IOLI_ALKHC
ID IOLI_ALKHC Reviewed; 282 AA.
AC Q9KAH2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Inosose isomerase;
DE EC=5.3.99.11;
DE AltName: Full=2-keto-myo-inositol isomerase;
DE Short=2KMI isomerase;
GN Name=iolI; OrderedLocusNames=BH2315;
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).
CC -!- FUNCTION: Involved in the reversible interconverion of 2-keto-myo-
CC inositol (2KMI, inosose or 2,4,6/3,5-pentahydroxycyclohexanone) to 1-
CC keto-D-chiro-inositol (1KDCI or 2,3,5/4,6-pentahydroxycyclohexanone).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=scyllo-inosose = scyllo-inosine; Xref=Rhea:RHEA:25776,
CC ChEBI:CHEBI:17811, ChEBI:CHEBI:50920; EC=5.3.99.11;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000250};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA.
CC -!- SIMILARITY: Belongs to the IolI family. {ECO:0000305}.
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DR EMBL; BA000004; BAB06034.1; -; Genomic_DNA.
DR PIR; C83939; C83939.
DR RefSeq; WP_010898471.1; NC_002570.2.
DR AlphaFoldDB; Q9KAH2; -.
DR SMR; Q9KAH2; -.
DR STRING; 272558.10174935; -.
DR EnsemblBacteria; BAB06034; BAB06034; BAB06034.
DR KEGG; bha:BH2315; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_035063_3_0_9; -.
DR OMA; YIEIRTM; -.
DR OrthoDB; 1478083at2; -.
DR UniPathway; UPA00076; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
PE 3: Inferred from homology;
KW Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..282
FT /note="Inosose isomerase"
FT /id="PRO_0000352278"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 282 AA; 32033 MW; 06053287A5A712BD CRC64;
MKLCYNQATT LENSNLVKDL EYCEKNGYDY IEIRTMDKLP EYLKDHTLDE LKHFFQTNHI
KPLALNALVF FNNRDEAGYK EIITEFKGMM ETAKALNIPY VVAVPLVTEE KILKSEIKRS
CVNVLTELSE IAKPYGVKVA LEFIGHPQCT VNTFGQAYEI VEAVGRDNIG LVLDCFHFHA
MGSNISDLEK ADISKIFILH MDDTEDFPVG FLTDEDRVWP GHGAINLDQM LSILKEKGYS
GAVSVELFRP EYYQLSAEEA IKTAKDTTVE VVSKHFTLET TK
