ID   IOLC_BACAA              Reviewed;         332 AA.
AC   C3PAZ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=BAA_2568;
OS   Bacillus anthracis (strain A0248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=592021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A0248;
RA   Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA   Brettin T.;
RT   "Genome sequence of Bacillus anthracis A0248.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001598; ACQ48015.1; -; Genomic_DNA.
DR   RefSeq; WP_001068616.1; NC_012659.1.
DR   AlphaFoldDB; C3PAZ0; -.
DR   SMR; C3PAZ0; -.
DR   GeneID; 45022375; -.
DR   KEGG; bai:BAA_2568; -.
DR   HOGENOM; CLU_027634_6_0_9; -.
DR   OMA; SPTDCSI; -.
DR   UniPathway; UPA00076; UER00146.
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_1000187303"
SQ   SEQUENCE   332 AA;  36663 MW;  D6A7BCA70DB25043 CRC64;
     MNPLIFKENR PFDLIAVGRL CVDLNANETQ RPMEETRTFT KYVGGSPANI AIGAARLGLQ
     TGFIGKVSDD QMGRFITGYL KDNKINTDQI PIDCTGAVTG LAFTEIKSPE DCSILMYRDN
     VADLNLDPTE VSEDYIKQSK ALLISGTALA KSPSREAVFL ALEYARKHDV VVFFDVDYRP
     YTWQSEAETA VYYNLAAEKS DVIIGTREEF DMMEKLLNYE KSNDQVTAER WFSHHAKIVV
     IKHGGDGSIA YTRDGQSHRG GIFKTKVLKT FGAGDSYASA FIYGLMQGLE IPQAMRLGGA
     SASIVISKHS CSDAMPTRAE ISAFMETAEE LV