G1PDH_PYRCJ
ID G1PDH_PYRCJ Reviewed; 338 AA.
AC A3MTM6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Pcal_0566;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) 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; CP000561; ABO07993.1; -; Genomic_DNA.
DR PDB; 5FB3; X-ray; 2.45 A; A/B/C/D/E/F=1-338.
DR PDBsum; 5FB3; -.
DR AlphaFoldDB; A3MTM6; -.
DR SMR; A3MTM6; -.
DR STRING; 410359.Pcal_0566; -.
DR PRIDE; A3MTM6; -.
DR EnsemblBacteria; ABO07993; ABO07993; Pcal_0566.
DR KEGG; pcl:Pcal_0566; -.
DR eggNOG; arCOG00982; Archaea.
DR HOGENOM; CLU_038362_0_0_2; -.
DR OMA; ALHGEQC; -.
DR BRENDA; 1.1.1.261; 7282.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001431; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; NAD; NADP; Oxidoreductase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Zinc.
FT CHAIN 1..338
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_1000050607"
FT BINDING 81..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 103..106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5FB3"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:5FB3"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5FB3"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:5FB3"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5FB3"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:5FB3"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5FB3"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5FB3"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 207..227
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 256..271
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:5FB3"
FT TURN 291..295
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:5FB3"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:5FB3"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:5FB3"
SQ SEQUENCE 338 AA; 36990 MW; CBB439BAEFEEB468 CRC64;
MKKVERFEVP RTIIFGPGAL EKTPEVIPPS GRVLIITGKS STRKYAERVA ELLKQNCEII
SYDQVELEKP GFDLVIGIGG GRPLDMAKVY SYIHKKPFVA IPTSASHDGI ASPYVSFSLT
QRFSKYGKIS SSPVAIIADT SIILSAPSRL LKAGIGDLLG KIIAVRDWQL AHRLKGEEYS
EYAAHLSLTS YKIAVGNAQK IKNFIREEDV RVLVKALIGC GVAMGIAGSS RPCSGSEHLF
AHAIEVRVEK EDEVVHGELV ALGTIIMAYL HGINWRRIKR IADIIGLPTS LRQANIDVDL
ALEALTTAHT LRPDRYTILG DGLSREAAKR ALEDVELI
