ID BLO1_KLEOX Reviewed; 291 AA. AC P22391; Q9S6S0; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=Beta-lactamase OXY-1; DE EC=3.5.2.6; DE AltName: Full=Penicillinase; DE Flags: Precursor; GN Name=bla; OS Klebsiella oxytoca. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=571; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=E23004; RX PubMed=2653216; DOI=10.1128/aac.33.1.63; RA Arakawa Y., Ohta M., Kido N., Mori M., Ito H., Komatsu T., Fujii Y., RA Kato N.; RT "Chromosomal beta-lactamase of Klebsiella oxytoca, a new class A enzyme RT that hydrolyzes broad-spectrum beta-lactam antibiotics."; RL Antimicrob. Agents Chemother. 33:63-70(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SL781, and SL7811; RX PubMed=8132152; DOI=10.1111/j.1574-6968.1994.tb06671.x; RA Fournier B., Arlet G., Lagrange P.H., Philippon A.; RT "Klebsiella oxytoca: resistance to aztreonam by overproduction of the RT chromosomally encoded beta-lactamase."; RL FEMS Microbiol. Lett. 116:31-36(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=KH66; RX PubMed=10223957; DOI=10.1128/aac.43.5.1294; RA Wu S.W., Dornbusch K., Kronvall G.; RT "Genetic characterization of resistance to extended-spectrum beta-lactams RT in Klebsiella oxytoca isolates recovered from patients with septicemia at RT hospitals in the Stockholm area."; RL Antimicrob. Agents Chemother. 43:1294-1297(1999). CC -!- FUNCTION: Hydrolyzes broad-spectrum beta-lactam antibiotics. Active CC against cephalosporins. 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:PRU10101}; CC -!- MISCELLANEOUS: In strain KH66 OXY-1 is known as OXY-1a. CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M27459; AAA25084.1; -; Genomic_DNA. DR EMBL; Z30177; CAA82916.1; -; Genomic_DNA. DR EMBL; Z30178; CAA82917.1; -; Genomic_DNA. DR EMBL; Y17715; CAB42615.1; -; Genomic_DNA. DR PIR; S42075; S42075. DR RefSeq; WP_014228247.1; NZ_CP026269.1. DR RefSeq; WP_063864546.1; NG_049845.1. DR PDB; 3BYD; X-ray; 1.93 A; A=25-291. DR PDBsum; 3BYD; -. DR AlphaFoldDB; P22391; -. DR SMR; P22391; -. DR STRING; 571.AB185_28800; -. DR KEGG; ag:AAA25084; -. DR KEGG; ag:CAB42615; -. DR eggNOG; COG2367; Bacteria. DR EvolutionaryTrace; P22391; -. DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC. DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR045155; Beta-lactam_cat. DR InterPro; IPR000871; Beta-lactam_class-A. DR InterPro; IPR023650; Beta-lactam_class-A_AS. DR PANTHER; PTHR35333; BETA-LACTAMASE; 1. DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF13354; Beta-lactamase2; 1. DR PRINTS; PR00118; BLACTAMASEA. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR PROSITE; PS00146; BETA_LACTAMASE_A; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Hydrolase; Signal. FT SIGNAL 1..24 FT CHAIN 25..291 FT /note="Beta-lactamase OXY-1" FT /id="PRO_0000016997" FT ACT_SITE 73 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10101" FT BINDING 237..239 FT /ligand="substrate" FT /evidence="ECO:0000250" FT VARIANT 262 FT /note="L -> P (in strain: KH66)" FT VARIANT 278 FT /note="E -> K (in strain: KH66)" FT HELIX 32..44 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:3BYD" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 76..89 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:3BYD" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 135..145 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 148..157 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 186..197 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 204..215 FT /evidence="ECO:0007829|PDB:3BYD" FT TURN 221..223 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 232..241 FT /evidence="ECO:0007829|PDB:3BYD" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 245..253 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:3BYD" FT STRAND 260..267 FT /evidence="ECO:0007829|PDB:3BYD" FT HELIX 277..288 FT /evidence="ECO:0007829|PDB:3BYD" SQ SEQUENCE 291 AA; 31044 MW; 9908F5AA97EDDC8A CRC64; MLKSSWRKTA LMAAAAVPLL LASGSLWASA DAIQQKLADL EKRSGGRLGV ALINTADDSQ TLYRGDERFA MCSTGKVMAA AAVLKQSESN PEVVNKRLEI KKSDLVVWSP ITEKHLQSGM TLAELSAAAL QYSDNTAMNK MISYLGGPEK VTAFAQSIGD VTFRLDRTEP ALNSAIPGDK RDTTTPLAMA ESLRKLTLGN ALGEQQRAQL VTWLKGNTTG GQSIRAGLPA SWAVGDKTGA GDYGTTNDIA VIWPENHAPL VLVTYFTQPQ QDAKSRKEVL AAAAKIVTEG L //