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Database: UniProt
Entry: A0A0D8D2J7_9GAMM
LinkDB: A0A0D8D2J7_9GAMM
Original site: A0A0D8D2J7_9GAMM 
ID   A0A0D8D2J7_9GAMM        Unreviewed;       513 AA.
AC   A0A0D8D2J7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-MAR-2018, entry version 18.
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=SG35_05550 {ECO:0000313|EMBL:KJE42710.1};
OS   Thalassomonas actiniarum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassomonas.
OX   NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE42710.1, ECO:0000313|Proteomes:UP000032568};
RN   [1] {ECO:0000313|EMBL:KJE42710.1, ECO:0000313|Proteomes:UP000032568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A5K-106 {ECO:0000313|EMBL:KJE42710.1,
RC   ECO:0000313|Proteomes:UP000032568};
RA   Olonade I., van Zyl L.J., Tuffin M.I.;
RT   "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT   actiniarum.";
RL   Submitted (JAN-2015) 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:KJE42710.1}.
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DR   EMBL; JYNI01000010; KJE42710.1; -; Genomic_DNA.
DR   RefSeq; WP_044831405.1; NZ_JYNI01000010.1.
DR   EnsemblBacteria; KJE42710; KJE42710; SG35_05550.
DR   PATRIC; fig|485447.4.peg.349; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000032568; 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:UP000032568};
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:UP000032568}.
FT   DOMAIN      206    499       6PGD. {ECO:0000259|SMART:SM01350}.
FT   REGION      138    140       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      213    214       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    210    210       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    217    217       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     113    113       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     218    218       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     288    288       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     315    315       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     475    475       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     481    481       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   513 AA;  55988 MW;  AE53D60A16D3CDE0 CRC64;
     MTRDTVLCDI GFIGLGVMGK NLVLNLADNG YKIAAFDLSS EKVNDVILQD QQENNSDIPR
     VHGCSSYTEL LSQLKPPHLI VLSVPAGAPV DQVCENLIGA GIGADDIVID TGNSLWMDTV
     AREQKYKNNF ILFSSAVSGG EVGARFGPAL MPSGSAYAWT RIKPIWEAIS AKVDPHTGKP
     LERTKPGQVI NEGDPCAAYI GPAGAGHYVK MVHNGIEYAD MQIIGEAYHI LRSGLGLSTD
     DIADIFEKWH QGPLDSYLME ITVEVLRQKS SDTGTSLVDL ILDKAGQKGT GLWTAVSSLE
     VGCPAPTISQ AVYARSISSF KDFRVQAAQK LSGPQAVSFT AEEQTAFIDR LHDAIYSAKI
     CVYAQGFQLM KLAAKEHNWT LNFASIAKIW RAGCIIRAVF LQPITEAFER NEDLDNLLLD
     DFFAGQLNEH QGNWRKSVAD ATLLGIPVGA LSSALSYYDS MRAEVLPANL LQGQRDFFGA
     HTFERVDKPA GKKYHVQWSS PERKTVEIPP VQK
//
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