IOLI_BACVZ
ID IOLI_BACVZ Reviewed; 280 AA.
AC A7ZAH3;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=RBAM_036700;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; 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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000560; ABS75999.1; -; Genomic_DNA.
DR RefSeq; WP_012118841.1; NC_009725.2.
DR AlphaFoldDB; A7ZAH3; -.
DR SMR; A7ZAH3; -.
DR STRING; 326423.RBAM_036700; -.
DR EnsemblBacteria; ABS75999; ABS75999; RBAM_036700.
DR GeneID; 66323974; -.
DR KEGG; bay:RBAM_036700; -.
DR HOGENOM; CLU_035063_3_0_9; -.
DR OMA; YIEIRTM; -.
DR UniPathway; UPA00076; -.
DR Proteomes; UP000001120; 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.
FT CHAIN 1..280
FT /note="Inosose isomerase"
FT /id="PRO_0000352277"
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 280 AA; 31999 MW; 61F3BBEFA4562F91 CRC64;
MKLCFNEATT LENSNLKQDL ELCEKHGYDY IEIRTMDKLP EYLKDHSLAD LAEYFRTHHI
KPLALNALVF FNNRDEKGYR EIISEFKSMM ETCRTLGVKY VVAVPLVTER KILKEEIKKS
SAEVLTELSD IAEPYGVNIA LEFVGHPQCT VNTFEQAYDI VNAVGRDNVG LVFDSFHFHA
MGSNIESLKQ ADGKKIFIYH IDDTEDFPIG FLTDEDRVWP GQGAIDLDAH LSALKEIGFN
DVVSVELFRP EYYKLTAEET IKTAKETTEA VVSKYFMKEA
