ID A0A0A3AUF0_9PAST Unreviewed; 411 AA.
AC A0A0A3AUF0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:KGQ70660.1};
GN ORFNames=OA57_04640 {ECO:0000313|EMBL:KGQ70660.1};
OS Chelonobacter oris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Chelonobacter.
OX NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ70660.1, ECO:0000313|Proteomes:UP000030380};
RN [1] {ECO:0000313|EMBL:KGQ70660.1, ECO:0000313|Proteomes:UP000030380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1662 {ECO:0000313|EMBL:KGQ70660.1,
RC ECO:0000313|Proteomes:UP000030380};
RA Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT respiratory disease in Hermann's Tortoises.";
RL Submitted (NOV-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}.
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:KGQ70660.1}.
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DR EMBL; JSUM01000006; KGQ70660.1; -; Genomic_DNA.
DR RefSeq; WP_034614056.1; NZ_JSUM01000006.1.
DR AlphaFoldDB; A0A0A3AUF0; -.
DR STRING; 505317.OA57_04640; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000030380; 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 GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KGQ70660.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030380};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 216..312
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 215
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 275
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 288
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 411 AA; 44721 MW; D22B867FD66CB092 CRC64;
MAINMQRIKT LIDHLATISS GDSELTRLAF SPEDLTAREY LLDLCRALGL NVRIDEIGNA
IIRRDGIEND LPAVAFGSHI DTVVNAGKFD GPLGSIAGLE ILLQLCEQRQ QTRYPLELIL
FTCEESSRFN YATLGSKVMC GITNQAALSH LQDKNGVSLA EALAQIGLDF EKVDQAKRAA
QAFKCFIELH IEQGPRLENE NKTIGVVTGI AAPIRCIVKI HGQADHSGAT AMNYRHDALL
GGAELALELE RAAIRAGHET VATVGQMQAK PGVMNVVPGY CELLVDIRGT DIEARESVFL
ALQQKIDDVA KQRGLQIDLQ LIAKDQPIIL DSGMVNAVKH AADTLGYAYE IMPSGAGHDA
MHMATFCPTA MIFVPSHQGI SHNPLEHTDW QDIEAGVNVL QHVILQQAEL K
//