IOLI_BACSU
ID IOLI_BACSU Reviewed; 278 AA.
AC P42419;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
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; Synonyms=yxdH; OrderedLocusNames=BSU39680; ORFNames=B65B;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7952181; DOI=10.1099/13500872-140-9-2289;
RA Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y.;
RT "Cloning and nucleotide sequencing of a 15 kb region of the Bacillus
RT subtilis genome containing the iol operon.";
RL Microbiology 140:2289-2298(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=168 / 60015;
RX PubMed=16461681; DOI=10.1128/aem.72.2.1310-1315.2006;
RA Yoshida K., Yamaguchi M., Morinaga T., Ikeuchi M., Kinehara M., Ashida H.;
RT "Genetic modification of Bacillus subtilis for production of D-chiro-
RT inositol, an investigational drug candidate for treatment of type 2
RT diabetes and polycystic ovary syndrome.";
RL Appl. Environ. Microbiol. 72:1310-1315(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=12112707; DOI=10.1002/prot.10159;
RA Zhang R.G., Dementieva I., Duke N., Collart F., Quaite-Randall E.,
RA Alkire R., Dieckman L., Maltsev N., Korolev O., Joachimiak A.;
RT "Crystal structure of Bacillus subtilis iolI shows endonuclease IV fold
RT with altered Zn binding.";
RL Proteins 48:423-426(2002).
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:0000269|PubMed:16461681}.
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 Evidence={ECO:0000269|PubMed:16461681};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16461681};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:16461681};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16461681};
CC Note=Binds 1 divalent metal cation per subunit. Can use Mn(2+), Fe(2+)
CC or Co(2+). {ECO:0000269|PubMed:16461681};
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; D14399; BAA03298.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16004.1; -; Genomic_DNA.
DR PIR; A69646; A69646.
DR RefSeq; NP_391847.1; NC_000964.3.
DR RefSeq; WP_003244546.1; NZ_JNCM01000034.1.
DR PDB; 1I60; X-ray; 1.60 A; A=1-278.
DR PDB; 1I6N; X-ray; 1.80 A; A=1-278.
DR PDBsum; 1I60; -.
DR PDBsum; 1I6N; -.
DR AlphaFoldDB; P42419; -.
DR SMR; P42419; -.
DR STRING; 224308.BSU39680; -.
DR jPOST; P42419; -.
DR PaxDb; P42419; -.
DR PRIDE; P42419; -.
DR DNASU; 937582; -.
DR EnsemblBacteria; CAB16004; CAB16004; BSU_39680.
DR GeneID; 937582; -.
DR KEGG; bsu:BSU39680; -.
DR PATRIC; fig|224308.179.peg.4293; -.
DR eggNOG; COG1082; Bacteria.
DR InParanoid; P42419; -.
DR OMA; YIEIRTM; -.
DR PhylomeDB; P42419; -.
DR BioCyc; BSUB:BSU39680-MON; -.
DR BioCyc; MetaCyc:BSU39680-MON; -.
DR BRENDA; 5.3.99.11; 658.
DR UniPathway; UPA00076; -.
DR EvolutionaryTrace; P42419; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Cobalt; Iron; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..278
FT /note="Inosose isomerase"
FT /id="PRO_0000084215"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 200
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1I60"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1I60"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 76..96
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 114..132
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1I60"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:1I60"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:1I60"
FT HELIX 257..272
FT /evidence="ECO:0007829|PDB:1I60"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1I60"
SQ SEQUENCE 278 AA; 31656 MW; 11D54EEBAF14710C CRC64;
MKLCFNEATT LENSNLKLDL ELCEKHGYDY IEIRTMDKLP EYLKDHSLDD LAEYFQTHHI
KPLALNALVF FNNRDEKGHN EIITEFKGMM ETCKTLGVKY VVAVPLVTEQ KIVKEEIKKS
SVDVLTELSD IAEPYGVKIA LEFVGHPQCT VNTFEQAYEI VNTVNRDNVG LVLDSFHFHA
MGSNIESLKQ ADGKKIFIYH IDDTEDFPIG FLTDEDRVWP GQGAIDLDAH LSALKEIGFS
DVVSVELFRP EYYKLTAEEA IQTAKKTTVD VVSKYFSM
