G1PDH_ALKCK
ID G1PDH_ALKCK Reviewed; 394 AA.
AC Q5WL08;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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;
GN OrderedLocusNames=ABC0405;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP006627; BAD62947.1; -; Genomic_DNA.
DR RefSeq; WP_011245266.1; NC_006582.1.
DR AlphaFoldDB; Q5WL08; -.
DR SMR; Q5WL08; -.
DR STRING; 66692.ABC0405; -.
DR EnsemblBacteria; BAD62947; BAD62947; ABC0405.
DR KEGG; bcl:ABC0405; -.
DR eggNOG; COG0371; Bacteria.
DR HOGENOM; CLU_038362_1_0_9; -.
DR OMA; DFICRST; -.
DR OrthoDB; 717704at2; -.
DR Proteomes; UP000001168; 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: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;
KW Reference proteome.
FT CHAIN 1..394
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000350639"
FT BINDING 52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 114..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 136..139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 188
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 268
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 288
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
SQ SEQUENCE 394 AA; 42745 MW; 0498F7DC2474BB69 CRC64;
MNISALKARI RASKEDLYPL PLEQIVVAEG ALREAAAFIA KQAESGVVLV ADSHTYKAAG
RDLHDHLCQK GVKADWHLLE PNSNGDIIAD EVSLISVMLK VEQSTKLLVA VGAGTIHDIV
RFVSGKTNKP FVSIPTAPSV DGFTSLGAPI VVQGSKKTYQ LVAPIALFAD TVVLQHAPPA
LIAAGFGDMV GKYTSLFDWK IGSLLKNEAY SDLVADLTEE ALSTCVDKVA DIGKRTSAGV
QVLMESLLTS GLAMALFGYS HPASGAEHHL SHYWEMEALR LGKKQLLHGA KVGLSTQIIN
RFYKNTVLPD VHRFLDDDEA KQVIALVEAL PDPDDVKALL EQAGWNEALV PIAPELVEES
LQHAYLLRDR YTLLRLYREG TTMKKEGDAH VGRS
