360; -.
DR PATRIC; 18995114; VBIBacThu63319_1560.
DR eggNOG; COG0240; -.
DR HOGENOM; HOG000246854; -.
DR KO; K00057; -.
DR OMA; DVIGCEI; -.
DR ProtClustDB; PRK00094; -.
DR BioCyc; BTHU412694:GH1W-1395-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:HAMAP.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:InterPro.
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: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: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; 6DGDH_C_like; 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 1 340 Glycerol-3-phosphate dehydrogenase
FT [NAD(P)+].
FT /FTId=PRO_1000049482.
FT NP_BIND 8 13 NAD (By similarity).
FT REGION 256 257 Substrate binding (By similarity).
FT ACT_SITE 192 192 Proton acceptor (By similarity).
FT BINDING 106 106 NAD; via amide nitrogen (By similarity).
FT BINDING 106 106 Substrate (By similarity).
FT BINDING 141 141 NAD; via amide nitrogen (By similarity).
FT BINDING 256 256 NAD (By similarity).
FT BINDING 282 282 NAD (By similarity).
SQ SEQUENCE 340 AA; 36593 MW; C9F726A6F3465B45 CRC64;
MTKITVVGAG SWGTALAMVL ADNGHDVRIW GNRSELMDEI NTKHENSRYL PGITLPSTIV
AYSSLEEALV DVNVVLLVVP TKAYREVLQD MKKYVAGPTT WIHASKGIEP GTSKRISEVI
EEEIPEDLIK DVVVLSGPSH AEEVGLRQAT TVTSAAKRME AAEEVQDLFM NSYFRVYTNP
DIVGVELGGA LKNIIALAAG ITDGLGLGDN AKAALMTRGL TEIARLGRKM GGNPLTFAGL
TGMGDLIVTC TSVHSRNWRA GNMLGKGHSL EEVLESMGMV VEGVRTTKAA HELAEKMEVE
MPITAALYDV LFNGNNVKDA VGSLMGRVRK HEVEAIPDLL
//
