ID A0A0E0L972_ORYPU Unreviewed; 467 AA.
AC A0A0E0L972;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
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};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC06G06590.2};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC06G06590.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC06G06590.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0E0L972; -.
DR EnsemblPlants; OPUNC06G06590.2; OPUNC06G06590.2; OPUNC06G06590.
DR Gramene; OPUNC06G06590.2; OPUNC06G06590.2; OPUNC06G06590.
DR HOGENOM; CLU_021802_5_0_1; -.
DR Proteomes; UP000026962; Chromosome 6.
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; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR InterPro; IPR002933; Peptidase_M20.
DR NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR PANTHER; PTHR45892:SF3; PUTATIVE-RELATED; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF036696; ACY-1; 3.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036696-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Zinc {ECO:0000256|PIRSR:PIRSR036696-2}.
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
SQ SEQUENCE 467 AA; 51659 MW; 6C529B82B19DB4EA CRC64;
MNSSSDIWLK RTSVKLKPHF FFSKKEKRKR KIKLKTHSNL TMPPLRRRHR RRLLAVVAVL
LLSTVVAHPA AAAFTELESA QIGRFQDYLR IRTAHPSPDY AAAAAFLLPY AASLGLRAAT
LHFTPCKSKP LLLLTWQGTD PSLPSVLLNS HLDSVPAEPE QWVHPPFAAH RDAATGRVYA
RGAQDDKCLP IQYLEAIRGL RDAGFAPTRT LHISLVPDEE IGGADGFEKF AQSEEFRDLN
VGFMLDEGQA SLTDEFRVFY GDRLVWRLIV TATGAPGHGS KLFDGAAVEN LMDCIETIAG
FREAQFGMVK SGQRGPGEVV SVNPVYMKAG TPSPTLMQKG PLRDLAGRPM VTPTNASNPW
WSVFEQAIKS AGGKLAKPEI LSSTTDSRFI RQLGIPALGF SPMINTPILL HDNNEVIDLG
LLLFILGYNV MLKLRDVSNP QFLEDKVFLR GIKVYEHIIR ALSSFKG
//
