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Database: UniProt
Entry: P37756
LinkDB: P37756
Original site: P37756 
ID   6PGD_SHIFL              Reviewed;         468 AA.
AC   P37756;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   14-MAY-2014, entry version 106.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=gnd; OrderedLocusNames=SF2091, S2212;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PE577 / Serotype 2a;
RX   PubMed=7507920;
RA   Morona R., Mavris M., Fallarino A., Manning P.A.;
RT   "Characterization of the rfc region of Shigella flexneri.";
RL   J. Bacteriol. 176:733-747(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-456.
RC   STRAIN=ATCC 29903;
RX   PubMed=7937867; DOI=10.1073/pnas.91.21.10227;
RA   Nelson K., Selander R.K.;
RT   "Intergeneric transfer and recombination of the 6-phosphogluconate
RT   dehydrogenase gene (gnd) in enteric bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC       5-phosphate + CO(2) + NADPH.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 3/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family.
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DR   EMBL; X71970; CAA50781.1; -; Genomic_DNA.
DR   EMBL; AE005674; AAN43630.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17458.1; -; Genomic_DNA.
DR   EMBL; U14468; AAC43834.1; -; Genomic_DNA.
DR   RefSeq; NP_707923.1; NC_004337.2.
DR   RefSeq; NP_837649.1; NC_004741.1.
DR   ProteinModelPortal; P37756; -.
DR   SMR; P37756; 1-466.
DR   STRING; 198214.SF2091; -.
DR   PaxDb; P37756; -.
DR   EnsemblBacteria; AAN43630; AAN43630; SF2091.
DR   EnsemblBacteria; AAP17458; AAP17458; S2212.
DR   GeneID; 1025304; -.
DR   GeneID; 1078514; -.
DR   KEGG; sfl:SF2091; -.
DR   KEGG; sfx:S2212; -.
DR   PATRIC; 18705945; VBIShiFle31049_2451.
DR   eggNOG; COG0362; -.
DR   HOGENOM; HOG000255147; -.
DR   KO; K00033; -.
DR   OMA; DKDGVFH; -.
DR   OrthoDB; EOG6MSS4W; -.
DR   UniPathway; UPA00115; UER00410.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   Gene3D; 1.20.5.320; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_decarbox.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR012284; Fibritin/6PGD_C-extension.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000109; 6PGD; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   TIGRFAMs; TIGR00873; gnd; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Gluconate utilization; NADP; Oxidoreductase;
KW   Pentose shunt.
FT   CHAIN         1    468       6-phosphogluconate dehydrogenase,
FT                                decarboxylating.
FT                                /FTId=PRO_0000090050.
FT   NP_BIND      10     15       NADP (By similarity).
FT   NP_BIND      33     35       NADP (By similarity).
FT   NP_BIND      74     76       NADP (By similarity).
FT   REGION      128    130       Substrate binding (By similarity).
FT   REGION      186    187       Substrate binding (By similarity).
FT   ACT_SITE    183    183       Proton acceptor (By similarity).
FT   ACT_SITE    190    190       Proton donor (By similarity).
FT   BINDING     102    102       NADP (By similarity).
FT   BINDING     102    102       Substrate (By similarity).
FT   BINDING     191    191       Substrate (By similarity).
FT   BINDING     260    260       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     287    287       Substrate (By similarity).
FT   BINDING     445    445       Substrate; shared with dimeric partner
FT                                (By similarity).
FT   BINDING     451    451       Substrate; shared with dimeric partner
FT                                (By similarity).
SQ   SEQUENCE   468 AA;  51344 MW;  2203A0D82120CD61 CRC64;
     MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LAPYYTVKEF
     VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF
     NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH
     YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL SNEELAQTFT EWNNGELSSY LIDITKDIFT
     KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS
     KVLSGPQAQS AGDKAEFIEK VRSALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF
     RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT
     FAAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD
//
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