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G1PDH_PYRIL
ID   G1PDH_PYRIL             Reviewed;         342 AA.
AC   A1RV58;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Pisl_1689;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL88840.1; -; Genomic_DNA.
DR   RefSeq; WP_011763415.1; NC_008701.1.
DR   AlphaFoldDB; A1RV58; -.
DR   SMR; A1RV58; -.
DR   STRING; 384616.Pisl_1689; -.
DR   EnsemblBacteria; ABL88840; ABL88840; Pisl_1689.
DR   GeneID; 4618030; -.
DR   KEGG; pis:Pisl_1689; -.
DR   eggNOG; arCOG00982; Archaea.
DR   HOGENOM; CLU_038362_0_0_2; -.
DR   OMA; ALHGEQC; -.
DR   OrthoDB; 57545at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000002595; 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; Zinc.
FT   CHAIN           1..342
FT                   /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT                   /id="PRO_1000050608"
FT   BINDING         84..88
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         106..109
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         115
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
SQ   SEQUENCE   342 AA;  37155 MW;  9164C9A2FBF4DC09 CRC64;
     MKQLESFEIP RTVIFGPGAI SKIHQIVASQ KASKILIITG RSVTLQYAKT IADMLTDRSV
     EVLRYDYIDI EKSGFDLVLG VGGGRPIDMA KVYSYVHKKP LVIVPTSASH DGIASPYVSY
     TLAQKMIKYG KIMASPIAIV ADTSIILNAP SRLLKAGVGD LLGKIIAVRD WKLAHRLKGE
     EYSEYASHLS LTSYRIVVAN AARIKNFVRE EDVRVLVKAL IGCGVAMGIA GSSRPCSGSE
     HLFAHAIEIR LEESGGDAIH GELVALGTII MAYLHGINWR RVKKIAKLVG LPTTLREAGI
     DYDLAIEALV VAHTLRPDRY TILGDGLSKD AARRAIEATE LA
 
 
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