GenomeNet

Database: UniProt
Entry: A0A2V5IXS6_9EURO
LinkDB: A0A2V5IXS6_9EURO
Original site: A0A2V5IXS6_9EURO 
ID   A0A2V5IXS6_9EURO        Unreviewed;       510 AA.
AC   A0A2V5IXS6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|ARBA:ARBA00020444, ECO:0000256|RuleBase:RU362120};
DE            EC=1.1.1.49 {ECO:0000256|ARBA:ARBA00013019, ECO:0000256|RuleBase:RU362120};
GN   ORFNames=BP00DRAFT_392017 {ECO:0000313|EMBL:PYI33710.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI33710.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI33710.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI33710.1,
RC   ECO:0000313|Proteomes:UP000248817};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025382}.
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:0000256|ARBA:ARBA00000740,
CC         ECO:0000256|RuleBase:RU362120};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000256|ARBA:ARBA00004937, ECO:0000256|RuleBase:RU362120}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|RuleBase:RU362120}.
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; KZ825482; PYI33710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5IXS6; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000248817; Unassembled WGS sequence.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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 {ECO:0000256|RuleBase:RU362120};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW   ECO:0000256|RuleBase:RU362120}; NADP {ECO:0000256|RuleBase:RU362120};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362120}.
FT   DOMAIN          26..203
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          205..493
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ   SEQUENCE   510 AA;  58746 MW;  F555476618327085 CRC64;
     MASTIARTEE RQSAGTAELK DDTVIVVLGA SGDLAKKKTF PALFGLYRNK FLPKGIKIVG
     YARTNMDHEE YLRRVRSYIK TPTKEIEEQL DSFCQFCSYI SGQYDKDDSF INLNKHLEEV
     EKGQKEQNRI FYMALPPSVF TTVSDQLKRN CYPKSGVARI IVEKPFGKDL QSSRDLQKAL
     DPNWKEEEIF RIDHYLGKEM VKNILIMRFG NEFFNATWNR HHIDNVQITF KEPFGTEGRG
     GYFDEFGIIR DVMQNHLLQV LTLLAMERPI SFSAEDIRDE KVRVLRAMDA IEPKNVIIGQ
     YGKSLDGSKP AYKEDETVPQ DSRCPTFCAM VAYIKNERWD GVPFILKAGK ALNEQKTEIR
     IQFRDVTSGI FKDIPRNELV IRVQPNESVY IKMNSKLPGL SMQTVVTELD LTYRRRFSDL
     KIPEAYESLI LDALKGDHSN FVRDDELDAS WRIFTPLLHY LDDNKEIIPM EYPYGSRGPA
     VLDDFTASFG YKFSDAAGYQ WPLTSTPNRL
//
DBGET integrated database retrieval system