ID   A0A1Q5SUV1_9BRAD        Unreviewed;       416 AA.
AC   A0A1Q5SUV1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:OKO91763.1};
GN   ORFNames=AC629_02145 {ECO:0000313|EMBL:OKO91763.1};
OS   Bradyrhizobium sp. NAS80.1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1680159 {ECO:0000313|EMBL:OKO91763.1, ECO:0000313|Proteomes:UP000186592};
RN   [1] {ECO:0000313|EMBL:OKO91763.1, ECO:0000313|Proteomes:UP000186592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAS80.1 {ECO:0000313|EMBL:OKO91763.1,
RC   ECO:0000313|Proteomes:UP000186592};
RA   Granada C., Sant'Anna F.H., Passaglia L.;
RT   "Genome of Bradyrhizobium sp. NAS80.1.";
RL   Submitted (JUL-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:OKO91763.1}.
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DR   EMBL; LGHL01000007; OKO91763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5SUV1; -.
DR   OrthoDB; 9808195at2; -.
DR   Proteomes; UP000186592; 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:OKO91763.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          216..315
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   416 AA;  44168 MW;  50ACC397BC657DB9 CRC64;
     MSRAATNLQI DSARLWGSIH ETAQFGATQK GGVRRLTLST EDKQVRNWFR KACEDAGLEV
     HVDALGSMFG LRKGRDMSKP PVGIGSHLDT QPTGGKYDGI LGTLGALEVI RTLNDAGIET
     EAPICVVNWT NEEGSRFAPA MMASAAYVGD FTTDDILSRK DAEGVTVSQA LDGIGYRGDK
     PVGFQKLGCF VELHIEQGPI LEAEGKTIGV VDSGQGVLWY DGKISGFESH AGSTPMPLRR
     DALATLSEIV LAMEAIAKKH GPKAVGTIGE AVIVNPSRNV IPGEIAFTVD CRSADGTIMD
     ALDRDLRAAI AEIAARRKVE VKIDLVWRKP PTHFDPKLIA AVENAANTLG YSSRRITSGA
     GHDACNLNTV MPAAMVFVPC KDGISHNELE DATQPDCAAG TNVLLHTVLA IAGVAS
//