IOLD_BACSU
ID IOLD_BACSU Reviewed; 637 AA.
AC P42415;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase;
DE Short=THcHDO hydrolase;
DE EC=3.7.1.22;
GN Name=iolD; Synonyms=yxdD; OrderedLocusNames=BSU39730; ORFNames=E83D;
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 SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=168 / 60015;
RX PubMed=18310071; DOI=10.1074/jbc.m708043200;
RA Yoshida K., Yamaguchi M., Morinaga T., Kinehara M., Ikeuchi M., Ashida H.,
RA Fujita Y.;
RT "Myo-inositol catabolism in Bacillus subtilis.";
RL J. Biol. Chem. 283:10415-10424(2008).
CC -!- FUNCTION: Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-
CC trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate
CC (5DG). {ECO:0000269|PubMed:18310071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O = 5-deoxy-D-
CC glucuronate + H(+); Xref=Rhea:RHEA:25836, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28446, ChEBI:CHEBI:58852; EC=3.7.1.22;
CC Evidence={ECO:0000269|PubMed:18310071};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 3/7.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03293.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D14399; BAA03293.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB16009.2; -; Genomic_DNA.
DR PIR; D69645; D69645.
DR RefSeq; NP_391852.2; NC_000964.3.
DR RefSeq; WP_003242642.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42415; -.
DR SMR; P42415; -.
DR STRING; 224308.BSU39730; -.
DR jPOST; P42415; -.
DR PaxDb; P42415; -.
DR PRIDE; P42415; -.
DR EnsemblBacteria; CAB16009; CAB16009; BSU_39730.
DR GeneID; 937590; -.
DR KEGG; bsu:BSU39730; -.
DR PATRIC; fig|224308.179.peg.4298; -.
DR eggNOG; COG3962; Bacteria.
DR InParanoid; P42415; -.
DR OMA; PNTYHLE; -.
DR PhylomeDB; P42415; -.
DR BioCyc; BSUB:BSU39730-MON; -.
DR BioCyc; MetaCyc:BSU39730-MON; -.
DR BRENDA; 3.7.1.22; 658.
DR UniPathway; UPA00076; UER00145.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0102481; F:3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_01669; IolD; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR030817; Myo_inos_IolD.
DR InterPro; IPR023757; THcHDO_hydrolase_firmi.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR PANTHER; PTHR18968:SF9; PTHR18968:SF9; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR04377; myo_inos_iolD; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; NAD; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..637
FT /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione
FT hydrolase"
FT /id="PRO_0000090815"
FT REGION 442..522
FT /note="Thiamine pyrophosphate binding"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 637 AA; 70380 MW; BB8633F2B9358971 CRC64;
MGKKIRLTTA QALIKFLNQQ YIHVDGKEEP FVEGIFTIFG HGNVLGIGQA LEQDAGHLKV
YQGKNEQGMA HAAMAYSKQM LRRKIYAVST SVGPGAANLV AAAGTALANN IPVLLIPADT
FATRQPDPVL QQMEQEYSAA ITTNDALKPV SRYWDRITRP EQLMSSLLRA FEVMTDPAKA
GPATICISQD VEGEAYDFDE SFFVKRVHYI DRMQPSEREL QGAAELIKSS KKPVILVGGG
AKYSGARDEL VAISEAYNIP LVETQAGKST VEADFANNLG GMGITGTLAA NKAARQADLI
IGIGTRYTDF ATSSKTAFDF DKAKFLNINV SRMQAYKLDA FQVVADAKVT LGKLHGLLEG
YESEFGTTIR ELKDEWLAER ERLSKVTFKR EAFDPEIKNH FSQEVLNEYA DALNTELPQT
TALLTINETI PEDSVIICSA GSLPGDLQRL WHSNVPNTYH LEYGYSCMGY EVSGTLGLKL
AHPDREVYSI VGDGSFLMLH SELITAIQYN KKINVLLFDN SGFGCINNLQ MDHGSGSYYC
EFRTDDNQIL NVDYAKVAEG YGAKTYRANT VEELKAALED AKKQDVSTLI EMKVLPKTMT
DGYDSWWHVG VAEVSEQESV QKAYEAKEKK LESAKQY
