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