IOLC_CLOBB
ID IOLC_CLOBB Reviewed; 339 AA.
AC B2TJ78;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=CLL_A1302;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001056; ACD24006.1; -; Genomic_DNA.
DR RefSeq; WP_012424792.1; NC_018648.1.
DR AlphaFoldDB; B2TJ78; -.
DR SMR; B2TJ78; -.
DR EnsemblBacteria; ACD24006; ACD24006; CLL_A1302.
DR KEGG; cbk:CLL_A1302; -.
DR PATRIC; fig|935198.13.peg.1248; -.
DR HOGENOM; CLU_027634_6_0_9; -.
DR OMA; AIVKQGP; -.
DR OrthoDB; 1604782at2; -.
DR UniPathway; UPA00076; UER00146.
DR Proteomes; UP000001195; 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_0000352295"
SQ SEQUENCE 339 AA; 37895 MW; 0F9365A205506B7D CRC64;
MGYIKFQKDR KFEIVPIGRV AIDFNPIDIN RPLSESKTFK KYLGGSPANI AVGLSRLGKK
VGFIGKVSKD QFGKFVVDYF DNEGIDTSQI KYAENGESLG LTFTEIASPT ESSILMYRNG
IADLELDVNE IDEEYIKNTK AIVISGTALA KSPSREAALK ALELAKKNDT IVIFDVDYRE
YNWKNKDEIA IYYSIVGKQS DIVMGSREEF DLMESLIVKE KSTDEESAKR WLGFGNKIVV
IKHGKEGSTA YTNDRKSYKI KPFPVKLLKS FGGGDAYASA FIYGILEEWD IMDALEFGSA
SAAMLVASHS CSEDMPTVKE INEFIKEKKE QYGEMIARG
