ID   IOLC_BACAH              Reviewed;         332 AA.
AC   A0REB4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=5-dehydro-2-deoxygluconokinase {ECO:0000255|HAMAP-Rule:MF_01668};
DE            EC=2.7.1.92 {ECO:0000255|HAMAP-Rule:MF_01668};
DE   AltName: Full=2-deoxy-5-keto-D-gluconate kinase {ECO:0000255|HAMAP-Rule:MF_01668};
DE            Short=DKG kinase {ECO:0000255|HAMAP-Rule:MF_01668};
GN   Name=iolC {ECO:0000255|HAMAP-Rule:MF_01668}; OrderedLocusNames=BALH_2258;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
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:0000255|HAMAP-Rule:MF_01668}.
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:0000255|HAMAP-Rule:MF_01668};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 5/7. {ECO:0000255|HAMAP-
CC       Rule:MF_01668}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000255|HAMAP-Rule:MF_01668}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK85557.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000485; ABK85557.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001068612.1; NC_008600.1.
DR   AlphaFoldDB; A0REB4; -.
DR   SMR; A0REB4; -.
DR   EnsemblBacteria; ABK85557; ABK85557; BALH_2258.
DR   KEGG; btl:BALH_2258; -.
DR   HOGENOM; CLU_027634_6_0_9; -.
DR   UniPathway; UPA00076; UER00146.
DR   Proteomes; UP000000761; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..332
FT                   /note="5-dehydro-2-deoxygluconokinase"
FT                   /id="PRO_0000352291"
SQ   SEQUENCE   332 AA;  36665 MW;  26358B336E72F2DD CRC64;
     MNPLIFKEDR PLDLIAVGRL CVDLNANETQ RPMEETKTFT KYVGGSPANI AIGASRLGLQ
     TGFIGKVSDD QMGRFITGYL KDNKINTDQI HIDCTGAVTG LAFTEIKSPE DCSILMYRDN
     VADLNLDPTE VSEDYIKQSK ALLISGTALA KSPSREAVFL ALEYAHKHDV VVFFDVDYRP
     YTWQSEAETA VYYNLAAEKS DVIIGTREEF DMMEKLLNYE QSNDQVTAER WFSHYAKIVV
     IKHGGDGSIA YTRDGQSHRG GIFKTKVLKT FGAGDSYASA FIYGLMQGLE IPQAMRLGGA
     SASIVISKHS CSDAMPTRAE ISAFMETAEE LV