ID   IOLC_CLOP1              Reviewed;         338 AA.
AC   Q0TUZ4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=CPF_0082;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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; CP000246; ABG83660.1; -; Genomic_DNA.
DR   RefSeq; WP_003448561.1; NC_008261.1.
DR   AlphaFoldDB; Q0TUZ4; -.
DR   SMR; Q0TUZ4; -.
DR   STRING; 195103.CPF_0082; -.
DR   PRIDE; Q0TUZ4; -.
DR   EnsemblBacteria; ABG83660; ABG83660; CPF_0082.
DR   GeneID; 29572755; -.
DR   KEGG; cpf:CPF_0082; -.
DR   eggNOG; COG0524; Bacteria.
DR   HOGENOM; CLU_027634_6_0_9; -.
DR   OMA; AIVKQGP; -.
DR   OrthoDB; 1604782at2; -.
DR   UniPathway; UPA00076; UER00146.
DR   Proteomes; UP000001823; 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..338
FT                   /note="5-dehydro-2-deoxygluconokinase"
FT                   /id="PRO_0000352297"
SQ   SEQUENCE   338 AA;  37662 MW;  5BA30E9842C12B4B CRC64;
     MRYIEFDEKR KFDIVPVGRV AIDFNPTDIH KPLSESRNFN KYLGGSPANI AVGLARLGKK
     VGFIGKVSDD RFGEFVVNYF KKEGIDVSEI SKAKNGESLG LTFTEILSPT ESSILMYRNG
     IADLQLDVDD IDEDYIKNTK AIVISGTALA MSPSREAALK ALRLAKKNGT VVIFDVDYRE
     YNWKNKDEIA IYYSIVGKES DIIMGSREEF DLMEGLIAKD STDEETAKRW LDYGNKIVVI
     KHGKDGSTAY TRDGKAYRIK PFPVKLLKSF GGGDAYASAF IYGILEGWDM MDALEFGSAS
     AAMLVASHSC SEDMPTVEAI KEFIKKEKEE YGEMVARS