ID IOLC_BACVZ Reviewed; 330 AA.
AC A7ZAH9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=RBAM_036760;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(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; CP000560; ABS76005.1; -; Genomic_DNA.
DR RefSeq; WP_012118846.1; NC_009725.2.
DR AlphaFoldDB; A7ZAH9; -.
DR SMR; A7ZAH9; -.
DR KEGG; bay:RBAM_036760; -.
DR HOGENOM; CLU_027634_6_0_9; -.
DR UniPathway; UPA00076; UER00146.
DR Proteomes; UP000001120; 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 CDD; cd01166; KdgK; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 2.20.150.10; putative 5-dehydro-2- deoxygluconokinase; 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 NCBIfam; TIGR04382; myo_inos_iolC_N; 1.
DR PANTHER; PTHR43085:SF49; 5-DEHYDRO-2-DEOXYGLUCONOKINASE; 1.
DR PANTHER; PTHR43085; HEXOKINASE FAMILY MEMBER; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..330
FT /note="5-dehydro-2-deoxygluconokinase"
FT /id="PRO_0000352284"
SQ SEQUENCE 330 AA; 36018 MW; E23DA44E56D2209A CRC64;
MKYTFNEEKE FDIVAIGRAC IDLNAAEYNR PMEETMTFSK YVGGSPANIA IGSAKLGLKA
GFIGKIPDDQ HGRFIVSYMQ GKGVDTSQMT VDREGRKAGL AFTEILSPEE CSILMYRDDV
ADLYLEPSEV NEGYIANAKM LLVSGTALAK SPSREAVLKA VHIAKKHDVK VVFELDYRPY
TWQSAEETAV YYTLVAEQSD IVIGTRDEFD VMENRSGGGN DETVRHLFAH SADLVVIKHG
VDGSYAYSRS GEVFRAHAYK TKVLKTFGAG DSYASAFIYG LVSGRDIETA LKYGSASASI
VVSKHSSSEA MPAAGEIIEL IEAQHSLNGK
//
