(data stored in SCRATCH zone)

SWISSPROT: D4YXR6_SPHJU

ID   D4YXR6_SPHJU            Unreviewed;       323 AA.
AC   D4YXR6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 56.
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:BAI95148.1};
GN   OrderedLocusNames=SJA_C1-03140 {ECO:0000313|EMBL:BAI95148.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95148.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95148.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) =
CC       glycerone phosphate + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU000439, ECO:0000256|SAAS:SAAS00764424}.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism. {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764434}.
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:SAAS00649394}.
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DR   EMBL; AP010803; BAI95148.1; -; Genomic_DNA.
DR   RefSeq; WP_013038936.1; NC_014006.1.
DR   ProteinModelPortal; D4YXR6; -.
DR   STRING; 452662.SJA_C1-03140; -.
DR   EnsemblBacteria; BAI95148; BAI95148; SJA_C1-03140.
DR   GeneID; 29272016; -.
DR   KEGG; sjp:SJA_C1-03140; -.
DR   eggNOG; ENOG4105CSF; Bacteria.
DR   eggNOG; COG0240; LUCA.
DR   HOGENOM; HOG000246853; -.
DR   KO; K00057; -.
DR   OMA; NMIGKGY; -.
DR   OrthoDB; POG091H060E; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000007753; Chromosome 1.
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   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
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   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; D4YXR6.
DR   SWISS-2DPAGE; D4YXR6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764341};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764443};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764450};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3,
KW   ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00764378};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00809767,
KW   ECO:0000313|EMBL:BAI95148.1};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764418};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764387};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        3    151       NAD_Gly3P_dh_N. {ECO:0000259|Pfam:
FT                                PF01210}.
FT   DOMAIN      172    312       NAD_Gly3P_dh_C. {ECO:0000259|Pfam:
FT                                PF07479}.
FT   NP_BIND       7     12       NAD. {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   REGION      247    248       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00394, ECO:0000256|PIRSR:
FT                                PIRSR000114-2}.
FT   ACT_SITE    183    183       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00394, ECO:0000256|PIRSR:PIRSR000114-
FT                                1}.
FT   BINDING     100    100       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00394}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00394, ECO:0000256|PIRSR:PIRSR000114-
FT                                2}.
FT   BINDING     132    132       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     247    247       NAD. {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     273    273       NAD. {ECO:0000256|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   323 AA;  32995 MW;  ABBAD4A8F53CB2BC CRC64;
     MKAGIIGAGA WGTALAQTLA AGGQHVRLWA LEPEVVEAVN NDRQNPLYLP RIPLSPSIEA
     TGDIAAMADR DMLLIVSPAQ HLRKVVAQAP AGPPLILCSK GIEAGTGLLM SEVAAEAQPG
     SPIAVLSGPT FAHEVAKGLP TAITLACADA DLAAKIAARI ARPAFRPYLS DDVVGAEIGG
     AVKNVLAIAC GVAEGAGLGL NARASLISRG FAEMTRFGLA RGARAETLAG LSGLGDLVLT
     CSSTDSRNFS LGKGLGEGRA ARDLLANRRT VAEGAFTAPV LREAARAARV EMPVVEAVCA
     LLEDAAPLAQ VMDALLARPL RAE
//

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