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Database: UniProt
Entry: A7F5K8_SCLS1
LinkDB: A7F5K8_SCLS1
Original site: A7F5K8_SCLS1 
ID   A7F5K8_SCLS1            Unreviewed;       511 AA.
AC   A7F5K8;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
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=SS1G_12886 {ECO:0000313|EMBL:EDN98029.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98029.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR   EMBL; CH476642; EDN98029.1; -; Genomic_DNA.
DR   RefSeq; XP_001586308.1; XM_001586258.1.
DR   AlphaFoldDB; A7F5K8; -.
DR   STRING; 665079.A7F5K8; -.
DR   GeneID; 5482288; -.
DR   KEGG; ssl:SS1G_12886; -.
DR   VEuPathDB; FungiDB:sscle_02g012100; -.
DR   InParanoid; A7F5K8; -.
DR   OMA; VEICVYE; -.
DR   OrthoDB; 989808at2759; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; 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 {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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312}.
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   511 AA;  58673 MW;  A1E61651AA92355B CRC64;
     MADTVIKPEE SGNAGSLELK DNTVIIVLGA SGDLAKKKTF PALFGLYRNQ FLPKDVRIIG
     YARTKMDHEE YIKRVRSYIK TPTKDMEQQL QEFCDICTYI SGQYDKPEGF IELRKHCEEF
     EKGRKEANRI FYMALPPSVF TTVSQQLKAN TYPETGVARI IVEKPFGKDL GSSRELQKAL
     EPNWKEDEIF RIDHYLGKEM VKNILILRFG NEFFGATWNR NHIDNVQITF KEPFGTEGRG
     GYFDEFGIIR DVMQNHLLQV LTLLAMERPI SFSAEDVRDE KVRVLRGIPA IEPKNVIIGQ
     YGKSLDGTKP SYKEDDTVPK DSRCPTFCAM VAYIKNERWD GVPFILKAGK ALNEQKTEIR
     IQFKDVTSGI FKDIPRNELV MRIQPNESVY IKMNSKLPGL SMQTVVTELD LTYRRRFSDL
     KIPEAYESLI LDALKGDHSN FVRDDELDAS WRIFTPLLHY LDDNKEIIPM EYPYGSRGPA
     VLDDFTSSYG YKFSDAAGYQ WPTTQTAPNK L
//
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