G1PDH_GEOSE
ID G1PDH_GEOSE Reviewed; 404 AA.
AC B3EYN8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 42.
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}; Synonyms=araM;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6 / NCIMB 40222;
RA Shoham Y., Shulami S., Ben-David A., Langut Y.;
RT "Hemicellulose utilization cluster in Geobacillus stearothermophilus strain
RT T-6.";
RL Submitted (JUN-2008) 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 probably used for the
CC synthesis of phosphoglycerolipids in Gram-positive bacterial species.
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=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00497};
CC Note=Binds 1 nickel ion per subunit. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACE73686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ868502; ACE73686.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B3EYN8; -.
DR SMR; B3EYN8; -.
DR PRIDE; B3EYN8; -.
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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00497_B; G1P_dehydrogenase_B; 1.
DR InterPro; IPR023003; G1P_dehydrogenase_bac.
DR InterPro; IPR032837; G1PDH.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; PTHR43616; 1.
DR Pfam; PF13685; Fe-ADH_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Metal-binding; NAD; NADP;
KW Nickel; Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism.
FT CHAIN 1..404
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000350640"
FT BINDING 56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 118..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 140..143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 192
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 272
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 292
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
SQ SEQUENCE 404 AA; 45407 MW; A0FB8FE86ED11027 CRC64;
MNQTLEEVVS LARQCGCGHR HYDIPIEQMV VGREAFARLV AYLRHKRYER VAIVADDHTF
AAVERSLCDQ LENGSIRYTV CLVQPDENGD VIADERSIVQ VLLETPDDVD VLIAVGAGTI
HDITRFSSYK MRIPFISVPT APSVDGFTSM GAPLIIRGVK KTIQAQAPIA VFAHTGVLCQ
SPKEMIAAGF GDMVAKYTSL ADWQFAHWMA DEPYCPFVHQ LTEQSLQTCV DHIDDIAAGG
EQGIRVLMDA LLQSGIAMLL MGQSYSASGA EHHLSHYWEM EFLRQKKRQV LHGAKVGVST
PIIIEHYQRV FWPLLNELEK RPKSMDEATW ERLKANTASI RELLESLPSP ERIRTMLAKV
GGAIAPEQLG IDPQLVERSL REAHRLRLNR FTMLYFLNEL IFVE
