(data stored in ACNUC1104 zone)

SWISSPROT: B1K3Q1_BURCC

ID   B1K3Q1_BURCC            Unreviewed;       470 AA.
AC   B1K3Q1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 82.
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   OrderedLocusNames=Bcenmc03_3620 {ECO:0000313|EMBL:ACA92772.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92772.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) 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:
CC       Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-
CC         phosphate + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58121, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58759; EC=1.1.1.44;
CC         Evidence={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 (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000959; ACA92772.1; -; Genomic_DNA.
DR   RefSeq; WP_006479382.1; NC_010515.1.
DR   EnsemblBacteria; ACA92772; ACA92772; Bcenmc03_3620.
DR   KEGG; bcm:Bcenmc03_3620; -.
DR   HOGENOM; HOG000255147; -.
DR   KO; K00033; -.
DR   OMA; EGEPCVT; -.
DR   BioCyc; BCEN406425:G1GBC-3843-MONOMER; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000002169; Chromosome 2.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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   PANTHER; PTHR11811; PTHR11811; 1.
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;
DR   PRODOM; B1K3Q1.
DR   SWISS-2DPAGE; B1K3Q1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
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, ECO:0000313|EMBL:ACA92772.1};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485}.
FT   DOMAIN      180    470       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND      10     15       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      33     35       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      74     76       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      128    130       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      187    188       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    184    184       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    191    191       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     102    102       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     102    102       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     192    192       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     262    262       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     289    289       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     448    448       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     454    454       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   470 AA;  50944 MW;  0BDC58CA96722195 CRC64;
     MGKQAIGVIG LAVMGRNLAL NIESRGYAVS VFNRSREKTD ELIAEFPGRN LVPTYTLEEF
     VASLETPRRI LMMVKAGEAT DATIASLKPL LEKGDVLIDG GNTHFTDTIR RNQELAQSGL
     HFIGTGVSGG EEGALRGPSI MPGGQRDAYD LVEPILKQIA AKAPSDGEPC VAYMGPDGAG
     HYVKMVHNGI EYGDMQLIAE SYSVLKDVAG LTNDELGAVY TEWNQGELDS YLIEITSKIF
     GKKDEETGKH LVDVILDRAA QKGTGKWTSQ NALDLGVPLP LITESVFARV LSSLKTERVA
     ASKILSGPAA APFDGDRAAF VEAVRRALYL SKVISYAQGF AQLRTASEEY GWNLDLGTIA
     KIFRAGCIIR ARFLQKITDA YAKDPALANL LLDPYFKDIA ANYQTALRDV VVAAVKAGVP
     VPAFASAVAY FDSYRSERLP ANLVQAQRDF FGAHTFERTD KPGSFHANWS
//

If you have problems or comments...

PBIL Back to PBIL home page