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Entry: A0A099WHN2_9LIST
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ID   A0A099WHN2_9LIST        Unreviewed;       472 AA.
AC   A0A099WHN2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   28-MAR-2018, entry version 20.
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=EP56_06615 {ECO:0000313|EMBL:KGL45224.1};
OS   Listeriaceae bacterium FSL A5-0209.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae.
OX   NCBI_TaxID=1497679 {ECO:0000313|EMBL:KGL45224.1, ECO:0000313|Proteomes:UP000029855};
RN   [1] {ECO:0000313|EMBL:KGL45224.1, ECO:0000313|Proteomes:UP000029855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL A5-0209 {ECO:0000313|EMBL:KGL45224.1,
RC   ECO:0000313|Proteomes:UP000029855};
RA   den Bakker H.C.;
RT   "Novel Listeriaceae from food processing plants.";
RL   Submitted (MAY-2014) 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:KGL45224.1}.
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DR   EMBL; JNEZ01000011; KGL45224.1; -; Genomic_DNA.
DR   RefSeq; WP_036094000.1; NZ_JNEZ01000011.1.
DR   EnsemblBacteria; KGL45224; KGL45224; EP56_06615.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000029855; 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:UP000029855};
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:UP000029855}.
FT   DOMAIN      178    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      74     76       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      128    130       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      185    186       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    182    182       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    189    189       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     102    102       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     102    102       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     260    260       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     287    287       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   472 AA;  52080 MW;  794FF24B277F1C72 CRC64;
     MAKQEIGVIG MGVMGRNLAL NIESRGYSVS IFNRSSEKTK AVAEEHSDKK LVPTYNLEEF
     VNSIEVPRRI LLMVQAGAAT DMMIDAVKPF LSQGDILIDG GNTFFKDTIR RNKTLSEEGF
     NFIGTGVSGG EEGALKGPSI MPGGQRKAYD LVAPILQEIA AVADGEPCVT YIGPDGAGHY
     VKMVHNGIEY GDMQLIAEAY TILKQIGGLT NDELADVFTE WNDGELDSYL IQITKNIVKT
     KDPETGKPIV DVILDKAGQK GTGKWTSQSA LDLGVPLSLI TESVFARYIS ALKEERVHAS
     TVLSGPSNYS FNGDKKAFVE SVRRALYFSK IASYAQGFAQ MKAASDEYEW DLQYGEIAKI
     FRAGCIIRAR FLQKITDAYN NDKNLNNLLL DPYFKDIAHN YQDALREVVA ESVKAGIPVP
     TFTAAISYYD SYRSEVLSAN LIQAQRDYFG AHTYERVDKA GTFHTEWPEI DE
//
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