(data stored in ACNUC7421 zone)

SWISSPROT: GPDA_STRM5

ID   GPDA_STRM5              Reviewed;         341 AA.
AC   B4SSF9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394};
DE            EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394};
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394};
GN   Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394};
GN   OrderedLocusNames=Smal_0136;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.94;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + H(+) + NADPH; Xref=Rhea:RHEA:11096,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.94;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00394};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism. {ECO:0000255|HAMAP-Rule:MF_00394}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}.
DR   EMBL; CP001111; ACF49841.1; -; Genomic_DNA.
DR   RefSeq; WP_004134677.1; NC_011071.1.
DR   SMR; B4SSF9; -.
DR   STRING; 391008.Smal_0136; -.
DR   EnsemblBacteria; ACF49841; ACF49841; Smal_0136.
DR   KEGG; smt:Smal_0136; -.
DR   eggNOG; ENOG4105CSF; Bacteria.
DR   eggNOG; COG0240; LUCA.
DR   HOGENOM; HOG000246853; -.
DR   KO; K00057; -.
DR   OMA; WLCKGFE; -.
DR   OrthoDB; 1419877at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00680-MONOMER; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001867; Chromosome.
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-UniRule.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] 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-UniRule.
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-UniRule.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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; IPR036291; NAD(P)-bd_dom_sf.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SSF9.
DR   SWISS-2DPAGE; B4SSF9.
KW   Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW   NAD; Oxidoreductase; Phospholipid biosynthesis;
KW   Phospholipid metabolism.
FT   CHAIN         1    341       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_1000123193.
FT   NP_BIND      12     17       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   REGION      258    259       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   ACT_SITE    194    194       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     110    110       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     110    110       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     143    143       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     258    258       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     284    284       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   341 AA;  35850 MW;  D73E1FABAD4C66D2 CRC64;
     MSTTADKIAV LGAGSWGTAL ASLLARHGHP TVLWGRDAAM VEAIDQRHEN PRYLPGIPLP
     DSLRATTDLA SAVEGAAWIL VVTPSHAFGE TVRALAPLRP AGAGVAWATK GFEPGSGRFL
     HEVAREVLGE DVPLAVVTGP SFAKEVTQGL PTAITVHGDV PEFAQTVAEA MHGPAFRAYT
     GDDMVGAELG GAMKNVLAVA TGVADGMQLG LNARAGLITR GLNEMLRLAA AIGAKPETLM
     GLAGLGDLVL TCTGDLSRNR RLGLALGRGQ TLQDAVREIG QVVESVQTAD EVMRQARRHG
     IDLPISDRVR AVLHGEQTPE EGLRALLARE QKPEYPDTLF K
//

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