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Database: UniProt
Entry: A0A0F0FC17_9BURK
LinkDB: A0A0F0FC17_9BURK
Original site: A0A0F0FC17_9BURK 
ID   A0A0F0FC17_9BURK        Unreviewed;       415 AA.
AC   A0A0F0FC17;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:KJK17836.1};
GN   ORFNames=UB46_34715 {ECO:0000313|EMBL:KJK17836.1};
OS   Burkholderiaceae bacterium 16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae.
OX   NCBI_TaxID=1619952 {ECO:0000313|EMBL:KJK17836.1, ECO:0000313|Proteomes:UP000033515};
RN   [1] {ECO:0000313|EMBL:KJK17836.1, ECO:0000313|Proteomes:UP000033515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16 {ECO:0000313|EMBL:KJK17836.1,
RC   ECO:0000313|Proteomes:UP000033515};
RA   Roco C.A., Bergaust L., Bakken L., Yavitt J., Shapleigh J.P.;
RT   "The modularity of denitrifying soil bacteria: using gas kinetics and
RT   genome sequencing to connect denitrifier phenotype to genotype.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC       1};
CC   -!- SIMILARITY: Belongs to the peptidase M20 family.
CC       {ECO:0000256|ARBA:ARBA00006153}.
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:KJK17836.1}.
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DR   EMBL; JYOD01000107; KJK17836.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0FC17; -.
DR   STRING; 1619952.UB46_34715; -.
DR   PATRIC; fig|1619952.3.peg.534; -.
DR   Proteomes; UP000033515; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03884; M20_bAS; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01879; hydantase; 1.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJK17836.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          218..318
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   415 AA;  44178 MW;  F2A105774A2E4BD6 CRC64;
     MDQQYLPRIN AARLWQSLMD LAQIGATPKG GVCRIALTEL DRQGRDLVVG RCREAGLAVR
     TDEVGNVFAR RAGSDADARA VATGSHIDTQ PSGGKFDGNF GVLAGLEVMR TLNDLGIVTR
     APLELAFWTN EEGTRFTPVM MGSGAFAGVF GAEFIRAQRD LDGISVGEAL EQIGYRGEQP
     VGEVPGGMFA AYFEAHIEQG PVLEAAGLPI GVVSGALGQQ WYDVAVTGMD AHAGPTPLAL
     RHDAMLAAAR MIDEVNRIAV AEAPHGRGTV GYVQVTPNSR NVIPGRVDFS VDFRNLSQAG
     LDRMDAAMRT TFAEIAERGA VSVEIRQVVK FEPCVFAPEC VDSVRRAAAA LGLPHMDVVS
     GAGHDAVYVA QRAPTGMIFV PCKDGISHNE LEDALPEHIE AGANVLLQAM LEHAR
//
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