G6PD_CAEEL
ID G6PD_CAEEL Reviewed; 522 AA.
AC Q27464;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
GN Name=gspd-1; ORFNames=B0035.5;
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=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 -!- FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes
CC the first and rate-limiting step of the oxidative branch within the
CC pentose phosphate pathway/shunt, an alternative route to glycolysis for
CC the dissimilation of carbohydrates and a major source of reducing power
CC and metabolic intermediates for fatty acid and nucleic acid
CC biosynthetic processes. {ECO:0000250|UniProtKB:P11413}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000250|UniProtKB:P11413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC Evidence={ECO:0000250|UniProtKB:P11413};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000250|UniProtKB:P11413}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P11413}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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; Z73102; CAA97412.1; -; Genomic_DNA.
DR PIR; T18657; T18657.
DR RefSeq; NP_502129.1; NM_069728.4.
DR AlphaFoldDB; Q27464; -.
DR SMR; Q27464; -.
DR BioGRID; 43145; 17.
DR STRING; 6239.B0035.5; -.
DR iPTMnet; Q27464; -.
DR EPD; Q27464; -.
DR PaxDb; Q27464; -.
DR PeptideAtlas; Q27464; -.
DR EnsemblMetazoa; B0035.5.1; B0035.5.1; WBGene00007108.
DR GeneID; 178046; -.
DR KEGG; cel:CELE_B0035.5; -.
DR UCSC; B0035.5.1; c. elegans.
DR CTD; 178046; -.
DR WormBase; B0035.5; CE05163; WBGene00007108; gspd-1.
DR eggNOG; KOG0563; Eukaryota.
DR GeneTree; ENSGT00530000063435; -.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; Q27464; -.
DR OMA; VEICVYE; -.
DR OrthoDB; 383995at2759; -.
DR PhylomeDB; Q27464; -.
DR Reactome; R-CEL-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-CEL-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:Q27464; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007108; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..522
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068089"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40..47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207..211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 409..411
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 429..431
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 522 AA; 60215 MW; 7329CC6508B8E378 CRC64;
MACKRHSVSD PISKDLVECL RESMQRDLKF ETPYVFVIFG ASGDLAKKKI YPTLWWLFRD
NLLPVNIKFI GYARSDLTVF KLRESFEKNC KVRENEKCAF DDFIKKCSYV QGQYDTSEGF
QRLQSSIDDF QKESNNQAVN RLYYLALPPS VFNVVSTELK KNCMDHGDSW TRVIIEKPFG
HDLKSSCELS THLAKLFKED QIYRIDHYLG KEMVQNLMVM RFGNRILAPS WNRDHIASVM
ISFKEDFGTG GRAGYFDTAG IIRDVMQNHL MQILTLVAME KPASLNAEDI RDEKVKVLKA
AKVVELKDVV VGQYIASPEF DHPEASQGYK DDKSVPADST TPTYALAVVH INNERWEGVP
FFLRCGKALN EKKAEVRIQF KEVSGDIYPS GELKRSELVM RVQPNEAVYM KLMTKKPGMG
FGVEETELDL TYNNRFKEVR LPDAYERLFL EVFMGSQINF VRTDELEYAW RILTPVLEEL
KKKKVQPVQY KFGSRGPTEG DELMKKYGFI FTGTYKWVAP KL
