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IOLC_CLOB8
ID   IOLC_CLOB8              Reviewed;         339 AA.
AC   A6M229;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Cbei_4550;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) 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; CP000721; ABR36659.1; -; Genomic_DNA.
DR   RefSeq; WP_012060706.1; NC_009617.1.
DR   AlphaFoldDB; A6M229; -.
DR   SMR; A6M229; -.
DR   STRING; 290402.Cbei_4550; -.
DR   EnsemblBacteria; ABR36659; ABR36659; Cbei_4550.
DR   GeneID; 66347413; -.
DR   KEGG; cbe:Cbei_4550; -.
DR   eggNOG; COG0524; Bacteria.
DR   HOGENOM; CLU_027634_6_0_9; -.
DR   OMA; AIVKQGP; -.
DR   OrthoDB; 1604782at2; -.
DR   UniPathway; UPA00076; UER00146.
DR   Proteomes; UP000000565; 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..339
FT                   /note="5-dehydro-2-deoxygluconokinase"
FT                   /id="PRO_0000352293"
SQ   SEQUENCE   339 AA;  37652 MW;  3340463172C91E71 CRC64;
     MEYIKFDKAR KMDIVPIGRV AIDFNPIDIN KPLSESSTFK KYLGGSPANI AVGLARLGKK
     IGFIGKVSKD QFGEFVVNYF DNEGIDTSQI KYSKNGENLG LTFTEIASPT ESSILMYRQG
     IADLELNVDE IDEEYIKNTK AIVISGTALA KSPSREAALK ALELAKRNNT VVIFDVDYRA
     YNWKNSDEIA IYYSIAGKQS DIIMGSREEF DLMEKLITRE KNSDEETAKR WLDYGNKIVV
     IKHGKEGSTA YTSDGKSYNI KPFPVKLLKS FGGGDAYASA FLYGLLEGWS IIDSLEFGSA
     SAAMLVASHS CSQDMPTVEA IRNFIKEEKE EYGDMVARA
 
 
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