ID   ARYA_PSEPU              Reviewed;          28 AA.
AC   P35902;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Arylalkyl acylamidase;
DE            EC=3.5.1.76;
DE   Flags: Fragment;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=SC2;
RX   PubMed=1396711; DOI=10.1111/j.1432-1033.1992.tb17299.x;
RA   Shimizu S., Ogawa J., Chung M.C.-M., Yamada H.;
RT   "Purification and characterization of a novel enzyme, arylalkyl
RT   acylamidase, from Pseudomonas putida Sc2.";
RL   Eur. J. Biochem. 209:375-382(1992).
CC   -!- FUNCTION: Shows a strict specificity for N-acetyl arylalkylamines but
CC       not acetanilide derivatives.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetylarylalkylamine + H2O = acetate + an aralkylamine;
CC         Xref=Rhea:RHEA:10352, ChEBI:CHEBI:15377, ChEBI:CHEBI:18096,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:88332; EC=3.5.1.76;
CC   -!- ACTIVITY REGULATION: Activated by divalent metal ions. Inhibited by
CC       certain thiol reagents.
CC   -!- SUBUNIT: Homotetramer.
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DR   PIR; S29285; S29285.
DR   AlphaFoldDB; P35902; -.
DR   GO; GO:0047416; F:arylalkyl acylamidase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN           1..>28
FT                   /note="Arylalkyl acylamidase"
FT                   /id="PRO_0000064687"
FT   NON_TER         28
SQ   SEQUENCE   28 AA;  3150 MW;  933B9D0560084488 CRC64;
     TRRTAFLFDE LSLWHSASQY ALILPVGG