ID   IOLC2_BACCZ             Reviewed;         332 AA.
AC   Q4V1F7;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=5-dehydro-2-deoxygluconokinase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01668};
DE            Short=DKG kinase 2 {ECO:0000255|HAMAP-Rule:MF_01668};
GN   Name=iolC2 {ECO:0000255|HAMAP-Rule:MF_01668};
GN   OrderedLocusNames=pE33L466_0300;
OS   Bacillus cereus (strain ZK / E33L).
OG   Plasmid pE33L466.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., 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   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; CP000040; AAY60450.1; -; Genomic_DNA.
DR   RefSeq; WP_001068599.1; NZ_CP009967.1.
DR   AlphaFoldDB; Q4V1F7; -.
DR   SMR; Q4V1F7; -.
DR   EnsemblBacteria; AAY60450; AAY60450; pE33L466_0300.
DR   KEGG; bcz:pE33L466_0300; -.
DR   PATRIC; fig|288681.22.peg.5506; -.
DR   OMA; AIVKQGP; -.
DR   UniPathway; UPA00076; UER00146.
DR   Proteomes; UP000002612; Plasmid pE33L466.
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; Plasmid; Transferase.
FT   CHAIN           1..332
FT                   /note="5-dehydro-2-deoxygluconokinase 2"
FT                   /id="PRO_0000352287"
SQ   SEQUENCE   332 AA;  36706 MW;  D3AAAAAD9065C1F0 CRC64;
     MNPLIFKEDC PLDLIAVGRL CVDLNANETQ RPMEATRTFT KYVGGSPANI AIGATRLGLQ
     TGFIGKVSDD QMGRFITRYL QDNNINTDQI CIDRTGAVTG LAFTEIKSPE DCSILMYRDN
     VADLNLDPTE VSEDYIKQSK ALLISGTALA KSPSREAVFL ALEYARKHDV VVFFDVDYRP
     YTWQSEAETA VYYNLAAEKS DVIIGTREEF DMMEKLLNYE ESNDQVTAER WFSHHAKIVV
     IKHGGDGSIA YTRDGQSHRG GIFKTKVLKT FGAGDSYASA FIYGLMQGLE IPQAMRLGGA
     SASIVISKHS CSDAMPTRAE ISAFMEIAEE IV