IOLN_THEMA
ID IOLN_THEMA Reviewed; 311 AA.
AC Q9WYP4;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=3-dehydro-scyllo-inosose hydrolase {ECO:0000305|PubMed:23441918};
DE EC=3.7.1.- {ECO:0000269|PubMed:23441918};
DE AltName: Full=Diketo-inositol hydrolase {ECO:0000303|PubMed:23441918};
GN Name=iolN {ECO:0000303|PubMed:23441918};
GN OrderedLocusNames=TM_0413 {ECO:0000312|EMBL:AAD35498.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, SUBUNIT, AND REACTION
RP MECHANISM.
RX PubMed=23441918; DOI=10.1111/1462-2920.12096;
RA Rodionova I.A., Leyn S.A., Burkart M.D., Boucher N., Noll K.M.,
RA Osterman A.L., Rodionov D.A.;
RT "Novel inositol catabolic pathway in Thermotoga maritima.";
RL Environ. Microbiol. 15:2254-2266(2013).
CC -!- FUNCTION: Catalyzes the ring-opening hydrolysis of 3-dehydro-scyllo-
CC inosose (diketo-inositol) to 5-dehydro-L-gluconate, and thus probably
CC functions in a myo-inositol degradation pathway together with IolG,
CC IolM and IolO. {ECO:0000269|PubMed:23441918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-scyllo-inosose + H2O = 5-dehydro-L-gluconate + H(+);
CC Xref=Rhea:RHEA:53288, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:137015, ChEBI:CHEBI:137108;
CC Evidence={ECO:0000269|PubMed:23441918};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P83772, ECO:0000305|PubMed:23441918};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P83772,
CC ECO:0000305|PubMed:23441918};
CC -!- PATHWAY: Polyol metabolism; myo-inositol metabolism.
CC {ECO:0000305|PubMed:23441918}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:23441918}.
CC -!- MISCELLANEOUS: The proposed catalytic mechanism involves two water
CC molecules. The first molecule is bound as a bridge between the two
CC metal ions and attacks the carbonyl carbon of the substrate. The second
CC water molecule, that is bound to metal 1, likely functions as a proton
CC donor in catalysis. {ECO:0000305|PubMed:23441918}.
CC -!- SIMILARITY: Belongs to the creatininase superfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35498.1; -; Genomic_DNA.
DR PIR; C72381; C72381.
DR RefSeq; NP_228223.1; NC_000853.1.
DR AlphaFoldDB; Q9WYP4; -.
DR SMR; Q9WYP4; -.
DR STRING; 243274.THEMA_02660; -.
DR EnsemblBacteria; AAD35498; AAD35498; TM_0413.
DR KEGG; tma:TM0413; -.
DR PATRIC; fig|243274.5.peg.418; -.
DR eggNOG; COG1402; Bacteria.
DR InParanoid; Q9WYP4; -.
DR OMA; NWYHAIQ; -.
DR BioCyc; MetaCyc:MON-17950; -.
DR UniPathway; UPA00914; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006020; P:inositol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10310; -; 1.
DR InterPro; IPR024087; Creatininase-like_sf.
DR InterPro; IPR003785; Creatininase/forma_Hydrolase.
DR PANTHER; PTHR35005; PTHR35005; 1.
DR Pfam; PF02633; Creatininase; 1.
DR SUPFAM; SSF102215; SSF102215; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..311
FT /note="3-dehydro-scyllo-inosose hydrolase"
FT /id="PRO_0000440856"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
SQ SEQUENCE 311 AA; 34947 MW; D81586D6B096CBBA CRC64;
MERPTGVYFQ TMTMKQIRER LKQCDLIIIP VGSTENHGPN APTGEDTFLV TRMAEQVALK
TGCTVAEPIW YGYHPYHHIG MPGTVPVKDE AFIDYLVSVI AGFWNTGFRK QILLNGHGQE
FVIPIAIHKF AKIFQVPAII INLNWYHAIQ DKFKTKEEGG PYETPFIHAD EVETSWSLAL
FPEFMHQEWA VDTEPKGFLP EGHIDKAGNL LHRPIAWYGH VGGGPIEVVA YPEGVVGKAT
LASAEKAKEG VEALLDYLEK LVRDIMERFP AGKLPPAEML SQRPKEELEA LTKEPLTEGW
RNLYTAGNLW G
