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Database: UniProt
Entry: A0A0R1JNB8_9LACO
LinkDB: A0A0R1JNB8_9LACO
Original site: A0A0R1JNB8_9LACO 
ID   A0A0R1JNB8_9LACO        Unreviewed;       373 AA.
AC   A0A0R1JNB8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-OCT-2025, entry version 38.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:KRK72933.1};
GN   ORFNames=FD02_GL001353 {ECO:0000313|EMBL:KRK72933.1};
OS   Lacticaseibacillus nasuensis JCM 17158.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK72933.1, ECO:0000313|Proteomes:UP000051804};
RN   [1] {ECO:0000313|EMBL:KRK72933.1, ECO:0000313|Proteomes:UP000051804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK72933.1,
RC   ECO:0000313|Proteomes:UP000051804};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Genome Announc. 6:8322-8322(2015).
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:KRK72933.1}.
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DR   EMBL; AZDJ01000016; KRK72933.1; -; Genomic_DNA.
DR   RefSeq; WP_054723014.1; NZ_AZDJ01000016.1.
DR   AlphaFoldDB; A0A0R1JNB8; -.
DR   STRING; 1291734.FD02_GL001353; -.
DR   PATRIC; fig|1291734.4.peg.1392; -.
DR   OrthoDB; 9796020at2; -.
DR   Proteomes; UP000051804; 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:UP000051804};
KW   Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         152
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         152
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         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   SITE            154
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT   MOD_RES         152
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ   SEQUENCE   373 AA;  40331 MW;  44F68C874DAFE89F CRC64;
     MYDVLIKNAL TARRQPIEIA LNGNKIAAVA TQLVGATAQQ VIDLHGATYV SAGWIDDHVH
     CDEQLTLYYD DPDEDGYKTG VTTVVDAGST GADNIRDFYQ RTRAKITNVY ALINIGRTGI
     LAQDELGDLS KIDRDALLAA HHELPDFILG IKARESHSVV VDNGIKPLLA ARSYAALMGG
     LPVMVHVGAK PPELQDILQA MGPGDILTHA YNGKPNGMVA PDGTIHQFVY DAYDRGVIFD
     VGHGTDSFNF RTMSIARDHG LDPQSLSTDI YHRNREDGPV VNMATTMAKM LAVGYTLPEV
     IRMVTLAPAQ NMHLLTKGRL RPGADADLTI FTVTAGEQPL TDANGNTRTG HAIITPRTTI
     VGGKVYDLEA THD
//
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