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BLO3_PSEAI
ID   BLO3_PSEAI              Reviewed;         275 AA.
AC   Q51429;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Beta-lactamase OXA-3;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=oxa3;
OS   Pseudomonas aeruginosa.
OG   Plasmid pMG25.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7785990; DOI=10.1128/aac.39.4.887;
RA   Sanschagrin F., Couture F., Levesque R.C.;
RT   "Primary structure of OXA-3 and phylogeny of oxacillin-hydrolyzing class D
RT   beta-lactamases.";
RL   Antimicrob. Agents Chemother. 39:887-893(1995).
CC   -!- FUNCTION: This is an oxacillin-hydrolyzing beta-lactamase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10103};
CC   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; L07945; AAC41449.1; -; Genomic_DNA.
DR   RefSeq; WP_063862540.1; NG_049595.1.
DR   AlphaFoldDB; Q51429; -.
DR   SMR; Q51429; -.
DR   KEGG; ag:AAC41449; -.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR002137; Beta-lactam_class-D_AS.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..275
FT                   /note="Beta-lactamase OXA-3"
FT                   /id="PRO_0000017027"
FT   ACT_SITE        72
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10103"
FT   BINDING         210..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         75
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  31879 MW;  4F9F95D755140146 CRC64;
     MAIRIFAILF STFVFGTFAH AQEGMRERSD WRKFFSEFQA KGTIVVADER QTDRVILVFD
     QVRSEKRYSP ASTFKIPHTL FALDAGAARD EFQVFRWDGI KRSFAAHNQD QDLRSAMRNS
     TVWIYELFAK EIGEDKARRY LKQIDYGNAD PSTSNGDYWI DGNLAIAAQE QIAFLRKLYH
     NELPFRVEHQ RLVKDLMIVE AGRNWILRAK TGWEGRIGWW VGWVEWPTGP VFFALNIDTP
     NRMDDLFKRE AIVRAILRSI EALPPNPAVN SDAAR
 
 
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