G6PD_ASPNG
ID G6PD_ASPNG Reviewed; 510 AA.
AC P48826;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=g6pdh;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RA Thamm A.;
RT "G6PD-promoter activity in A. niger.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=7753033; DOI=10.1007/bf00705654;
RA van den Broek P., Goosen T., Wennekes B., van den Broek H.;
RT "Isolation and characterization of the glucose-6-phosphate dehydrogenase
RT encoding gene (gsdA) from Aspergillus niger.";
RL Mol. Gen. Genet. 247:229-239(1995).
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; X87942; CAA61194.1; -; mRNA.
DR EMBL; X77829; CAA54840.1; -; Genomic_DNA.
DR PIR; S54720; S54720.
DR AlphaFoldDB; P48826; -.
DR SMR; P48826; -.
DR STRING; 5061.CADANGAP00002664; -.
DR PRIDE; P48826; -.
DR VEuPathDB; FungiDB:An02g12140; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1145051; -.
DR VEuPathDB; FungiDB:ATCC64974_53050; -.
DR VEuPathDB; FungiDB:M747DRAFT_293654; -.
DR eggNOG; KOG0563; Eukaryota.
DR UniPathway; UPA00115; UER00408.
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 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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase.
FT CHAIN 1..510
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068102"
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 135
FT /note="L -> F (in Ref. 2; CAA54840)"
FT /evidence="ECO:0000305"
FT CONFLICT 508..510
FT /note="NRL -> TVCK (in Ref. 2; CAA54840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 58950 MW; FDDF3F5025483AF6 CRC64;
MASTIARTEE RQNAGTMELK DDTVIIVLGA SGDLAKKKTF PALFGLYRNK FLPKGIKIVG
YARTNMDHEE YLRRVRSYIK TPTKEIEEQL DSFCQFCTYI SGQYDKDDSF INLNKHLEEI
EKGQKEQNRI YYMALPPSVF TTVSDQLKRN CYPKNGVARI IVEKPFGKDL QSSRDLQKAL
EPNWKEEEIF RIDHYLGKEM VKNILIMRFG NEFFNATWNR HHIDNVQITF KEPFGTEGRG
GYFDEFGIIR DVMQNHLLQV LTLLAMERPI SFSAEDIRDE KVRVLRAMDA IEPKNVIIGQ
YGKSLDGSKP AYKEDETVPQ DSRCPTFCAM VAYIKNERWD GVPFIMKAGK ALNEQKTEIR
IQFRDVTSGI FKDIPRNELV IRVQPNESVY IKMNSKLPGL SMQTVVTELD LTYRRRFSDL
KIPEAYESLI LDALKGDHSN FVRDDELDAS WRIFTPLLHY LDDNKEIIPM EYPYGSRGPA
VLDDFTASFG YKFSDAAGYQ WPLTSTPNRL
