PAC1_PSES3
ID PAC1_PSES3 Reviewed; 558 AA.
AC P15557;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 78.
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 SE83).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=309;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 368-388,
RP AND SUBUNIT.
RC STRAIN=SE83;
RX PubMed=3680178; DOI=10.1128/jb.169.12.5821-5826.1987;
RA Matsuda A., Toma K., Komatsu K.;
RT "Nucleotide sequences of the genes for two distinct cephalosporin acylases
RT from a Pseudomonas strain.";
RL J. Bacteriol. 169:5821-5826(1987).
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. {ECO:0000269|PubMed:3680178}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M18279; AAA88424.1; -; Genomic_DNA.
DR PIR; B28392; B28392.
DR AlphaFoldDB; P15557; -.
DR SMR; P15557; -.
DR MEROPS; T03.001; -.
DR BRENDA; 3.5.1.93; 5085.
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:0000269|PubMed:3680178"
FT CHAIN 2..?367
FT /note="Acylase ACY 1 large subunit"
FT /id="PRO_0000011080"
FT CHAIN 368..558
FT /note="Acylase ACY 1 small subunit"
FT /id="PRO_0000011081"
FT ACT_SITE 368
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 58095 MW; 9659691DE0DC528B CRC64;
MNAPVPVPRV ADFTCEKKPA SGSRGMVVTN HPLASAAGAQ ILLAGGNAID AAVASLFALT
VAEPMMVGIL GGGLSHIRLA DGRHVVIDNL STAPGKATAE MYECLSDEIG KQRDTRDRQN
VVGAKAVAVP GALKGWCEAL ARFGTLPLAE VLQPAIGLAE RGFVVTPYLS NCITDNAGDL
ARDPGLAAML LPGGKPLQPG MRLVQSDYAA SLKLIAAEGP DALYGGKLGR ALTDYMAANG
GLIDQADLAN YRIELREPIR GSYRGYEIIG PPPPSSSGVH ITQMLNILEG YDIGSLGFGS
TDAVHLLAEA LKIAFADRAV ATADPAFVKV PVARLIDKAY ADERRALIEM EQAKSWTAGL
SGGESADTTH VTVADAMGNV VSATQTINGL FGACVQIPGT GMIANNYMYN FDPHPGRALS
IAPGKRVFTS MAPMMALKEG RIAFALGLPG ALRIFPSALQ AIVNLIDHRM SLQEAVEAPR
VWTEGGVLEL EEAIPEAVAQ ALIARGHKVV RSPRVAGGMN AIAFNPDGTL TGAACWRADG
TPVAISGGLA RAGARFTI
