ID F6DT41_DESRL Unreviewed; 352 AA.
AC F6DT41;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
DE EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
GN Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394};
GN OrderedLocusNames=Desru_2932 {ECO:0000313|EMBL:AEG61146.1};
OS Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
OS (Desulfotomaculum ruminis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG61146.1, ECO:0000313|Proteomes:UP000009234};
RN [1] {ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., Plugge C.M., Muyzer G.,
RA Kuever J., Parshina S.N., Ivanova A.E., Nazina T.N., Brambilla E.,
RA Spring S., Klenk H.-P., Woyke T.;
RT "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG61146.1, ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RX PubMed=23408247; DOI=10.4056/sigs.3226659;
RA Spring S., Visser M., Lu M., Copeland A., Lapidus A., Lucas S., Cheng J.F.,
RA Han C., Tapia R., Goodwin L.A., Pitluck S., Ivanova N., Land M., Hauser L.,
RA Larimer F., Rohde M., Goker M., Detter J.C., Kyrpides N.C., Woyke T.,
RA Schaap P.J., Plugge C.M., Muyzer G., Kuever J., Pereira I.A.,
RA Parshina S.N., Bernier-Latmani R., Stams A.J., Klenk H.P.;
RT "Complete genome sequence of the sulfate-reducing firmicute
RT Desulfotomaculum ruminis type strain (DL(T)).";
RL Stand. Genomic Sci. 7:304-319(2012).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00394, ECO:0000256|RuleBase:RU000439};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_00394}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437}.
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DR EMBL; CP002780; AEG61146.1; -; Genomic_DNA.
DR RefSeq; WP_013842898.1; NC_015589.1.
DR AlphaFoldDB; F6DT41; -.
DR STRING; 696281.Desru_2932; -.
DR KEGG; dru:Desru_2932; -.
DR eggNOG; COG0240; Bacteria.
DR HOGENOM; CLU_033449_0_2_9; -.
DR OrthoDB; 9812273at2; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000009234; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 1.
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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00394};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00394}; Reference proteome {ECO:0000313|Proteomes:UP000009234}.
FT DOMAIN 3..159
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 180..320
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 8..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 255..256
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
SQ SEQUENCE 352 AA; 38246 MW; D33C5C2B97021D38 CRC64;
MSKIAMIGAG SWATALAQVL AQKDYSAVLW ARRQELADLI NDGENSRYLP GIPLHAKVTA
DTDLERVLQG AEAVVFGVPS HCFRDLLKKA LPFLQPGAQI INVAKGLEES TLLRLSQVFA
QEVGEAALDR YTVLSGPSHA EEVGRNIPTA VVAASRNLAT AEYVQDLFMS TNFRIYTNPD
VTGVELSGAL KNIIALGTGI ADGLEYGDNT KAAMMTRGLA EITRLGFSMG AELLTFAGLA
GVGDLIVTCT SMHSRNRRCG IEIGRGKTLE EAVESVKMVV EGVRTTRVAW QLAKQQGVEM
PITEQIYRVL FENCSPRTAV MHLMGRGKKL EMEEIVSEKI SCTMDQGREE KQ
//
