G6PD_DICDI
ID G6PD_DICDI Reviewed; 497 AA.
AC Q557D2; Q869V9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
GN Name=g6pd-1; Synonyms=zwf; ORFNames=DDB_G0273131;
GN and
GN Name=g6pd-2; Synonyms=zwf; ORFNames=DDB_G0273639;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AAFI02000009; EAL70783.1; -; Genomic_DNA.
DR EMBL; AAFI02000011; EAL70510.1; -; Genomic_DNA.
DR RefSeq; XP_644436.1; XM_639344.1.
DR RefSeq; XP_644814.1; XM_639722.1.
DR AlphaFoldDB; Q557D2; -.
DR SMR; Q557D2; -.
DR STRING; 44689.DDB0231285; -.
DR PaxDb; Q557D2; -.
DR EnsemblProtists; EAL70510; EAL70510; DDB_G0273639.
DR EnsemblProtists; EAL70783; EAL70783; DDB_G0273131.
DR GeneID; 8618916; -.
DR GeneID; 8619061; -.
DR KEGG; ddi:DDB_G0273131; -.
DR KEGG; ddi:DDB_G0273639; -.
DR dictyBase; DDB_G0273131; g6pd-1.
DR dictyBase; DDB_G0273639; g6pd-2.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; Q557D2; -.
DR OMA; PDEGIQM; -.
DR PhylomeDB; Q557D2; -.
DR Reactome; R-DDI-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DDI-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:Q557D2; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
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..497
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000312855"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 17..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181..185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 497 AA; 56697 MW; 5ECF966E8C5AA31A CRC64;
MTSTPDSRSV LTVIILGASG DLAKKKTYPA LFGLYLRDLL PSNTIIYGYA RSHIEIGDFK
ARISKGLKGD EEKKKQFLNL LHYHSGKYDE KASYDEFEKL ILAEEKKQQG VDKFNRLFYM
AIPPSIFIEV SIGIHGSLIS KNGWSRVIVE KPFGRDLASS RELVSELGKL FKEKDLFRID
HYLGKEMVQN LMVLRFANAV FEPLWSKSHI SSITITFKED IGTEGRGGYF DQFGIIRDVM
QNHLLQVLSL VAMEPPVSLN ADDITNEKVK LLRCIQPIKM SEVVLGQYTS DPEGKIPAYL
DDEGVPKDST TPTYAAAVFH INNPRWRGMP FILKCGKALD ERKTEVRIQF KRPDNFLFSD
DDISRNELVM RIQPGEAVYL KLLSKKPGLE NKIEQTELDL SYRHRFENLD LPDAYERLIL
DSIKGDHNLF VRDDELDVAW QIFTPLLDQI EKEKIKPEPY SFGSRGPKSA DELSKKFGFI
RSLGYNWPGN SPQGSKK
