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Database: UniProt
Entry: A0A089KPW3_9BACL
LinkDB: A0A089KPW3_9BACL
Original site: A0A089KPW3_9BACL 
ID   A0A089KPW3_9BACL        Unreviewed;       428 AA.
AC   A0A089KPW3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:AIQ51221.1};
GN   ORFNames=R70331_06640 {ECO:0000313|EMBL:AIQ51221.1};
OS   Paenibacillus sp. FSL R7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ51221.1, ECO:0000313|Proteomes:UP000029487};
RN   [1] {ECO:0000313|EMBL:AIQ51221.1, ECO:0000313|Proteomes:UP000029487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ51221.1,
RC   ECO:0000313|Proteomes:UP000029487};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009284; AIQ51221.1; -; Genomic_DNA.
DR   RefSeq; WP_042173848.1; NZ_CP009284.1.
DR   AlphaFoldDB; A0A089KPW3; -.
DR   STRING; 1536773.R70331_06640; -.
DR   KEGG; paee:R70331_06640; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_024588_6_0_9; -.
DR   Proteomes; UP000029487; Chromosome.
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 AMIDOHYDROLASE; 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:AIQ51221.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029487};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          228..317
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         231
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         291
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         304
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   428 AA;  44720 MW;  706A56ED9C4CC9CA CRC64;
     MSAPVINVPA EQMMELLEEL AAFSAPGPGV SRLLYTPEWL QAQRFLQERM AALGMGVRTD
     GVGNVYGRFT GSQPAAKVIL TGSHIDTVLN GGHYDGAYGI AAAVTALHYL IQNFGQPLRT
     IEAVAFCEEE GSRFPLAYWG SGNVTGLYDG SEAERCADSA GVTIASAMAG CGLACRPEDR
     GAAAAAGYAG GGTPLREDIG AFVELHIEQG IVLEQAALDI GIVEAIAGQR RYSVKVAGST
     NHAGTTPMGL RRDALAGAAE MLLAMEQAAI AAGDPLVATC GKLEAAPGTP NVIPGEVQFT
     LDIRHSEAEA LEHFCSFILD VFAGLAAKRG LTLQVTATLA TSPAPMDTGL NQQLEHIARQ
     QGRSFRSMVS GAGHDAQLFA PICPTAMIFV PSRAGISHSP EEYSSPEELA AGLNLLTAAL
     YELAYKES
//
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