ID A0A3R7K9Z1_9STRA Unreviewed; 439 AA.
AC A0A3R7K9Z1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=N-acyl-aliphatic-L-amino acid amidohydrolase {ECO:0000256|ARBA:ARBA00011913};
DE EC=3.5.1.14 {ECO:0000256|ARBA:ARBA00011913};
DE AltName: Full=N-acyl-L-amino-acid amidohydrolase {ECO:0000256|ARBA:ARBA00029656};
GN ORFNames=BBI17_006870 {ECO:0000313|EMBL:RLN38540.1}, BBO99_00005980
GN {ECO:0000313|EMBL:RLN78416.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN38540.1, ECO:0000313|Proteomes:UP000285883};
RN [1] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN38540.1}, and Chile4
RC {ECO:0000313|EMBL:RLN78416.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR036696-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR036696-
CC 2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:RLN38540.1}.
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DR EMBL; MAYM02000401; RLN38540.1; -; Genomic_DNA.
DR EMBL; MBDN02000190; RLN78416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7K9Z1; -.
DR STRING; 325452.A0A3R7K9Z1; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR PANTHER; PTHR45892:SF1; AMINOACYLASE-1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF036696; ACY-1; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036696-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000285624};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR036696-2}.
FT DOMAIN 205..333
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
SQ SEQUENCE 439 AA; 49121 MW; 29117C5309956F67 CRC64;
MNQNPFAMAP RTSAVERLLE YIRIPSVSGD GPSGSYGECA AWIKSYLEEE GLSVQVFSPI
AHKPIIVATW QGQDPSLPSL LLNSHYDVVP ALRKHWTHEP FDVRNSVGCR KDPKVLEDGM
IYGRGIQDMK SVGVQYVEAI HRLKASGFVP SRNVHLLFVP DEEIGGTDGM EAFLVSEQYK
SIQPVAFALD EGLANPNDAF TVFYGERVPW WFYVKATGPT GHGSRFIKNT ATSKIIDVCN
KALTFRAEQE ALLSADTGCK HGDIKKRNLG DVTTVNLNML KSGISQDGGK THALNVIPTE
AVAGFDVRIS PNMDLKEFKA MLDKWCSAEG LSWEFVSWWK NPLHEHYTTA IDDTNIWWKL
FNEGCEETGV PVETEVFPAA TDSRFLRQLG IPALGFSPMN KTEILLHEHN ESLHQDTFLR
GIEVYETIFR RMFTYTGAM
//
