ID   PAC1_PSESV              Reviewed;         558 AA.
AC   Q05053;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Acylase ACY 1 proenzyme;
DE   Includes:
DE     RecName: Full=Cephalosporin acylase;
DE              EC=3.5.1.93;
DE     AltName: Full=GL-7ACA acylase;
DE   Includes:
DE     RecName: Full=Gamma-glutamyltranspeptidase;
DE              Short=GGT;
DE              EC=2.3.2.2;
DE     AltName: Full=Glutathione hydrolase;
DE              EC=3.4.19.13;
DE   Contains:
DE     RecName: Full=Acylase ACY 1 large subunit;
DE   Contains:
DE     RecName: Full=Acylase ACY 1 small subunit;
GN   Name=acyI;
OS   Pseudomonas sp. (strain V22).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=33068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13 AND
RP   368-381.
RX   PubMed=1358202; DOI=10.1016/0167-4781(92)90155-s;
RA   Ishiye M., Niwa M.;
RT   "Nucleotide sequence and expression in Escherichia coli of the
RT   cephalosporin acylase gene of a Pseudomonas strain.";
RL   Biochim. Biophys. Acta 1132:233-239(1992).
CC   -!- FUNCTION: Besides the cephalosporin acylase I activity which converts
CC       GL-7ACA into 7-ACA; this enzyme displays some gamma
CC       glutamyltranspeptidase activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-
CC         aminocephalosporanate + glutarate; Xref=Rhea:RHEA:23508,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30921, ChEBI:CHEBI:58501,
CC         ChEBI:CHEBI:58693; EC=3.5.1.93;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC         5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC         Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC         ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC         ChEBI:CHEBI:78608; EC=2.3.2.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC         Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC         cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC         ChEBI:CHEBI:143103; EC=3.4.19.13;
CC   -!- SUBUNIT: Dimer of two non-identical chains processed from the same
CC       precursor.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X69020; CAA48785.1; -; Genomic_DNA.
DR   PIR; S27199; S27199.
DR   AlphaFoldDB; Q05053; -.
DR   SMR; Q05053; -.
DR   MEROPS; T03.001; -.
DR   GO; GO:0033968; F:glutaryl-7-aminocephalosporanic-acid acylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.246.130; -; 1.
DR   Gene3D; 3.60.20.40; -; 1.
DR   InterPro; IPR043138; GGT_lsub_C.
DR   InterPro; IPR000101; GGT_peptidase.
DR   InterPro; IPR043137; GGT_ssub.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR00066; g_glut_trans; 1.
DR   PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic resistance; Direct protein sequencing;
KW   Hydrolase; Transferase; Zymogen.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..?367
FT                   /note="Acylase ACY 1 large subunit"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011082"
FT   CHAIN           368..558
FT                   /note="Acylase ACY 1 small subunit"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011083"
FT   ACT_SITE        368
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   558 AA;  58040 MW;  22573EEACF69F5E4 CRC64;
     MNAPVPVPRV ADFTCEKKPA TGSRGMVVTN HPLASAAGAQ ILLAGGNAID AAVASLFALT
     VAEPMMVGIL GGGLSHIRLA DGRHVVIDNL STAPGKATAD MYECLSDEIG KQRDTRDREN
     VVGAKAVAVP GALKGWCEAL ARFGTLPLAE VLQPAIGLAE RGFVVTPYLS NCITDNAADL
     ARDPGLAAML LPGGQPLQPG MRLIQSDYAA SLKLIAAEGP EALYGGKLGR ALTDYMAANG
     GLIDQADLSN YRIELREPIR GSYRGYEIIG PPPPSSSGVH IAQMLNILEG YDIGALGFGS
     TDAVHLLAEA LKIAFADRAV ATADPAFVKV PVARLIDKAY ADERRALIAM EQAKSWTAGL
     SGGESADTTH VTVADAMGNV VSATQTINGL FGACVQTPGT GMIANNYMYN FDPHPGRALS
     IAPGKRVFTS MAPMMAVKEG RLAFALGLPG ALRIFPSALQ AIVNLIDHRM SLQEAVEAPR
     VWTEGGVLEL EEAIPESVAQ ALIARGHKVV RSPRVAGGMN AIAFNPDGTL TGAACWRADG
     TPVAISGGLA RAGARFTI