ID 6PGD_SALTY Reviewed; 468 AA.
AC P14062;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 01-MAY-2013, entry version 111.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=gnd; OrderedLocusNames=STM2081;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2671649; DOI=10.1007/BF00330960;
RA Reeves P., Stevenson G.;
RT "Cloning and nucleotide sequence of the Salmonella typhimurium LT2 gnd
RT gene and its homology with the corresponding sequence of Escherichia
RT coli K12.";
RL Mol. Gen. Genet. 217:182-184(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1938920;
RA Dykhuizen D.E., Green L.;
RT "Recombination in Escherichia coli and the definition of biological
RT species.";
RL J. Bacteriol. 173:7257-7268(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA Waterston R., Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RC STRAIN=LT2;
RX PubMed=1710759; DOI=10.1111/j.1365-2958.1991.tb00741.x;
RA Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.;
RT "Structure and sequence of the rfb (O antigen) gene cluster of
RT Salmonella serovar typhimurium (strain LT2).";
RL Mol. Microbiol. 5:695-713(1991).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X15651; CAA33677.1; -; Genomic_DNA.
DR EMBL; M64332; AAA27137.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20985.1; -; Genomic_DNA.
DR EMBL; X56793; CAA40131.1; -; Genomic_DNA.
DR PIR; S04397; S04397.
DR RefSeq; NP_461026.1; NC_003197.1.
DR ProteinModelPortal; P14062; -.
DR SMR; P14062; 1-466.
DR STRING; 99287.STM2081; -.
DR PaxDb; P14062; -.
DR PRIDE; P14062; -.
DR EnsemblBacteria; AAL20985; AAL20985; STM2081.
DR GeneID; 1253602; -.
DR KEGG; stm:STM2081; -.
DR PATRIC; 32382745; VBISalEnt20916_2203.
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; Reference proteome.
FT CHAIN 1 468 6-phosphogluconate dehydrogenase,
FT decarboxylating.
FT /FTId=PRO_0000090047.
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; 51395 MW; D8EBB53A2DAADBF7 CRC64;
MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK LVPYYTVKEF
VESLETPRRI LLMVKAGAGT DAAIDSLKPY LEKGDIIIDG GNTFFQDTIR RNRELSAEGF
NFIGTGVSGG EEGALKGPSI MPGGQKDAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH
YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL SNEELANTFT EWNNGELSSY LIDITKDIFT
KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKAQRVAAS
KVLSGPKAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYHWD LNYGEIAKIF
RAGCIIRAQF LQKITDAYAE NADIANLLLA PYFKKIADEY QQALRDVVAY AVQNGIPVPT
FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRTDKEG IFHTEWLE
//
