IOLC_BACSU
ID IOLC_BACSU Reviewed; 325 AA.
AC P42414;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=5-dehydro-2-deoxygluconokinase;
DE EC=2.7.1.92;
DE AltName: Full=2-deoxy-5-keto-D-gluconate kinase;
DE Short=DKG kinase;
GN Name=iolC; Synonyms=yxdC; OrderedLocusNames=BSU39740; ORFNames=E83C;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7952181; DOI=10.1099/13500872-140-9-2289;
RA Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y.;
RT "Cloning and nucleotide sequencing of a 15 kb region of the Bacillus
RT subtilis genome containing the iol operon.";
RL Microbiology 140:2289-2298(1994).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=168 / 60015;
RX PubMed=18310071; DOI=10.1074/jbc.m708043200;
RA Yoshida K., Yamaguchi M., Morinaga T., Kinehara M., Ikeuchi M., Ashida H.,
RA Fujita Y.;
RT "Myo-inositol catabolism in Bacillus subtilis.";
RL J. Biol. Chem. 283:10415-10424(2008).
CC -!- FUNCTION: Catalyzes the phosphorylation of 5-dehydro-2-deoxy-D-
CC gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2-
CC deoxy-D-gluconate (DKGP). {ECO:0000269|PubMed:18310071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydro-2-deoxy-D-gluconate + ATP = 6-phospho-5-dehydro-2-
CC deoxy-D-gluconate + ADP + H(+); Xref=Rhea:RHEA:13497,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16669, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57949, ChEBI:CHEBI:456216; EC=2.7.1.92;
CC Evidence={ECO:0000269|PubMed:18310071};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 5/7.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; D14399; BAA03292.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16010.1; -; Genomic_DNA.
DR PIR; C69645; C69645.
DR RefSeq; NP_391853.1; NC_000964.3.
DR RefSeq; WP_003243753.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42414; -.
DR SMR; P42414; -.
DR STRING; 224308.BSU39740; -.
DR jPOST; P42414; -.
DR PaxDb; P42414; -.
DR PRIDE; P42414; -.
DR EnsemblBacteria; CAB16010; CAB16010; BSU_39740.
DR GeneID; 937622; -.
DR KEGG; bsu:BSU39740; -.
DR PATRIC; fig|224308.179.peg.4299; -.
DR eggNOG; COG0524; Bacteria.
DR InParanoid; P42414; -.
DR OMA; AIVKQGP; -.
DR PhylomeDB; P42414; -.
DR BioCyc; BSUB:BSU39740-MON; -.
DR BioCyc; MetaCyc:BSU39740-MON; -.
DR UniPathway; UPA00076; UER00146.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047590; F:5-dehydro-2-deoxygluconokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.20.150.10; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01668; IolC; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR022841; DKG_kinase_firmi.
DR InterPro; IPR030830; Myo_inos_IolC.
DR InterPro; IPR023314; Myo_inos_IolC-like_sf.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR04382; myo_inos_iolC_N; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..325
FT /note="5-dehydro-2-deoxygluconokinase"
FT /id="PRO_0000080073"
SQ SEQUENCE 325 AA; 35632 MW; 3C603A1E5512EC8C CRC64;
MKYTFNEEKA FDIVAIGRAC IDLNAVEYNR PMEETMTFSK YVGGSPANIA IGSAKLGLKA
GFIGKIPDDQ HGRFIESYMR KTGVDTTQMI VDQDGHKAGL AFTEILSPEE CSILMYRDDV
ADLYLEPSEV SEDYIANAKM LLVSGTALAK SPSREAVLKA VQYAKKHQVK VVFELDYRPY
TWQSSDETAV YYSLVAEQSD IVIGTRDEFD VMENRTGGSN EESVNHLFGH SADLVVIKHG
VEGSYAYSKS GEVFRAQAYK TKVLKTFGAG DSYASAFIYG LVSGKDIETA LKYGSASASI
VVSKHSSSEA MPTAEEIEQL IEAQS
