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Database: UniProt
Entry: A0A0A3AUF0_9PAST
LinkDB: A0A0A3AUF0_9PAST
Original site: A0A0A3AUF0_9PAST 
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
//
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