IOLC_LISMC
ID IOLC_LISMC Reviewed; 325 AA.
AC C1KZA1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=Lm4b_00403;
OS Listeria monocytogenes serotype 4b (strain CLIP80459).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=568819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP80459;
RX PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT "Comparative genomics and transcriptomics of lineages I, II, and III
RT strains of Listeria monocytogenes.";
RL BMC Genomics 13:144-144(2012).
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; FM242711; CAS04171.1; -; Genomic_DNA.
DR RefSeq; WP_003734601.1; NC_012488.1.
DR AlphaFoldDB; C1KZA1; -.
DR SMR; C1KZA1; -.
DR KEGG; lmc:Lm4b_00403; -.
DR HOGENOM; CLU_027634_6_0_9; -.
DR OMA; AIVKQGP; -.
DR BioCyc; LMON568819:LM4B_RS02005-MON; -.
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..325
FT /note="5-dehydro-2-deoxygluconokinase"
FT /id="PRO_1000215881"
SQ SEQUENCE 325 AA; 35643 MW; 88E0913E50836503 CRC64;
MNLNKHSERK FDLITVGRAC IDLNAVEYNR PMEETMTFSK YVGGSPANIA IGTAKLGLKV
GFIGKISADQ HGRFIEKYMR DLSINTDGMV KDTEGRKVGL AFTEIKSPDE CSILMYRENV
ADLYLTPEEI SEDYIKEARV LLISGTALAQ SPSREAVLKA VSLARKNDVA VAFELDYRPY
TWTNTEETAV YYSLVAEQAD VIIGTRDEFD MMENQVGGKN EATKAHLFQH QAEIVVIKHG
VEGSFAYTKA GETFQAKAYK TKVLKTFGAG DSYASAFLYG LFSGESIETA LKYGSAAASI
VVSKHSSSDA MPTADEIKAL IAQAE
