G1PDH_METJA
ID G1PDH_METJA Reviewed; 335 AA.
AC Q58122;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=MJ0712;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- 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; L77117; AAB98707.1; -; Genomic_DNA.
DR PIR; H64388; H64388.
DR RefSeq; WP_010870218.1; NC_000909.1.
DR PDB; 4RFL; X-ray; 2.20 A; A/B/C/D=1-335.
DR PDB; 4RGQ; X-ray; 2.23 A; A/B/C/D=1-335.
DR PDB; 4RGV; X-ray; 2.45 A; A/B=1-335.
DR PDBsum; 4RFL; -.
DR PDBsum; 4RGQ; -.
DR PDBsum; 4RGV; -.
DR AlphaFoldDB; Q58122; -.
DR SMR; Q58122; -.
DR STRING; 243232.MJ_0712; -.
DR PRIDE; Q58122; -.
DR EnsemblBacteria; AAB98707; AAB98707; MJ_0712.
DR GeneID; 1451590; -.
DR KEGG; mja:MJ_0712; -.
DR eggNOG; arCOG00982; Archaea.
DR HOGENOM; CLU_038362_0_0_2; -.
DR InParanoid; Q58122; -.
DR OMA; ALHGEQC; -.
DR OrthoDB; 57545at2157; -.
DR PhylomeDB; Q58122; -.
DR BRENDA; 1.1.1.261; 3260.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000805; 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; Reference proteome; Zinc.
FT CHAIN 1..335
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000157342"
FT BINDING 78..82
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 100..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4RFL"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 139..166
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 172..191
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:4RFL"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 247..265
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4RFL"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4RFL"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:4RFL"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:4RFL"
SQ SEQUENCE 335 AA; 37275 MW; A99C777C3126367B CRC64;
MIIVTPRYTI IEDGAINKIE EILKKLNLKN PLVITGKNTK KYCRFFYDIV YYDEILNNLE
IELKKYTAYD CVIGIGGGRS IDTGKYLAYK LGIPFISVPT TASNDGIASP IVSIRQPSFM
VDAPIAIIAD TEIIKKSPRR LLSAGMGDIV SNITAVLDWK LAYKEKGEKY SESSAIFSKT
IAKELISYVL NSDLSEYHNK LVKALVGSGI AIAIANSSRP ASGSEHLFSH ALDKLKEEYN
LNINSLHGEQ CGIGTIMMSY LHEKENKKLS GLHEKIKMSL KKVDAPTTAK ELGFDEDIII
EALTMAHKIR NRWTILRDGL SREEARKLAE ETGVI
