GenomeNet

Database: UniProt
Entry: A1A126_BIFAA
LinkDB: A1A126_BIFAA
Original site: A1A126_BIFAA 
ID   A1A126_BIFAA            Unreviewed;       487 AA.
AC   A1A126;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   28-MAR-2018, entry version 84.
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   Name=gnt {ECO:0000313|EMBL:BAF39409.1};
GN   OrderedLocusNames=BAD_0628 {ECO:0000313|EMBL:BAF39409.1};
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 /
OS   NCTC 11814 / E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39409.1, ECO:0000313|Proteomes:UP000008702};
RN   [1] {ECO:0000313|EMBL:BAF39409.1, ECO:0000313|Proteomes:UP000008702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC   {ECO:0000313|Proteomes:UP000008702};
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S.,
RA   Hirai S., Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP009256; BAF39409.1; -; Genomic_DNA.
DR   ProteinModelPortal; A1A126; -.
DR   STRING; 367928.BAD_0628; -.
DR   EnsemblBacteria; BAF39409; BAF39409; BAD_0628.
DR   KEGG; bad:BAD_0628; -.
DR   eggNOG; ENOG4105C7Q; Bacteria.
DR   eggNOG; COG0362; LUCA.
DR   HOGENOM; HOG000255147; -.
DR   KO; K00033; -.
DR   OMA; NSHYPDS; -.
DR   OrthoDB; POG091H01QF; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000008702; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008702};
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:UP000008702}.
FT   DOMAIN      185    478       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND      16     21       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      39     41       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      81     83       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      135    137       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      192    193       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    189    189       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     109    109       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     109    109       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     197    197       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     267    267       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     294    294       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     456    456       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     462    462       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   487 AA;  52788 MW;  29A98C00B816877C CRC64;
     MKGNSMSAEA NVGVVGLAAM GGSLARNLAH HGNKVAVFNR TYARTEKLMN EHGGEGEFYP
     AKTLEEFVDS LVKPRTAIIM VKAGEPTDAM INALADLMEP GDIIVDAGNA YFPDIIRREK
     EISARGLHFV GCGVSGGEEG ALLGPSMMPG GSEESWKTLK PIFESIAAKA EGEPCVTHIG
     LNGAGHFVKM VHNGIEYSDM QLIAESYDLM RRGLGMTPAE IGDVFEEWNK TELDSYLIEI
     TAEVLHQVDK KTGKPLVDLI VDHAGMKGTG TWTVQTALSL AVPVTGIAEA VFARGLSSEA
     DLREEAQKQG FAGPDGKLNL NDDEKKAFIE DIRQALYASK IVAYAQGFNE ITTAAKEYGW
     DIDLAAVARI WRGGCIIRAK FLNRISEAFE SGEANVSLLF APYFKNAIEN AEKSWRNVVA
     QAAINGLPTP AFASSLSYFD GLRSKRLPAA LIQGQRDYFG AHTYQRVDQP GAFHTLWAEP
     GREEIEA
//
DBGET integrated database retrieval system