(data stored in ACNUC1104 zone)

SWISSPROT: D3VGU4_XENNA

ID   D3VGU4_XENNA            Unreviewed;       334 AA.
AC   D3VGU4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
DE            EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
GN   Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394,
GN   ECO:0000313|EMBL:CBJ88229.1};
GN   OrderedLocusNames=XNC1_0141 {ECO:0000313|EMBL:CBJ88229.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88229.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88229.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:0000256|HAMAP-Rule:MF_00394,
CC         ECO:0000256|SAAS:SAAS01123910};
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:0000256|HAMAP-Rule:MF_00394,
CC         ECO:0000256|RuleBase:RU000439, ECO:0000256|SAAS:SAAS01123901};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism. {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS01090075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS01090105}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00567958}.
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DR   EMBL; FN667742; CBJ88229.1; -; Genomic_DNA.
DR   STRING; 406817.XNC1_0141; -.
DR   EnsemblBacteria; CBJ88229; CBJ88229; XNC1_0141.
DR   KEGG; xne:XNC1_0141; -.
DR   eggNOG; ENOG4105CSF; Bacteria.
DR   eggNOG; COG0240; LUCA.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; WLCKGFE; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000008075; 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; D3VGU4.
DR   SWISS-2DPAGE; D3VGU4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS01090070};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS01090084};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS01090080};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3,
KW   ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS01090086};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00321802,
KW   ECO:0000313|EMBL:CBJ88229.1};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS01090074};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS01090066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN        2    155       NAD_Gly3P_dh_N. {ECO:0000259|Pfam:
FT                                PF01210}.
FT   DOMAIN      177    316       NAD_Gly3P_dh_C. {ECO:0000259|Pfam:
FT                                PF07479}.
FT   NP_BIND       5     10       NAD. {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   REGION      252    253       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00394, ECO:0000256|PIRSR:
FT                                PIRSR000114-2}.
FT   ACT_SITE    188    188       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00394, ECO:0000256|PIRSR:PIRSR000114-
FT                                1}.
FT   BINDING     103    103       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00394}.
FT   BINDING     103    103       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00394, ECO:0000256|PIRSR:PIRSR000114-
FT                                2}.
FT   BINDING     136    136       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     252    252       NAD. {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     278    278       NAD. {ECO:0000256|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   334 AA;  35982 MW;  38ACCB3FA2355A86 CRC64;
     MTVIGAGSYG TALAITLARN GYKVVLWGHN PEHIQTLQQT RCNQTFLPDV SFPDSLRPET
     DLKNAVSASR DILIVVPSHV FNDVLQQIKP HLQHDSRIVW ATKGLEAETG RLLQDVAREI
     LGNEIPLAVV SGPTFAKELA AGLPTAIAVS ATTPEFGEEL QQLFHCGKSF RVYKNPDFIG
     VQLGGAIKNV IAIGAGISDG MGFGANARTA LITRGLAEMS RLGVALGADP STFMGMAGLG
     DLVLTCTDNQ SRNRRFGMML GQGVNVDDAQ HEIGQVVEGY RNTKEVRALA ERTGVEMPIT
     EQIYQILYCN KNVIEAARAL LGRATRDEGE VSQS
//

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