IOLD2_BACCZ
ID IOLD2_BACCZ Reviewed; 644 AA.
AC Q4V1F5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase 2 {ECO:0000255|HAMAP-Rule:MF_01669};
DE Short=THcHDO hydrolase 2 {ECO:0000255|HAMAP-Rule:MF_01669};
DE EC=3.7.1.22 {ECO:0000255|HAMAP-Rule:MF_01669};
GN Name=iolD2 {ECO:0000255|HAMAP-Rule:MF_01669};
GN OrderedLocusNames=pE33L466_0302;
OS Bacillus cereus (strain ZK / E33L).
OG Plasmid pE33L466.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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:0000255|HAMAP-Rule:MF_01669}.
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:0000255|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01669};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 3/7. {ECO:0000255|HAMAP-
CC Rule:MF_01669}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000255|HAMAP-
CC Rule:MF_01669}.
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DR EMBL; CP000040; AAY60452.1; -; Genomic_DNA.
DR RefSeq; WP_001195334.1; NZ_CP009967.1.
DR AlphaFoldDB; Q4V1F5; -.
DR SMR; Q4V1F5; -.
DR EnsemblBacteria; AAY60452; AAY60452; pE33L466_0302.
DR KEGG; bcz:pE33L466_0302; -.
DR PATRIC; fig|288681.22.peg.5504; -.
DR UniPathway; UPA00076; UER00145.
DR Proteomes; UP000002612; Plasmid pE33L466.
DR GO; GO:0102481; F:3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase activity; IEA:UniProtKB-EC.
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 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 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; NAD; Plasmid; Thiamine pyrophosphate.
FT CHAIN 1..644
FT /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase
FT 2"
FT /id="PRO_0000352531"
FT REGION 442..522
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 65
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
SQ SEQUENCE 644 AA; 71017 MW; B3A6EF58DF3D2F60 CRC64;
MQTVRMTTAQ ALVKFLNQQY IEFDGEQQKF IKGIFTIFGH GNVVGLGQAL EEDAGELEVY
QGRNEQGMAN AAMAFAKQKH RKQIMACTSS VGPGSANMIT SAATASANNI PVLLLPGDVF
ATRQPDPVLQ QIEQTHDLSI STNDAFRAVS KYWDRINRPE QLMTAMIQAM RVLTNPADTG
AVTICLPQDV QGEAWDFPSY FFQKCVHRIE RRLPTRASLA DAVEMIKRKK KPVMICGGGV
RYAEAAEELK QFAEAFRIPF GETQAGKSAI ESSHPYNLGG IGVTGNLAAN TIAKEADLVI
GIGTRFTDFT TASKQLFQNE EVEFVNINIS EFHANKLDAL KVIADAKEAL LALINELQAI
EYRSSYTVEI AAAKEFWETE LARLHNIRFT GQDFKPEVEG HFDDNLNEYV DALGTQLTQT
AVIGEMNTLL DEDAIIVGAA GSLPGDLQRM WTSRKPNTYH MEYGYSCMGY EVAGALGAKL
AEPSKEVYAM VGDGSYQMLH SELVTSLQEN KKINVLLFDN SGFGCINNLQ MGNGMGSFGT
EFRYRNEETR KLNGAIMKID FAASAAGYGV KTYRVTSVEQ LQEALKDAKK QTVSTLIDIK
VLPKTMTNGY ESWWHVGVAE VSNSQSVQAA YESKVSNLQK ARSY
