IOLE_LACPL
ID IOLE_LACPL Reviewed; 300 AA.
AC Q88S37; F9ULG1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Inosose dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
DE EC=4.2.1.44 {ECO:0000255|HAMAP-Rule:MF_01672};
DE AltName: Full=2-keto-myo-inositol dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
DE Short=2KMI dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
GN Name=iolE {ECO:0000255|HAMAP-Rule:MF_01672}; OrderedLocusNames=lp_3607;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
CC -!- FUNCTION: Catalyzes the dehydration of inosose (2-keto-myo-inositol,
CC 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)-
CC trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol).
CC {ECO:0000255|HAMAP-Rule:MF_01672}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=scyllo-inosose = 3D-3,5/4-trihydroxycyclohexane-1,2-dione +
CC H2O; Xref=Rhea:RHEA:14065, ChEBI:CHEBI:15377, ChEBI:CHEBI:17811,
CC ChEBI:CHEBI:28446; EC=4.2.1.44; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01672};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 2/7. {ECO:0000255|HAMAP-
CC Rule:MF_01672}.
CC -!- SIMILARITY: Belongs to the IolE/MocC family. {ECO:0000255|HAMAP-
CC Rule:MF_01672}.
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; AL935263; CCC80568.1; -; Genomic_DNA.
DR RefSeq; WP_011102249.1; NC_004567.2.
DR RefSeq; YP_004891082.1; NC_004567.2.
DR PDB; 3CNY; X-ray; 1.85 A; A/B=1-300.
DR PDBsum; 3CNY; -.
DR AlphaFoldDB; Q88S37; -.
DR SMR; Q88S37; -.
DR STRING; 220668.lp_3607; -.
DR PRIDE; Q88S37; -.
DR EnsemblBacteria; CCC80568; CCC80568; lp_3607.
DR KEGG; lpl:lp_3607; -.
DR PATRIC; fig|220668.9.peg.3011; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_059523_0_0_9; -.
DR OMA; YDSRPEL; -.
DR PhylomeDB; Q88S37; -.
DR BioCyc; LPLA220668:G1GW0-3055-MON; -.
DR UniPathway; UPA00076; UER00144.
DR EvolutionaryTrace; Q88S37; -.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050114; F:myo-inosose-2 dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01672; IolE; 1.
DR InterPro; IPR023952; IolE.
DR InterPro; IPR030823; IolE/MocC.
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.
DR TIGRFAMs; TIGR04379; myo_inos_iolE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Lyase; Manganese; Reference proteome.
FT CHAIN 1..300
FT /note="Inosose dehydratase"
FT /id="PRO_0000352374"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3CNY"
FT TURN 24..29
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 79..100
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3CNY"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:3CNY"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:3CNY"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:3CNY"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3CNY"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3CNY"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:3CNY"
SQ SEQUENCE 300 AA; 33881 MW; 870B9B88384D024D CRC64;
MSSKAEKDIK WGIAPIGWRN DDIPSIGKDN NLQQLLSDIV VAGFQGTEVG GFFPGPEKLN
YELKLRNLEI AGQWFSSYII RDGIEKASEA FEKHCQYLKA INAPVAVVSE QTYTIQRSDT
ANIFKDKPYF TDKEWDEVCK GLNHYGEIAA KYGLKVAYHH HMGTGIQTKE ETDRLMANTD
PKLVGLLYDT GHIAVSDGDY MALLNAHIDR VVHVHFKDVR RSKEEECRAK GLTFQGSFLN
GMFTVPGDGD LDFKPVYDKL IANNYKGWIV VEAEQDPSKA NPLEMAQIAH RYIKQHLIEN
