ID   IOLC_LACCA              Reviewed;         326 AA.
AC   A5YBJ5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
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};
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BL23;
RX   PubMed=17449687; DOI=10.1128/aem.00243-07;
RA   Yebra M.J., Zuniga M., Beaufils S., Perez-Martinez G., Deutscher J.,
RA   Monedero V.;
RT   "Identification of a gene cluster allowing Lactobacillus casei BL23 the
RT   utilization of myo-inositol.";
RL   Appl. Environ. Microbiol. 73:3850-3858(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}.
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DR   EMBL; EF382358; ABP57764.1; -; Genomic_DNA.
DR   RefSeq; WP_003568831.1; NZ_MODT01000071.1.
DR   AlphaFoldDB; A5YBJ5; -.
DR   SMR; A5YBJ5; -.
DR   STRING; 1582.AAW28_06905; -.
DR   GeneID; 61268587; -.
DR   eggNOG; COG0524; Bacteria.
DR   OMA; AIVKQGP; -.
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..326
FT                   /note="5-dehydro-2-deoxygluconokinase"
FT                   /id="PRO_0000352301"
SQ   SEQUENCE   326 AA;  35650 MW;  F8A66323AA3C7EC4 CRC64;
     MPQKFDLIAI GRAAVDLNAV EYNRPLEDTK TFAKFVGGSP ANIAIGSAKL GQKVGFIGKV
     SDDQLGHYVT QYMASVGIDT SNMVKDDTGH KIGLTFTEII SPEESDILMY RNEAADLYLN
     AHEVSRAYLA QTKMLVISGT GLAQSPSREA ILKALLIAKE LGVEVIFELD YRPYTWQNAE
     ETSLYYQLVA QKADVIIGTR DEFDVLENHQ GRTDQETIAT LFQYDANLIV IKSGIQGSNA
     YTKAGETYHF GVFKTKVLKS FGAGDSFAAG FLYAYQHQLG LETALKYGSA AASIVISQLS
     SSEAMPNLDQ LTAFIEKAEA QEVHQS