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Database: UniProt
Entry: D7UWT3_LISGR
LinkDB: D7UWT3_LISGR
Original site: D7UWT3_LISGR 
ID   D7UWT3_LISGR            Unreviewed;       375 AA.
AC   D7UWT3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   28-JAN-2026, entry version 56.
DE   SubName: Full=Amidohydrolase, EF_0837/AHA_3915 family {ECO:0000313|EMBL:EFI84141.1};
GN   ORFNames=HMPREF0556_10694 {ECO:0000313|EMBL:EFI84141.1};
OS   Listeria grayi DSM 20601.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
OC   Listeria.
OX   NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI84141.1, ECO:0000313|Proteomes:UP000010119};
RN   [1] {ECO:0000313|EMBL:EFI84141.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI84141.1};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFI84141.1}.
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DR   EMBL; ACCR02000003; EFI84141.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7UWT3; -.
DR   STRING; 525367.HMPREF0556_10694; -.
DR   eggNOG; COG3964; Bacteria.
DR   HOGENOM; CLU_036699_1_0_9; -.
DR   Proteomes; UP000010119; Unassembled WGS sequence.
DR   GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR020043; Deacetylase_Atu3266-like.
DR   InterPro; IPR047601; EF_0837-like.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR03583; EF_0837; 1.
DR   NCBIfam; NF006689; PRK09237.1; 1.
DR   PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR   PANTHER; PTHR42717:SF1; IMIDAZOLONEPROPIONASE AND RELATED AMIDOHYDROLASES; 1.
DR   Pfam; PF22647; EF_0837-like_N; 1.
DR   PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010119};
KW   Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   SITE            161
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT   MOD_RES         159
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ   SEQUENCE   375 AA;  41332 MW;  B9F3587D6F9D4E47 CRC64;
     MYEKEGMTMY DILIKNGRTP SRETIDIAIQ ADKIAEIGSN LEVEAQRVID LHGDSYVSAG
     WIDDHVHCYE EMDLYYDSPD EQGYKAGVTT IIDAGSTGAE NMDRFHQLLK DVKTNVFAMI
     NISKTGIVRQ DELSDMRNIQ AELVREKVKA FPAFIVGLKA RMSKTVVGDN DILPLEEAKK
     IQQQVDLPLM VHIGSNPPTL ETILAELEQG DIVTHCFNGK ANGIFDKENH SIKNFAKEAY
     EKGIIFDVGH GTDSFNFDVA EAAKAEHITP YTISTDLYHR NRESGPVYDM ATTLEKLLAV
     GYSLAEIIPM VTSHPAASFK LKGKGELKKG ADADITIFNV GSGSKELVDS NGNTRTINQL
     IKPTTAIIGG AIYDI
//
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