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Database: UniProt
Entry: A0A0A2WLM1_BEABA
LinkDB: A0A0A2WLM1_BEABA
Original site: A0A0A2WLM1_BEABA 
ID   A0A0A2WLM1_BEABA        Unreviewed;       456 AA.
AC   A0A0A2WLM1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   23-MAY-2018, entry version 17.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN   ORFNames=BBAD15_g46 {ECO:0000313|EMBL:KGQ14014.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ14014.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ14014.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ14014.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J.,
RA   Lu Y., Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC       5-phosphate + CO(2) + NADPH. {ECO:0000256|RuleBase:RU000485}.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 3/3. {ECO:0000256|RuleBase:RU000485}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU000485}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGQ14014.1}.
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DR   EMBL; ANFO01000005; KGQ14014.1; -; Genomic_DNA.
DR   EnsemblFungi; KGQ14014; KGQ14014; BBAD15_g46.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0050661; F:NADP binding; IEA:EnsemblFungi.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0061688; P:glycolytic process via Entner-Doudoroff Pathway; IEA:EnsemblFungi.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:EnsemblFungi.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000109; 6PGD; 1.
DR   PRINTS; PR00076; 6PGDHDRGNASE.
DR   SMART; SM01350; 6PGD; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00873; gnd; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030106};
KW   Gluconate utilization {ECO:0000256|RuleBase:RU000485};
KW   NADP {ECO:0000256|RuleBase:RU000485};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000485};
KW   Pentose shunt {ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT   DOMAIN      166    455       6PGD. {ECO:0000259|SMART:SM01350}.
FT   REGION      115    117       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      173    174       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    170    170       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    177    177       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING      89     89       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     178    178       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     247    247       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     274    274       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     433    433       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     439    439       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   456 AA;  50255 MW;  5CD8E8E9C9290F50 CRC64;
     MGRNLALNIE SRGYTVSVFN RSREKTEEVV AENPGKKLVP YYTVKEFVES LETPRRILLM
     VQAGAGTDAA IDSLKPYLDK GDIIIDGGNT FFQDTIRRNR DLSAEGFNFI GTGVSGGEEG
     ALKGPSIMPG GQKDAYELVA PILTKIAAVA EDGEPCVTYI GPDGAGHYVK MVHNGIEYGD
     MQLIAEAYSL LKHGLNLSNE ELAETFTEWN KGELSSYLID ITKDIFTKKD EEGKYLVDVI
     LDEAANKGTG KWTSQSSLDL GEPLSLITES VFARYISSLK EQRVAASKVL SGPQAKPFSG
     DKAEFSEKVR RALYLGKIVS YAQGFSQLRA ASEENNWDLN YGEIAKIFRA GCIIRAQFLQ
     KITDAYAETP AIANLLLAPY FKKIADGYQQ ALRDVISYAV QNGIPTPTFS AAIAYYDSYR
     AAVLPANLIQ AQRDYFGAHT YKRTDKEGVF HTEWLD
//
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