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   27-MAR-2024, entry version 160.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=gnd; OrderedLocusNames=SF2091, S2212;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PE577 / Serotype 2a;
RX   PubMed=7507920; DOI=10.1128/jb.176.3.733-747.1994;
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., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., 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., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   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-phosphogluconate
CC       to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC       to NADPH. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC         + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       3/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000305}.
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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; WP_000043429.1; NZ_WPGW01000112.1.
DR   AlphaFoldDB; P37756; -.
DR   SMR; P37756; -.
DR   STRING; 198214.SF2091; -.
DR   PaxDb; 198214-SF2091; -.
DR   GeneID; 1025304; -.
DR   KEGG; sfl:SF2091; -.
DR   KEGG; sfx:S2212; -.
DR   PATRIC; fig|198214.7.peg.2501; -.
DR   HOGENOM; CLU_024540_4_2_6; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
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:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR00873; gnd; 1.
DR   PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 1.
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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW   Reference proteome.
FT   CHAIN           1..468
FT                   /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT                   /id="PRO_0000090050"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         33..35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         74..76
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..130
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
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
//