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Database: UniProt
Entry: Q2FY60_STAA8
LinkDB: Q2FY60_STAA8
Original site: Q2FY60_STAA8 
ID   Q2FY60_STAA8            Unreviewed;       468 AA.
AC   Q2FY60;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   28-MAR-2018, entry version 92.
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   OrderedLocusNames=SAOUHSC_01605 {ECO:0000313|EMBL:ABD30684.1};
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30684.1, ECO:0000313|Proteomes:UP000008816};
RN   [1] {ECO:0000313|Proteomes:UP000008816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 {ECO:0000313|Proteomes:UP000008816};
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J.
RL   (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
RL   Washington D.C (2006).
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}.
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DR   EMBL; CP000253; ABD30684.1; -; Genomic_DNA.
DR   RefSeq; WP_000193707.1; NC_007795.1.
DR   RefSeq; YP_500120.1; NC_007795.1.
DR   ProteinModelPortal; Q2FY60; -.
DR   SMR; Q2FY60; -.
DR   STRING; 93061.SAOUHSC_01605; -.
DR   EnsemblBacteria; ABD30684; ABD30684; SAOUHSC_01605.
DR   GeneID; 3920021; -.
DR   KEGG; sao:SAOUHSC_01605; -.
DR   PATRIC; fig|93061.5.peg.1461; -.
DR   eggNOG; ENOG4105C7Q; Bacteria.
DR   eggNOG; COG0362; LUCA.
DR   HOGENOM; HOG000255147; -.
DR   KO; K00033; -.
DR   OMA; NSHYPDS; -.
DR   BioCyc; SAUR93061:G1G5Y-1493-MONOMER; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000008816; Chromosome.
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:UP000008816};
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:ABD30684.1};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008816}.
FT   DOMAIN      178    466       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND       9     14       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      32     34       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      73     75       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      127    129       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     101    101       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     101    101       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     259    259       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     286    286       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   468 AA;  51803 MW;  61A5C2CAF3CCD011 CRC64;
     MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV
     NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN
     FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY
     VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK
     LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK
     ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR
     EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF
     SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE
//
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