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 01-MAY-2013, entry version 103.
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; KQQIGVI; -.
DR ProtClustDB; PRK09287; -.
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; 6DGDH_C_like; 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
//
