GPDH2_CAEEL
ID GPDH2_CAEEL Reviewed; 392 AA.
AC P34517; Q8I4H2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Probable glycerol-3-phosphate dehydrogenase 2;
DE EC=1.1.1.8;
GN Name=gpdh-2; ORFNames=K11H3.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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=1.1.1.8;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; Z22180; CAD54146.1; -; Genomic_DNA.
DR PIR; S40754; S40754.
DR RefSeq; NP_871632.1; NM_181903.5.
DR AlphaFoldDB; P34517; -.
DR SMR; P34517; -.
DR BioGRID; 41593; 4.
DR IntAct; P34517; 1.
DR STRING; 6239.K11H3.1b; -.
DR EPD; P34517; -.
DR PaxDb; P34517; -.
DR PeptideAtlas; P34517; -.
DR EnsemblMetazoa; K11H3.1b.1; K11H3.1b.1; WBGene00010778.
DR GeneID; 176399; -.
DR CTD; 176399; -.
DR WormBase; K11H3.1b; CE31851; WBGene00010778; gpdh-2.
DR eggNOG; KOG2711; Eukaryota.
DR InParanoid; P34517; -.
DR OMA; NRMFGNM; -.
DR OrthoDB; 476066at2759; -.
DR PhylomeDB; P34517; -.
DR Reactome; R-CEL-1483166; Synthesis of PA.
DR PRO; PR:P34517; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010778; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P34517; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; ISS:WormBase.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; 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:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IGI:WormBase.
DR GO; GO:0006973; P:intracellular accumulation of glycerol; IGI:WormBase.
DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 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; IPR017751; G3P_DH_NAD-dep_euk.
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 TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..392
FT /note="Probable glycerol-3-phosphate dehydrogenase 2"
FT /id="PRO_0000138070"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 42..47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 312..313
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 392 AA; 42792 MW; E42BCCBE280B04A5 CRC64;
MSSSRIPQCE NSSRLSLSSI FRYFGTTSTI ATMSPKKVTI IGSGNWGSAI ARIVGSTTKS
FPDEFDPTVR MWVFEEIVNG EKLSEVINNR HENIKYLPGK VLPNNVVAVT DLVESCEGSN
VLVFVVPHQF VKGICEKLVG KIPADTQAIS LIKGISFDKT NQGVSTEKRG GLKLISEEIK
EILKIEVSVL MGANLAPEVA NDNFCEATIG CKRKAEDGPL LKKLFHTDNF RINVVEDAHT
VELCGALKNV VACAAGFTDG LGYGDNTKAA VIRLGLMETT KFVEHYYPGS NLQTFFESCG
IADLITTCYG GRNRKVCEAF VKTGKSMAEV EKELLNGQSA QGPLTAEEVY LMMHKTGLDA
KFPLFTAVHK ICAGEMKPAE LVDCLRNHPE HM
