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Database: UniProt
Entry: A0A150X4Y1_9BACT
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ID   A0A150X4Y1_9BACT        Unreviewed;       467 AA.
AC   A0A150X4Y1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-NOV-2017, entry version 10.
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=AWW68_13820 {ECO:0000313|EMBL:KYG73753.1};
OS   Roseivirga spongicola.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Roseivirga.
OX   NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG73753.1, ECO:0000313|Proteomes:UP000075606};
RN   [1] {ECO:0000313|EMBL:KYG73753.1, ECO:0000313|Proteomes:UP000075606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG73753.1,
RC   ECO:0000313|Proteomes:UP000075606};
RA   Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G.,
RA   Chong C.S.;
RT   "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL   Submitted (JAN-2016) 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   -!- 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:KYG73753.1}.
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DR   EMBL; LRPC01000028; KYG73753.1; -; Genomic_DNA.
DR   RefSeq; WP_068222548.1; NZ_LRPC01000028.1.
DR   EnsemblBacteria; KYG73753; KYG73753; AWW68_13820.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000075606; 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; 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:UP000075606};
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:UP000075606}.
FT   DOMAIN      180    466       6PGD. {ECO:0000259|SMART:SM01350}.
FT   REGION      130    132       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     104    104       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     444    444       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     450    450       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   467 AA;  51587 MW;  DA309B49E179BE15 CRC64;
     MSEAKFDFGL IGLGVMGKNF ILNVADNGFS AIGYDLDQEK VDALKRESQN GMASATTDKL
     QFIRSLKTPR KVMFLVPSGA PVDSVIDDLM PFLDKGDLLI DGGNSYFLDT ERRVTKLKNS
     EINFLGLGIS GGAKGARKGP SMMAGGDNDV YELISPILES VSAKVNDEPC VARVGDNSAG
     HYVKMVHNGI EYGLMQLIAE TYDLAKFGLG LSNKEQAELF SGFNEGKLKS YLIEITADIF
     TKKDDLSPKD LIDVISDRAK QKGTGKWISQ NAMDIGIPIP AIDSSVSMRV LSSFKEERQK
     AALVYPKSQS DPSRFTKTDL EKALYFSFIV TFAQGMRQLL EASSKYQYGL DLAEIAKIWR
     GGCIIRAELL EHIREAFSDS SNKEHLLFDA YIISEIKELL PSVNRVISVA HNAGIAVSGM
     SASLNYFNAF RSEKLPLNLI QAQRDYFGGH TYERLDKPGI FHTEWED
//
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