ID   6PGD_BACSU              Reviewed;         469 AA.
AC   P80859; P54546;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=6-phosphogluconate dehydrogenase, NADP(+)-dependent, decarboxylating;
DE            EC=1.1.1.44;
DE   AltName: Full=GNTZII;
GN   Name=gndA; Synonyms=yqjI; OrderedLocusNames=BSU23860;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
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   [3]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ROLE IN PP PATHWAY, GENE NAME, AND DISRUPTION
RP   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 NADP
CC       to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in
CC       B.subtilis during growth on glucose and gluconate.
CC       {ECO:0000269|PubMed:15231785}.
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         Evidence={ECO:0000269|PubMed:15231785};
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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit a reduced growth
CC       on glucose as the sole carbon source, and they do not use the pentose
CC       phosphate (PP) pathway at all. {ECO:0000269|PubMed:15231785}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12615.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D84432; BAA12615.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB14318.2; -; Genomic_DNA.
DR   PIR; A69964; A69964.
DR   RefSeq; NP_390267.2; NC_000964.3.
DR   RefSeq; WP_003230365.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P80859; -.
DR   SMR; P80859; -.
DR   IntAct; P80859; 1.
DR   MINT; P80859; -.
DR   STRING; 224308.BSU23860; -.
DR   jPOST; P80859; -.
DR   PaxDb; 224308-BSU23860; -.
DR   EnsemblBacteria; CAB14318; CAB14318; BSU_23860.
DR   GeneID; 938695; -.
DR   KEGG; bsu:BSU23860; -.
DR   PATRIC; fig|224308.179.peg.2599; -.
DR   eggNOG; COG0362; Bacteria.
DR   InParanoid; P80859; -.
DR   OrthoDB; 9804542at2; -.
DR   PhylomeDB; P80859; -.
DR   BioCyc; BSUB:BSU23860-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-6842; -.
DR   BRENDA; 1.1.1.44; 658.
DR   UniPathway; UPA00115; UER00410.
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; 1.20.5.320; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Gluconate utilization; NADP; Oxidoreductase;
KW   Pentose shunt; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298659"
FT   CHAIN           2..469
FT                   /note="6-phosphogluconate dehydrogenase, NADP(+)-dependent,
FT                   decarboxylating"
FT                   /id="PRO_0000090027"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        189
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         185..186
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
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         446
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        11
FT                   /note="L -> W (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  51775 MW;  D0A94E0B4F2250EF CRC64;
     MSKQQIGVIG LAVMGKNLAL NIESRGFSVS VYNRSSSKTE EFLQEAKGKN VVGTYSIEEF
     VQSLETPRKI LLMVKAGTAT DATIQSLLPH LEKDDILIDG GNTYYKDTQR RNKELAESGI
     HFIGTGVSGG EEGALKGPSI MPGGQKEAHE LVKPILEAIS AKVDGEPCTT YIGPDGAGHY
     VKMVHNGIEY GDMQLISESY FILKQVLGLS ADELHEVFAE WNKGELDSYL IEITADIFTK
     KDEETGKPLV DVILDKAGQK GTGKWTSQSA LDLGVPLPII TESVFARFIS AMKEERVKAS
     GLLSGPEVKP VTENKEELIE AVRKALFMSK ICSYAQGFAQ MKAASEEYNW DLKYGEIAMI
     FRGGCIIRAA FLQKIKEAYD REPELDNLLL DSYFKNIVES YQGALRQVIS LAVAQGVPVP
     SFSSALAYYD SYRTAVLPAN LIQAQRDYFG AHTYERTDKE GIFHTEWMK
//