IOLC_ALKHC
ID IOLC_ALKHC Reviewed; 331 AA.
AC Q9KAG8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BH2319;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a putative 5-dehydro-2-deoxygluconokinase
RT (np_243185.1) from Bacillus halodurans at 1.90 a resolution.";
RL Submitted (AUG-2007) to the PDB data bank.
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; BA000004; BAB06038.1; -; Genomic_DNA.
DR PIR; G83939; G83939.
DR RefSeq; WP_010898475.1; NC_002570.2.
DR PDB; 2QCV; X-ray; 1.90 A; A=1-331.
DR PDBsum; 2QCV; -.
DR AlphaFoldDB; Q9KAG8; -.
DR SMR; Q9KAG8; -.
DR STRING; 272558.10174939; -.
DR EnsemblBacteria; BAB06038; BAB06038; BAB06038.
DR KEGG; bha:BH2319; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_6_0_9; -.
DR OMA; AIVKQGP; -.
DR OrthoDB; 1604782at2; -.
DR UniPathway; UPA00076; UER00146.
DR EvolutionaryTrace; Q9KAG8; -.
DR Proteomes; UP000001258; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..331
FT /note="5-dehydro-2-deoxygluconokinase"
FT /id="PRO_0000352289"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2QCV"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 288..304
FT /evidence="ECO:0007829|PDB:2QCV"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:2QCV"
SQ SEQUENCE 331 AA; 36641 MW; A9C559702FED958E CRC64;
MTYELSTDRE FDLIAIGRAC IDLNAVEYNR PMEETMTFSK YVGGSPANIV IGSSKLGLKA
GFIGKIADDQ HGRFIESYMR GVGVDTSNLV VDQEGHKTGL AFTEIKSPEE CSILMYRQDV
ADLYLSPEEV NEAYIRRSKL LLVSGTALSK SPSREAVLKA IRLAKRNDVK VVFELDYRPY
SWETPEETAV YYSLVAEQSD IVIGTREEFD VLENRTEKGD NDETIRYLFK HSPELIVIKH
GVEGSFAYTK AGEAYRGYAY KTKVLKTFGA GDSYASAFLY ALISGKGIET ALKYGSASAS
IVVSKHSSSD AMPSVEEIEA LIEKDETITI A
