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Database: UniProt
Entry: K9SV54_9SYNE
LinkDB: K9SV54_9SYNE
Original site: K9SV54_9SYNE 
ID   K9SV54_9SYNE            Unreviewed;       471 AA.
AC   K9SV54;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   28-MAR-2018, entry version 36.
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=Syn7502_02026 {ECO:0000313|EMBL:AFY74050.1};
OS   Synechococcus sp. PCC 7502.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY74050.1, ECO:0000313|Proteomes:UP000010385};
RN   [1] {ECO:0000313|EMBL:AFY74050.1, ECO:0000313|Proteomes:UP000010385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY74050.1,
RC   ECO:0000313|Proteomes:UP000010385};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y.,
RA   Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A.,
RA   Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL   Submitted (MAY-2012) 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; CP003594; AFY74050.1; -; Genomic_DNA.
DR   RefSeq; WP_015168707.1; NC_019702.1.
DR   ProteinModelPortal; K9SV54; -.
DR   EnsemblBacteria; AFY74050; AFY74050; Syn7502_02026.
DR   KEGG; synp:Syn7502_02026; -.
DR   PATRIC; fig|1173263.3.peg.2101; -.
DR   KO; K00033; -.
DR   OrthoDB; POG091H01QF; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000010385; 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:UP000010385};
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:UP000010385}.
FT   DOMAIN      179    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      75     77       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      129    131       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      186    187       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    183    183       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    190    190       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     103    103       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     103    103       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     261    261       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     288    288       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     446    446       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     452    452       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   471 AA;  51503 MW;  FFF127182777D879 CRC64;
     MSKQSFGLIG LAVMGENLAL NIERNGFSIA VYNRSREKTD TFMATRAAGK NFKATFSIPE
     FVESLESPRK ILIMVKAGAP VDAVISELKP LLDEGDIIID GGNSLFTDTD RRTIELEKDN
     LQFIGMGVSG GEEGALNGPS MMPGGQKTAY AEIEPIVTKI AAQVDDGACV TYIGPGSAGH
     YVKMVHNGIE YGDMQLIAEA YDLLKTGLGL GAQELHDTFV AWNSTELESF LIEITADIFT
     KIDEETGEPL VEKILDKAGQ KGTGKWTVES AFDLGVPIPT MIAAVTARVA SSYKDERIAA
     SKILGNATGS YTGDRTEFIN AVRDALYCSK ICSYAQGMAL LAAASKAYNY NLNLAEISRI
     WKGGCIIRAG FLDKIKNAYL RNPELKNLLV DPDFTQTIIT KERSWRLVVQ AAAQLGIAVP
     AFSASLSYFD SYRRDRLPQN LTQAQRDYFG AHTYERIDKP AGEFFHTEWT K
//
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