ID   G6PD_EMENI              Reviewed;         511 AA.
AC   P41764; C8VIZ3; Q5B8Z9; Q92408;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, 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=gsdA; Synonyms=g6pD; ORFNames=AN2981;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RA   Schaap P.J., Muller Y., Visser J.;
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WG096;
RA   van den Broek P., Goosen T., Wennekes B., van den Broek H.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC       phosphate pathway, which represents a route for the dissimilation of
CC       carbohydrates besides glycolysis. The main function of this enzyme is
CC       to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC       and nucleic acid synthesis (By similarity).
CC       {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   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X84001; CAA58825.1; -; Genomic_DNA.
DR   EMBL; X77830; CAA54841.1; -; Genomic_DNA.
DR   EMBL; AACD01000051; EAA63552.1; -; Genomic_DNA.
DR   EMBL; BN001306; CBF83624.1; -; Genomic_DNA.
DR   RefSeq; XP_660585.1; XM_655493.1.
DR   AlphaFoldDB; P41764; -.
DR   SMR; P41764; -.
DR   STRING; 227321.P41764; -.
DR   EnsemblFungi; CBF83624; CBF83624; ANIA_02981.
DR   GeneID; 2874290; -.
DR   KEGG; ani:AN2981.2; -.
DR   VEuPathDB; FungiDB:AN2981; -.
DR   eggNOG; KOG0563; Eukaryota.
DR   HOGENOM; CLU_013524_2_3_1; -.
DR   InParanoid; P41764; -.
DR   OMA; ERAGYYE; -.
DR   OrthoDB; 989808at2759; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000000560; Chromosome VI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:AspGD.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR00871; zwf; 1.
DR   PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..511
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068103"
FT   ACT_SITE        256
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P11411"
FT   BINDING         29..36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         63
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         164
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         194..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   CONFLICT        15..20
FT                   /note="Missing (in Ref. 1; CAA58825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76..85
FT                   /note="RSYIKTPTKE -> DTLRPRQRK (in Ref. 1; CAA58825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="L -> LP (in Ref. 1; CAA58825)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  58977 MW;  66BC15B72878A475 CRC64;
     MSATIARAEE QQNGSTVELK DDTVIVVLGA SGDLAKKKTF PALFGLFRNK FLPKGIKIVG
     YARTQMDHNE YLKRVRSYIK TPTKEIEEQL NSFCELCTYI SGQYDQDDSF KNLAKHLEEI
     EKNQKEQNRV FYMALPPSVF ITVSEQLKRN CYPKNGVARI IVEKPFGKDL QSSRDLQKAL
     EPNWKEEEIF RIDHYLGKEM VKNILIMRFG NEFFNATWNR HHIDNVQITF KEPFGTEGRG
     GYFDEFGIIR DVMQNHLLQV LTLLAMERPI SFSAEDIRDE KVRVLRAMDP IQPKDVIIGQ
     YGRSLDGSKP AYKEDDTVPQ DSRCPTFCAL VAHIKNERWD GVPFIMKAGK ALNEQKTEIR
     IQFKDVTSGI FKDIPRNELV IRVQPNESVY IKMNSKLPGL SMQTVVTELD LTYRRRFSDL
     KIPEAYESLI LDALKGDHSN FVRDDELDAS WRMFTPLLHY LDDNKEIIPM EYPYGSRGPS
     VLDDFTASYG YKFSDAAGYQ WPLTHTTPNR L
//