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Database: UniProt
Entry: A0A135HS71_9RHIZ
LinkDB: A0A135HS71_9RHIZ
Original site: A0A135HS71_9RHIZ 
ID   A0A135HS71_9RHIZ        Unreviewed;       473 AA.
AC   A0A135HS71;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-NOV-2017, entry version 9.
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=ATN84_14065 {ECO:0000313|EMBL:KXF76047.1};
OS   Paramesorhizobium deserti.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Paramesorhizobium.
OX   NCBI_TaxID=1494590 {ECO:0000313|EMBL:KXF76047.1, ECO:0000313|Proteomes:UP000070107};
RN   [1] {ECO:0000313|EMBL:KXF76047.1, ECO:0000313|Proteomes:UP000070107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-3-E {ECO:0000313|EMBL:KXF76047.1,
RC   ECO:0000313|Proteomes:UP000070107};
RA   Lv R., Yang X., Fang N., Guo J., Luo X., Peng F., Yang R., Cui Y.,
RA   Fang C., Song Y.;
RT   "Draft genome sequence of Paramesorhizobium deserti A-3-E, a strain
RT   highly resistant to diverse beta-lactam antibiotics.";
RL   Submitted (NOV-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:KXF76047.1}.
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DR   EMBL; LNTU01000034; KXF76047.1; -; Genomic_DNA.
DR   RefSeq; WP_068882789.1; NZ_LNTU01000034.1.
DR   EnsemblBacteria; KXF76047; KXF76047; ATN84_14065.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000070107; 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:UP000070107};
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:KXF76047.1};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070107}.
FT   DOMAIN      180    469       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      76     78       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
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       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
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     447    447       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     453    453       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   473 AA;  50274 MW;  BBB3F5DDD25DCF81 CRC64;
     MEKADIGLIG LGVMGANLAL NIAEKGYRIA VYNRTTEKTH EFHENAGELK DRIIPCDTLE
     QLVGSIRAPR PIILMIKAGD PVDHEIKALK PLLMRDDIII DAGNANFHDT VRRLNSLGTD
     DPTFVGMGVS GGEEGARHGP SIMVGGTKEA YDRISPVLTA IAAKYQGEPC CALLGPDGAG
     HFVKTIHNGI EYADMQMIAE IYGILRDGLG LSAPAIGSVF SKWNDGPLNS YLIEITAKVL
     LAVDPETGKA AVDVILDSAG QKGTGRWSAI EAQMLGVPAT GIEAAVAARS LSALKAERQV
     AEKAYPSGGA ALSPQDRAHF IDDLEQGLLA GKIAAYAQGF AVMAAASKEY QWNLPLATTA
     RIWRAGCIIR SQFLDVIAEA FDKGAPENLL LAPAFIERMT KGSAALRAVV STAALSGLPV
     PALSAALSYF DSYRQARGTA NLIQAQRDFF GAHGFKRLDR EGDFHGPWSD IGA
//
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