IOLC_PHOPR
ID IOLC_PHOPR Reviewed; 331 AA.
AC Q6LK43;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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}; Synonyms=SC8F11;
GN OrderedLocusNames=PBPRB0464;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378676; CAG22337.1; -; Genomic_DNA.
DR RefSeq; WP_011220546.1; NC_006371.1.
DR AlphaFoldDB; Q6LK43; -.
DR SMR; Q6LK43; -.
DR STRING; 298386.PBPRB0464; -.
DR EnsemblBacteria; CAG22337; CAG22337; PBPRB0464.
DR KEGG; ppr:PBPRB0464; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_6_0_6; -.
DR OMA; PYSWPSP; -.
DR OrthoDB; 1604782at2; -.
DR UniPathway; UPA00076; UER00146.
DR Proteomes; UP000000593; Chromosome 2.
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..331
FT /note="5-dehydro-2-deoxygluconokinase"
FT /id="PRO_0000352308"
SQ SEQUENCE 331 AA; 35574 MW; A2D8FA105160F4C7 CRC64;
MTKIALQQDR PLDAIVLGRA GVDLYAREAN TDMADISGFN KFVGGSAANI AVAISKLGGK
VGFIGCVADD AFGGYVRGYM TEQGINLDGM MTDNSGSRTS VAFTEMKPND CTVLIYRNKA
SDLTLKPEQV DPAYIAQSKM LVVTGTALSE SPSREATLIA MEHARRSNTV VVLDVDYRPY
SWRTDVDASI YYGIAAGLSD IVIGNREEFD MMETVLAPGN TDDDATADRF LRANTQVVIV
KAGELGSKVY CKDGHKFQQG IFRVEVKKPF GSGDSFAGGL IWTLVNGGEL EDGVKHGSAA
AAINVSGNSC TEAMPTKEVL FDFIETREQD L
