GPDA_CORGB
ID GPDA_CORGB Reviewed; 332 AA.
AC A4QDT3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=cgR_1394;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
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 -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00394}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}.
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DR EMBL; AP009044; BAF54380.1; -; Genomic_DNA.
DR RefSeq; WP_003858849.1; NC_009342.1.
DR AlphaFoldDB; A4QDT3; -.
DR SMR; A4QDT3; -.
DR EnsemblBacteria; BAF54380; BAF54380; cgR_1394.
DR GeneID; 58310664; -.
DR KEGG; cgt:cgR_1394; -.
DR HOGENOM; CLU_033449_0_2_11; -.
DR OMA; NRMFGNM; -.
DR PhylomeDB; A4QDT3; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000006698; 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.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism.
FT CHAIN 1..332
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_1000049499"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 8..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 255..256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
SQ SEQUENCE 332 AA; 34682 MW; 9697C6E1AB8349C3 CRC64;
MVSVSVMGAG SWGTTLAKVF SDAGNAVTLW ARREELASTI RDSHENRDYL PGITLPESLQ
VTSSATEALE GAAIVVLAIP SQALRGNLAE WKETIPQDAT LVSLAKGIEK GTHLRMSEVI
AEVTEADPSR IAVLSGPNLA REIAEGQPAA TVIACPDENR AKLVQAAVAA PYFRPYTNTD
VVGTEIGGAC KNVIALACGI SHGYGLGENT NASLITRGLA EIARLGATLG ADAKTFSGLA
GMGDLVATCS SPLSRNRSFG ERLGQGESLE KAREATNGQV AEGVISSQSI FDLATKLGVE
MPITQAVYGV CHRDMKVTDM IVALMGRSKK AE
