6PGDH_BACSU
ID 6PGDH_BACSU Reviewed; 468 AA.
AC P12013;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating;
DE EC=1.1.1.343;
GN Name=gntZ; OrderedLocusNames=BSU40080;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3020045; DOI=10.1016/s0021-9258(18)67083-8;
RA Fujita Y., Fujita T., Miwa Y., Nihashi J., Aratani Y.;
RT "Organization and transcription of the gluconate operon, gnt, of Bacillus
RT subtilis.";
RL J. Biol. Chem. 261:13744-13753(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7584049; DOI=10.1093/dnares/2.2.61;
RA Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
RT "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome
RT between the gnt and iol operons.";
RL DNA Res. 2:61-69(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 460-468.
RC STRAIN=168;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
RN [5]
RP PROBABLE FUNCTION.
RX PubMed=1659648; DOI=10.1111/j.1365-2958.1991.tb01880.x;
RA Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.;
RT "Analysis of the gluconate (gnt) operon of Bacillus subtilis.";
RL Mol. Microbiol. 5:1081-1089(1991).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=15231785; DOI=10.1128/jb.186.14.4528-4534.2004;
RA Zamboni N., Fischer E., Laudert D., Aymerich S., Hohmann H.P., Sauer U.;
RT "The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate
RT dehydrogenase in the pentose phosphate pathway.";
RL J. Bacteriol. 186:4528-4534(2004).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to
CC NADH. Does not contribute to oxidative pentose phosphate (PP) pathway
CC fluxes during growth on glucose. The functional role of GntZ remains
CC obscure. {ECO:0000269|PubMed:15231785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NAD(+) = CO2 + D-ribulose 5-phosphate
CC + NADH; Xref=Rhea:RHEA:33023, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58121, ChEBI:CHEBI:58759;
CC EC=1.1.1.343; Evidence={ECO:0000269|PubMed:15231785};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit no detectable
CC phenotype on glucose as the sole carbon source, and they grow normally
CC on gluconate. {ECO:0000269|PubMed:15231785}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; J02584; AAA56927.1; -; Genomic_DNA.
DR EMBL; AB005554; BAA21576.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16045.1; -; Genomic_DNA.
DR EMBL; D78193; BAA11267.1; -; Genomic_DNA.
DR PIR; D26190; D26190.
DR RefSeq; NP_391888.1; NC_000964.3.
DR RefSeq; WP_003243876.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P12013; -.
DR SMR; P12013; -.
DR STRING; 224308.BSU40080; -.
DR jPOST; P12013; -.
DR PaxDb; P12013; -.
DR EnsemblBacteria; CAB16045; CAB16045; BSU_40080.
DR GeneID; 937716; -.
DR KEGG; bsu:BSU40080; -.
DR PATRIC; fig|224308.179.peg.4335; -.
DR eggNOG; COG0362; Bacteria.
DR InParanoid; P12013; -.
DR OMA; QALYMGK; -.
DR PhylomeDB; P12013; -.
DR BioCyc; BSUB:BSU40080-MON; -.
DR BRENDA; 1.1.1.343; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
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 PANTHER; PTHR11811; PTHR11811; 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 1: Evidence at protein level;
KW Gluconate utilization; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..468
FT /note="6-phosphogluconate dehydrogenase, NAD(+)-dependent,
FT decarboxylating"
FT /id="PRO_0000090026"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 9..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 32..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 73..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 127..129
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 184..185
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 286
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; 51983 MW; 56D88BEB8E553856 CRC64;
MFNSIGVIGL GVMGSNIALN MANKGENVAV YNYTRDLTDQ LIQKLDGQSL SPYYELEDFV
QSLEKPRKIF LMVTAGKPVD SVIQSLKPLL EEGDVIMDGG NSHYEDTERR YDELKEKGIG
YLGVGISGGE VGALTGPSIM PGGDRDVYEK AAPILTKIAA QVGDDPCCVY IGPKGAGHFT
KMVHNGIEYA DMQLIAEAYT FLRETLRLPL DEIASIFETW NQGELKSYLI EITAEILRKK
DEKTGQPLID VILDKTGQKG TGKWTSMQAI DNGIPSTIIT ESLFARYLSS LKEERMAAQD
VLAGPEAEEK HLDKDTWIEY VRQALYMGKV CAYAQGFAQY KMSSELYGWN LPLKDIALIF
RGGCIIRADF LNVISEAFSE QPNLANLLIA PYFTDKLHAY QTGLRKVVCE GISTGISFPC
LTTALSYYDG YRTGRSNANL LQAQRDYFGA HTYERTDMDG VFHTNWSE
