IOLC_BACLD
ID IOLC_BACLD Reviewed; 325 AA.
AC Q65D02; Q62NH8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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};
GN OrderedLocusNames=BLi04249, BL00244;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU25683.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU43062.1; -; Genomic_DNA.
DR RefSeq; WP_009329981.1; NC_006322.1.
DR AlphaFoldDB; Q65D02; -.
DR SMR; Q65D02; -.
DR STRING; 279010.BL00244; -.
DR EnsemblBacteria; AAU25683; AAU25683; BL00244.
DR GeneID; 66213822; -.
DR KEGG; bld:BLi04249; -.
DR KEGG; bli:BL00244; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_6_0_9; -.
DR OMA; AIVKQGP; -.
DR OrthoDB; 1604782at2; -.
DR BioCyc; BLIC279010:BLI_RS20895-MON; -.
DR UniPathway; UPA00076; UER00146.
DR Proteomes; UP000000606; 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; Reference proteome; Transferase.
FT CHAIN 1..325
FT /note="5-dehydro-2-deoxygluconokinase"
FT /id="PRO_0000352290"
SQ SEQUENCE 325 AA; 35498 MW; BE2F0B1DBB5BF7C7 CRC64;
MKYTFNEEKE FDIVAIGRAC IDLNAVEYNR PMEQTMTFSK YVGGSPANIA IGSSKLGLKT
GFIGKIPDDQ HGRFIETYMR NTGVDTSQMA VDKDGHKAGL AFTEILSPEE CSILMYRDDV
ADLYLAPSEV NEDYIAKSKM LLVSGTALAK SPSREAVLKA VQLAKKHQVK VVFELDYRPY
TWTSAEETAV YYTLVAEQSD IVIGTRDEFD VMENKSGGSN EESVQHLFAH SADLVVIKHG
VEGSYAYSKS GDVFRAKAYK TKVLKTFGAG DSYASAFLYG LVSGKDIETA LKYGSASASI
VVSKHSSSEA MPTVAEIEEL IAAQS
