GNTK_BACSU
ID GNTK_BACSU Reviewed; 513 AA.
AC P12011;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Gluconokinase;
DE EC=2.7.1.12;
DE AltName: Full=Gluconate kinase;
GN Name=gntK; OrderedLocusNames=BSU40060;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC EC=2.7.1.12;
CC -!- ACTIVITY REGULATION: Catabolite repression by gluconate.
CC -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; J02584; AAA56925.1; -; Genomic_DNA.
DR EMBL; AB005554; BAA21578.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16043.1; -; Genomic_DNA.
DR PIR; B26190; B26190.
DR RefSeq; NP_391886.1; NC_000964.3.
DR RefSeq; WP_009968422.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P12011; -.
DR SMR; P12011; -.
DR STRING; 224308.BSU40060; -.
DR jPOST; P12011; -.
DR PaxDb; P12011; -.
DR PRIDE; P12011; -.
DR EnsemblBacteria; CAB16043; CAB16043; BSU_40060.
DR GeneID; 937713; -.
DR KEGG; bsu:BSU40060; -.
DR PATRIC; fig|224308.179.peg.4333; -.
DR eggNOG; COG1070; Bacteria.
DR InParanoid; P12011; -.
DR OMA; SDAMHFK; -.
DR PhylomeDB; P12011; -.
DR BioCyc; BSUB:BSU40060-MON; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR006002; Gluconate_kinase.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01314; gntK_FGGY; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Gluconate utilization; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..513
FT /note="Gluconokinase"
FT /id="PRO_0000059544"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 412..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 513 AA; 57169 MW; 351D44064C7AC3ED CRC64;
MTSYMLGIDI GTTSTKAVLF SENGDVVQKE SIGYPLYTPD ISTAEQNPEE IFQAVIHTTA
RITKQHPEKR ISFISFSSAM HSVIAIDEND KPLTPCITWA DNRSEGWAHK IKEELNGHEV
YKRTGTPIHP MAPLSKIAWI TNERKEIASK AKKYIGIKEY IFKQLFNEYV IDYSLASATG
MMNLKGLDWD EEALRIAGIT PDHLSKLVPT TEIFQHCSPE IAIQMGIDPE TPFVIGASDG
VLSNLGVNAI KKGEIAVTIG TSGAIRTIID KPQTDEKGRI FCYALTDKHW VIGGPVNNGG
IVLRWIRDEF ASSEIETATR LGIDPYDVLT KIAQRVRPGS DGLLFHPYLA GERAPLWNPD
VRGSFFGLTM SHKKEHMIRA ALEGVIYNLY TVFLALTECM DGPVTRIQAT GGFARSEVWR
QMMSDIFESE VVVPESYESS CLGACILGLY ATGKIDSFDA VSDMIGSTYR HTPIEDSAKE
YRTLMPIFIN LSRLLENQYT QIADYQRGLI THK