GPDA_ARCFU
ID GPDA_ARCFU Reviewed; 335 AA.
AC O29390;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394};
DE EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394};
DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394};
GN Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394}; OrderedLocusNames=AF_0871;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=15557260; DOI=10.1110/ps.04980304;
RA Sakasegawa S., Hagemeier C.H., Thauer R.K., Essen L.-O., Shima S.;
RT "Structural and functional analysis of the gpsA gene product of
RT Archaeoglobus fulgidus: a glycerol-3-phosphate dehydrogenase with an
RT unusual NADP+ preference.";
RL Protein Sci. 13:3161-3171(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00394};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00394};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for NADPH {ECO:0000269|PubMed:15557260};
CC KM=1 mM for dihydroxyacetone phosphate {ECO:0000269|PubMed:15557260};
CC Vmax=44 umol/min/mg enzyme {ECO:0000269|PubMed:15557260};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:15557260};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00394}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15557260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Has a strong preference for NADP over NAD.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}.
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; AE000782; AAB90367.1; -; Genomic_DNA.
DR PIR; G69358; G69358.
DR RefSeq; WP_010878372.1; NC_000917.1.
DR PDB; 1TXG; X-ray; 1.70 A; A/B=1-335.
DR PDBsum; 1TXG; -.
DR AlphaFoldDB; O29390; -.
DR SMR; O29390; -.
DR STRING; 224325.AF_0871; -.
DR EnsemblBacteria; AAB90367; AAB90367; AF_0871.
DR GeneID; 24794469; -.
DR KEGG; afu:AF_0871; -.
DR eggNOG; arCOG00456; Archaea.
DR HOGENOM; CLU_033449_1_1_2; -.
DR OMA; NRMFGNM; -.
DR OrthoDB; 71099at2157; -.
DR PhylomeDB; O29390; -.
DR SABIO-RK; O29390; -.
DR UniPathway; UPA00940; -.
DR EvolutionaryTrace; O29390; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome.
FT CHAIN 1..335
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000138068"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 7..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 259..260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 289
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:1TXG"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:1TXG"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1TXG"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 182..209
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 214..235
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:1TXG"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:1TXG"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:1TXG"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:1TXG"
SQ SEQUENCE 335 AA; 36785 MW; E6B87240B92BD059 CRC64;
MIVSILGAGA MGSALSVPLV DNGNEVRIWG TEFDTEILKS ISAGREHPRL GVKLNGVEIF
WPEQLEKCLE NAEVVLLGVS TDGVLPVMSR ILPYLKDQYI VLISKGLIDF DNSVLTVPEA
VWRLKHDLRE RTVAITGPAI AREVAKRMPT TVVFSSPSES SANKMKEIFE TEYFGVEVTT
DIIGTEITSA LKNVYSIAIA WIRGYESRKN VEMSNAKGVI ATRAINEMAE LIEILGGDRE
TAFGLSGFGD LIATFRGGRN GMLGELLGKG LSIDEAMEEL ERRGVGVVEG YKTAEKAYRL
SSKINADTKL LDSIYRVLYE GLKVEEVLFE LATFK
