ID A0A3Q3MAS9_9TELE Unreviewed; 309 AA.
AC A0A3Q3MAS9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acyl-aromatic-L-amino acid amidohydrolase {ECO:0000256|ARBA:ARBA00034807};
DE EC=3.5.1.114 {ECO:0000256|ARBA:ARBA00034807};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000024493.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000024493.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-
CC substituted L-cysteine; Xref=Rhea:RHEA:36855, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:58717, ChEBI:CHEBI:58718;
CC EC=3.5.1.114; Evidence={ECO:0000256|ARBA:ARBA00036061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate +
CC an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824,
CC ChEBI:CHEBI:138093; EC=3.5.1.114;
CC Evidence={ECO:0000256|ARBA:ARBA00036225};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR018001-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR018001-3};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00037831}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00037831}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000256|ARBA:ARBA00006173}.
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DR AlphaFoldDB; A0A3Q3MAS9; -.
DR STRING; 205130.ENSMAMP00000024493; -.
DR Ensembl; ENSMAMT00000025124.2; ENSMAMP00000024493.2; ENSMAMG00000016508.2.
DR GeneTree; ENSGT00390000001189; -.
DR InParanoid; A0A3Q3MAS9; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06909; M14_ASPA; 1.
DR Gene3D; 2.20.25.160; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00704; Aspartoacylase; 1.
DR InterPro; IPR016708; Aspartoacylase.
DR InterPro; IPR007036; Aste_AspA.
DR PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR PANTHER; PTHR15162:SF5; N-ACYL-AROMATIC-L-AMINO ACID AMIDOHYDROLASE (CARBOXYLATE-FORMING); 1.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF018001; Aspartoacylase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR018001-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR018001-3}.
FT ACT_SITE 174
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
SQ SEQUENCE 309 AA; 34557 MW; A9206525B9BE05BE CRC64;
MEHVSFPPLS RFAICGGTHG NEMTGVYMVR ELQKKKLEKA GSVSITSVLS NPRAVDVCKR
YIDKDLNRCF TNAFLSAPIT DLTPYEVKRA QELNAQLGPK GSEDAVDLIC DFHNTTANMG
LCLIFYTIDW LTLHIYKYIK SKITSVPVRL IQLDLPISEA YSLESVGKHS FAIEIGPQPC
GVLRADIFNI AKEALDLTME WIQKFNSGSS FEGDAVEAYN MAKSVDYPRD PTTGELTAVI
HPQLQDNDFK LLQPGDPVFL SFSGETVKHD GEELYPFFVN ECAYYEKKIA FHLARKITLA
IPSISVTRD
//
