IOLI_BACLD
ID IOLI_BACLD Reviewed; 278 AA.
AC Q65D08; Q62NI4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BLi04243, BL00238;
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: 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; CP000002; AAU25677.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU43056.1; -; Genomic_DNA.
DR RefSeq; WP_003177805.1; NC_006322.1.
DR AlphaFoldDB; Q65D08; -.
DR SMR; Q65D08; -.
DR STRING; 279010.BL00238; -.
DR EnsemblBacteria; AAU25677; AAU25677; BL00238.
DR GeneID; 66213828; -.
DR KEGG; bld:BLi04243; -.
DR KEGG; bli:BL00238; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_035063_3_0_9; -.
DR OMA; YIEIRTM; -.
DR OrthoDB; 1478083at2; -.
DR BioCyc; BLIC279010:BLI_RS20865-MON; -.
DR UniPathway; UPA00076; -.
DR Proteomes; UP000000606; 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..278
FT /note="Inosose isomerase"
FT /id="PRO_0000352279"
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 278 AA; 31827 MW; BE773F017916D890 CRC64;
MKLCFNEATT LENSNLAKDL EYCEKHGYDY IEIRTMDKLP EYLKDHALSE LAEYFQTHHI
KPLALNALVF FNNRDEKGHR EIIEEFKGMM ETCKMLGVKY VVAVPLVTEQ KILKEDIKAS
SVEVLTELSD IAEPYGVKIA VEFVGHPECT VNTFSQAYDI VMTVNRDNVG LVFDSFHFHA
MGSSLEDLKK ADGKKIFIYH IDDTEDFPIG FLRDEDRVWP GQGAIDLDAH LSTLKDIGFS
DVVSVELFRP EYYKLSAEET IRTAKETTVE VVSKYFKI