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Database: UniProt
Entry: B5HBT9_STRPR
LinkDB: B5HBT9_STRPR
Original site: B5HBT9_STRPR 
ID   B5HBT9_STRPR            Unreviewed;       480 AA.
AC   B5HBT9;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   22-NOV-2017, entry version 61.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
GN   ORFNames=SSDG_02622 {ECO:0000313|EMBL:EDY64300.1};
OS   Streptomyces pristinaespiralis ATCC 25486.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=457429 {ECO:0000313|EMBL:EDY64300.1, ECO:0000313|Proteomes:UP000002805};
RN   [1] {ECO:0000313|Proteomes:UP000002805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25486 {ECO:0000313|Proteomes:UP000002805};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A.,
RA   Heiman D., Hepburn T., Sykes S., Alvarado L., Kodira C.D.,
RA   Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., Walker S.,
RA   Walsh C.T., Lander E., Galagan J., Nusbaum C., Birren B.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDY64300.1, ECO:0000313|Proteomes:UP000002805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25486 {ECO:0000313|EMBL:EDY64300.1,
RC   ECO:0000313|Proteomes:UP000002805};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P.,
RA   Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA   Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces pristinaespiralis strain ATCC
RT   25486.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-
CC       phosphogluconate to ribulose 5-phosphate and CO(2), with
CC       concomitant reduction of NADP to NADPH.
CC       {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC       5-phosphate + CO(2) + NADPH. {ECO:0000256|PIRNR:PIRNR000109,
CC       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|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
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DR   EMBL; CM000950; EDY64300.1; -; Genomic_DNA.
DR   RefSeq; WP_005308508.1; NZ_CM000950.1.
DR   ProteinModelPortal; B5HBT9; -.
DR   STRING; 457429.SSDG_02622; -.
DR   EnsemblBacteria; EDY64300; EDY64300; SSDG_02622.
DR   eggNOG; ENOG4105C7Q; Bacteria.
DR   eggNOG; COG0362; LUCA.
DR   OrthoDB; POG091H01QF; -.
DR   BioCyc; SPRI457429:G12J3-473-MONOMER; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000002805; Chromosome.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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:UP000002805};
KW   Gluconate utilization {ECO:0000256|RuleBase:RU000485};
KW   NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002805}.
FT   DOMAIN      181    471       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND      11     16       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      34     36       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      76     78       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      130    132       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      188    189       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    185    185       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    192    192       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     104    104       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     104    104       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     193    193       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     263    263       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     290    290       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     449    449       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     455    455       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   480 AA;  51658 MW;  8390175F9EFC4F81 CRC64;
     MSGTAQIGVT GLAVMGRNLA RNFARNGFTV AVHNRTAART RALVEEFGDE GTFVAAESPE
     EFVAALERPR RLVIMVKAGE PTDAVIEEFA PLLEEGDVII DGGNAHFADT RRREKELRER
     GIHFVGVGIS GGEEGALHGP SIMPGGSAES YASLGPLLER IAAKAPDGTP CVTHVGPDGA
     GHFVKMVHNG IEYADMQLIA EAYHLLRTVA GYSPAQIAET FRTWNRGRLD SYLIEITAEV
     LAHTDADTGE PFVDIVMDQA EQKGTGRWTV QIALDLGVPV SGIAEAVFAR SLSGHAGLRE
     VSRSLPGPQP RALDAEAAGR FADRVEQALY ASKIVSYTQG FHQVQAGSEA YGWDVDAGSV
     AAIWRAGCII RAAFLDRIRG AYDEQRDLPS LLADKQFAEE IGAAQDDWRD VVATAVREGV
     PTPGFAAALA YYDALRAERL PAALTQGQRD FFGAHTYRRT DREGSFHTLW GGDRSEVASD
//
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