ID W8GIZ0_9MOLU Unreviewed; 355 AA.
AC W8GIZ0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU000439};
DE EC=1.1.1.94 {ECO:0000256|RuleBase:RU000439};
GN Name=gpsA {ECO:0000313|EMBL:AHK22207.1};
GN ORFNames=X271_00094 {ECO:0000313|EMBL:AHK22207.1};
OS Candidatus Hepatoplasma crinochetorum Av.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Hepatoplasma.
OX NCBI_TaxID=1427984 {ECO:0000313|EMBL:AHK22207.1, ECO:0000313|Proteomes:UP000019450};
RN [1] {ECO:0000313|EMBL:AHK22207.1, ECO:0000313|Proteomes:UP000019450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Av {ECO:0000313|EMBL:AHK22207.1,
RC ECO:0000313|Proteomes:UP000019450};
RX PubMed=24482531; DOI=10.1093/gbe/evu020;
RA Leclercq S., Dittmer J., Bouchon D., Cordaux R.;
RT "Phylogenomics of "Candidatus Hepatoplasma crinochetorum," a Lineage of
RT Mollicutes Associated with Noninsect Arthropods.";
RL Genome Biol. Evol. 6:407-415(2014).
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;
CC Evidence={ECO:0000256|RuleBase:RU000439};
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|RuleBase:RU000437}.
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DR EMBL; CP006932; AHK22207.1; -; Genomic_DNA.
DR AlphaFoldDB; W8GIZ0; -.
DR STRING; 1427984.X271_00094; -.
DR KEGG; hcr:X271_00094; -.
DR eggNOG; COG0240; Bacteria.
DR HOGENOM; CLU_033449_0_0_14; -.
DR OrthoDB; 9812273at2; -.
DR Proteomes; UP000019450; 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-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000019450}.
FT DOMAIN 27..183
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 204..343
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 30..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 278..279
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ SEQUENCE 355 AA; 40282 MW; 8C9A07CC1DB75061 CRC64;
MKNLNNTNNI NNELIENKDK LKKFNFTIIG SGAFGTAVAN FLVDNNNVII YGIDKKEIDD
IKINHKNTKY FGSIKLKNKI EATNNIKEAL KEADAILLAI PSHIFKIVLK EKILPNMKKA
AYFINLAKGF DYKEIKFLNQ IIDETIPKNL NLGTLKLSGP SFAKELLKKE PTKFVLAAKD
IEIAKNLKKY FETNYINIII SNEIYGVEIL SVIKNPLSIL LGIVQGLGYK MNSRAYIFSE
ALEEMKKIVN LYKLNENIIF LPAGVGDLYL TGNSKKSRNF SVGYKIGKND KVNKKILNSF
TTIEGLRSIE IIFLLAKKNG IDLKLFNLLY NITYKNTSPS KAMDEFFKGI NEHYE
//
