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Database: UniProt
Entry: K2FL83_9BACI
LinkDB: K2FL83_9BACI
Original site: K2FL83_9BACI 
ID   K2FL83_9BACI            Unreviewed;       469 AA.
AC   K2FL83;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   28-MAR-2018, entry version 34.
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=MJ3_06318 {ECO:0000313|EMBL:EKE31731.1};
OS   Salimicrobium jeotgali.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX   NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE31731.1, ECO:0000313|Proteomes:UP000011746};
RN   [1] {ECO:0000313|EMBL:EKE31731.1, ECO:0000313|Proteomes:UP000011746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ3 {ECO:0000313|EMBL:EKE31731.1,
RC   ECO:0000313|Proteomes:UP000011746};
RX   PubMed=23144427; DOI=10.1128/JB.01808-12;
RA   Lee S.H., Jung J.Y., Jeon C.O.;
RT   "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT   Myulchi-Jeot, Korean Fermented Seafood.";
RL   J. Bacteriol. 194:6695-6695(2012).
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   -!- 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:EKE31731.1}.
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DR   EMBL; AMPQ01000007; EKE31731.1; -; Genomic_DNA.
DR   RefSeq; WP_008589507.1; NZ_CP011361.2.
DR   ProteinModelPortal; K2FL83; -.
DR   EnsemblBacteria; EKE31731; EKE31731; MJ3_06318.
DR   KEGG; sje:AAV35_008075; -.
DR   PATRIC; fig|1230341.3.peg.1309; -.
DR   KO; K00033; -.
DR   OrthoDB; POG091H01QF; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000011746; Unassembled WGS sequence.
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:UP000011746};
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:EKE31731.1};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011746}.
FT   DOMAIN      179    468       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   469 AA;  52198 MW;  697C58DC62034D7C CRC64;
     MSGNQFGVIG LAVMGKNLAM NVESRGYSVS VFNRTFEKTE EFVNNEVKGR NFTGTETVEE
     FVASLEKPRK IMLMVKAGPA TDATIQSLLP HLDKGDVLID GGNTLYEETM RRNEELAESG
     IHFIGTGVSG GEEGALKGPS IMPGGQKEAY ELVRPIFEDI SAKVNGDPCT TYIGPDGAGH
     FVKMVHNGIE YGDMQLISEA YHLLKDVAGM DDTELHETFK KWNEGELDSY LMEITADIFT
     KKDEETGKPM VDVILDSAGQ KGTGKWTSKN ALDLGVPLPL ITEAVFARFI SSLKEERVAA
     SKVFSGPEIS FEEDREELIE AIRKALYMSK ICSYAQGFAQ MRKASDENGW ELKYGDIAMI
     WRGGCIIRAG FLQKIKEAYD RDPDLDNLLL DDYFRNIVES YQDALRTVVS IAVKNGIPVP
     TLQSAIAYYD SYRTADLPAN LIQAQRDYFG AHTYQRKDKE GTFHTEWLK
//
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