ID A0A431W8U3_9BACI Unreviewed; 413 AA.
AC A0A431W8U3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:RTR31836.1};
GN ORFNames=EKG37_10010 {ECO:0000313|EMBL:RTR31836.1};
OS Bacillus yapensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2492960 {ECO:0000313|EMBL:RTR31836.1, ECO:0000313|Proteomes:UP000271374};
RN [1] {ECO:0000313|EMBL:RTR31836.1, ECO:0000313|Proteomes:UP000271374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XXST-01 {ECO:0000313|EMBL:RTR31836.1,
RC ECO:0000313|Proteomes:UP000271374};
RA Yu L., Xu X., Tang X.;
RT "Bacillus yapensis draft genome sequence.";
RL Submitted (DEC-2018) 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:RTR31836.1}.
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DR EMBL; RXNT01000007; RTR31836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A431W8U3; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000271374; 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:0000313|EMBL:RTR31836.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000271374};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 218..313
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 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 221
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 281
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 294
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
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 413 AA; 46519 MW; 8031D7A4F955B89C CRC64;
MAIKMREQKF EKDSVSEMIE WLATFGRTTN GGVTRPLFSK DWRKAQDALK DKMEVLQLQT
YFDRAGNLFG KLPGTELGSK TILTGSHIDT VIDGGKYDGA YGIIASLLAT SQLFQKYGYP
KKTIEVISLS EEEGSRFPLT FWGSRNISGA YNLETVKDVQ DGDGIHFLEA MKESGFDPKE
YQSNLRTDIE RFVEIHIEQG MILEKNQNTI GVVSHIVGQR RFTINVVGES NHAGTTPMYY
RKDAVSTASK LITYLTEKAK EFDPLLVATV GKLNVRPNVP NVVAGEVEFS LDIRHHQEDV
LNRYCEDIFA EFERLSTDLD VQISQWMDVK PIAMDEKMNQ VIRQLATEKN ISYQDIVSGA
GHDAQVFASI CPTTLIFVPS QDGISHSPKE FTRIEDLETG VELLTELLYK LAY
//
