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 03-APR-2013, entry version 56.
DE RecName: Full=Acylase ACY 1;
DE Includes:
DE RecName: Full=Cephalosporin acylase;
DE EC=3.5.1.-;
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
CC converts GL-7ACA into 7-ACA; this enzyme displays some gamma
CC glutamyltranspeptidase activity.
CC -!- CATALYTIC ACTIVITY: 7-beta-(4-carboxybutanamido)-cephalosporanic
CC acid + H(2)O = 7-aminocephalosporanic acid + glutaric acid.
CC -!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a
CC peptide + a 5-L-glutamyl amino acid.
CC -!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L-
CC glutamate.
CC -!- SUBUNIT: Dimer of two non-identical chains processed from the same
CC precursor.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
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DR EMBL; X69020; CAA48785.1; -; Genomic_DNA.
DR PIR; S27199; S27199.
DR ProteinModelPortal; Q05053; -.
DR GO; GO:0003840; F:gamma-glutamyltransferase activity; IEA:EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR000101; GGT_peptidase.
DR PANTHER; PTHR11686; PTHR11686; 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
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 1 Removed (By similarity).
FT CHAIN 2 ?367 Acylase ACY 1 large subunit (By
FT similarity).
FT /FTId=PRO_0000011082.
FT CHAIN 368 558 Acylase ACY 1 small subunit (By
FT similarity).
FT /FTId=PRO_0000011083.
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
//
