ID YODQ_BACSU Reviewed; 436 AA.
AC O34984; Q796B3; Q7BVV8;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Uncharacterized metallohydrolase YodQ;
DE EC=3.-.-.-;
GN Name=yodQ; Synonyms=argE, yokP; OrderedLocusNames=BSU19710;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AF006665; AAB81157.1; -; Genomic_DNA.
DR EMBL; AF015775; AAB72071.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13862.1; -; Genomic_DNA.
DR PIR; H69588; H69588.
DR RefSeq; NP_389852.1; NC_000964.3.
DR RefSeq; WP_010886532.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34984; -.
DR SMR; O34984; -.
DR STRING; 224308.BSU19710; -.
DR MEROPS; M20.A21; -.
DR PaxDb; 224308-BSU19710; -.
DR DNASU; 940044; -.
DR EnsemblBacteria; CAB13862; CAB13862; BSU_19710.
DR GeneID; 940044; -.
DR KEGG; bsu:BSU19710; -.
DR PATRIC; fig|224308.43.peg.2091; -.
DR eggNOG; COG0624; Bacteria.
DR InParanoid; O34984; -.
DR OrthoDB; 9792335at2; -.
DR PhylomeDB; O34984; -.
DR BioCyc; BSUB:BSU19710-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03895; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR033687; YodQ-like.
DR NCBIfam; TIGR01910; DapE-ArgE; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Cobalt; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..436
FT /note="Uncharacterized metallohydrolase YodQ"
FT /id="PRO_0000386550"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 436 AA; 48555 MW; 5E60E80AD6777BDD CRC64;
MRMQDIERKV IEWLDQHSAK AIRLLKRLIG EKSTLGSEFN AQAVVLEKLR QFHMDIDVWE
PSIKQLKQHP YFKSNRSDFH ESPNIVAKKT GAGGGRSLIL NGHIDVVPEG SVKDWKYEPY
QAVEENGKIY GRGSTDMKGG NTALLFALEA LHACDVKLKG DVLFQSVVDE ECGGAGTLSA
IMRGYRADGA LIPEPTNMKL FIKQQGSMWF RITVKGLSAH GGTRYEGVSA IEKSMHVITA
IQELEKVRNA RISDPLYDNI PIPVPVNIGT ISGGAWPSSV ADRVVIEGRC GIAPHEKPEA
VKLELENWLK DLEYHDEWFK RHPVQVEWFG AQWLPNDLPD DHPLISVLQS AYQKMKQTEP
IIEASPWGTD GGLLYHAGDT PVIVFGPGET KTAHQANEYI EVEAMIESAK IIALFVMDWC
GLHTDGEDAD AQVNKE
//
