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G1PDH_STAMF
ID   G1PDH_STAMF             Reviewed;         355 AA.
AC   A3DN28;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00497};
DE            Short=G1P dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497};
DE            Short=G1PDH {ECO:0000255|HAMAP-Rule:MF_00497};
DE            EC=1.1.1.261 {ECO:0000255|HAMAP-Rule:MF_00497};
DE   AltName: Full=Enantiomeric glycerophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00497};
DE   AltName: Full=sn-glycerol-1-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497};
GN   Name=egsA {ECO:0000255|HAMAP-Rule:MF_00497}; OrderedLocusNames=Smar_0939;
OS   Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=399550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA   Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA   Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA   Woese C., Bristow J., Kyrpides N.;
RT   "The complete genome sequence of Staphylothermus marinus reveals
RT   differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL   BMC Genomics 10:145-145(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=21304655; DOI=10.4056/sigs.30527;
RA   Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT   type strain F1.";
RL   Stand. Genomic Sci. 1:183-188(2009).
CC   -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of
CC       dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-
CC       phosphate (G1P). The G1P thus generated is used as the glycerophosphate
CC       backbone of phospholipids in the cellular membranes of Archaea.
CC       {ECO:0000255|HAMAP-Rule:MF_00497}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685,
CC         ChEBI:CHEBI:57945; EC=1.1.1.261; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.261; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00497};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00497};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00497};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00497}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00497}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00497}.
CC   -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00497}.
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DR   EMBL; CP000575; ABN70038.1; -; Genomic_DNA.
DR   RefSeq; WP_011839229.1; NC_009033.1.
DR   AlphaFoldDB; A3DN28; -.
DR   SMR; A3DN28; -.
DR   STRING; 399550.Smar_0939; -.
DR   EnsemblBacteria; ABN70038; ABN70038; Smar_0939.
DR   GeneID; 4907415; -.
DR   KEGG; smr:Smar_0939; -.
DR   eggNOG; arCOG00982; Archaea.
DR   HOGENOM; CLU_038362_0_0_2; -.
DR   OMA; ALHGEQC; -.
DR   OrthoDB; 57545at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000254; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106357; F:glycerol-1-phosphate dehydrogenase [NAD+] activity; IEA:RHEA.
DR   GO; GO:0106358; F:glycerol-1-phosphate dehydrogenase [NADP+] activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1.
DR   InterPro; IPR023002; G1P_dehydrogenase_arc.
DR   InterPro; IPR032837; G1PDH.
DR   InterPro; IPR016205; Glycerol_DH.
DR   PANTHER; PTHR43616; PTHR43616; 1.
DR   Pfam; PF13685; Fe-ADH_2; 1.
DR   PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Metal-binding; NAD; NADP;
KW   Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Zinc.
FT   CHAIN           1..355
FT                   /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT                   /id="PRO_0000350661"
FT   BINDING         101..105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         123..126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
SQ   SEQUENCE   355 AA;  38601 MW;  E24F8CEA368C0C48 CRC64;
     MLNRSIHEIT LPLKVIIGSN ILDKIPDYLL KMKLTNQYKA GIITGPTTYN VAGKIVEEAM
     KNNGYIVEVW KARDARIETA NQIVEETKKH GIKIFLGVGG GKSIDLAKYA AYKNNGYMIS
     VPTAASHDGI ASPFASLKGT SKPTSTPTTT PYAIIADIDM ISKAPPRLIR SGVGDLLGKL
     TAVKDWQLAH RLKGEYYGEY AAQLALLSAK HVIRYHELIA SGNPDGIRIV VEALISSGVA
     MCIAGSSRPA SGSEHLFSHA LDLLAPGKAL HGEQVALGTI MMLYLYGDPK WKKIKRIMKK
     IGLPTTAEEI GIPIETIVKA LTIAHKIRPN RYTILGEKGL TEEAAWRLVR ETGII
 
 
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