ID   AMAA_GEOSE              Reviewed;         370 AA.
AC   P37112;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   13-SEP-2023, entry version 90.
DE   RecName: Full=N-acyl-L-amino acid amidohydrolase;
DE            Short=L-aminoacylase;
DE            EC=3.5.1.14;
GN   Name=amaA; Synonyms=ama;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, AND
RP   CHARACTERIZATION.
RC   STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX   PubMed=8285691; DOI=10.1128/aem.59.11.3878-3888.1993;
RA   Sakanyan V., Desmarez L., Legrain C., Charlier D.R.M., Mett I.,
RA   Kochikyan A., Savchenko A., Boyen A., Falmagne P., Pirard A.,
RA   Glansdorff N.;
RT   "Gene cloning, sequence analysis, purification, and characterization of a
RT   thermostable aminoacylase from Bacillus stearothermophilus.";
RL   Appl. Environ. Microbiol. 59:3878-3888(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX   PubMed=9023955; DOI=10.1128/aem.63.2.763-766.1997;
RA   Batisse N., Weigel P., Lecocq M., Sakanyan V.;
RT   "Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase
RT   and aminoacylase are organized in a common operon in Bacillus
RT   stearothermophilus.";
RL   Appl. Environ. Microbiol. 63:763-766(1997).
CC   -!- FUNCTION: Hydrolyzes most efficiently N-acetyl derivatives of aromatic
CC       amino acids but is also active on other amino acids. L-stereospecific.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-
CC         amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14;
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; EC=3.5.1.14;
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; X74289; CAA52342.1; -; Genomic_DNA.
DR   EMBL; Y08753; CAA70000.1; -; Genomic_DNA.
DR   PIR; I40358; I40358.
DR   AlphaFoldDB; P37112; -.
DR   SMR; P37112; -.
DR   GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF166; AMIDOHYDROLASE YHAA-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Direct protein sequencing; Hydrolase.
FT   CHAIN           1..370
FT                   /note="N-acyl-L-amino acid amidohydrolase"
FT                   /id="PRO_0000061949"
SQ   SEQUENCE   370 AA;  41676 MW;  479AF1559DB527FB CRC64;
     MTKEEIKRLV DEVKTDVIAW RRHLHAHPEL SFQEEKTAQF VYETLQSFGH LELSRPTKTS
     VMARLIGQQP GRVVAIRADM DALPIQEENT FEFASKNPGV MHACGHDGHT AMLLGTAKIF
     SQLRDDIRGE IRFLFQHAEE LFPGGAEEMV QAGVMDGVDV VIGTHLWSPL ERGKIGIVYG
     PMMAAPDRFF IRIIGKGGHG AMPHQTIDAI AIGAQVVTNL QHIVSRYVDP LEPLVLSVTQ
     FVAGTAHNVL PGEVEIQGTV RTFDETLRRT VPQWMERIVK GITEAHGASY EFRFDYGYRP
     VINYDEGDPR HGGNGVRAVR RRGSGPLETE HGRRRFLRLF AKSARQLFLR RRGQCRKRHR
     LPAPPPALYD
//