ID BLAB_PROVU Reviewed; 300 AA. AC P52664; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 101. DE RecName: Full=Beta-lactamase; DE EC=3.5.2.6; DE AltName: Full=Cefuroximase; DE Flags: Precursor; GN Name=blaB; Synonyms=cumA; OS Proteus vulgaris. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Morganellaceae; Proteus. OX NCBI_TaxID=585; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B317; RX PubMed=7957242; DOI=10.1111/j.1432-1033.1994.tb20036.x; RA Datz M., Joris B., Azab E.A., Galleni M., van Beeumen J., Frere J.-M., RA Martin H.H.; RT "A common system controls the induction of very different genes. The class- RT A beta-lactamase of Proteus vulgaris and the enterobacterial class-C beta- RT lactamase."; RL Eur. J. Biochem. 226:149-157(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=5E78-1; RA Okuguchi M., Komai T., Makajima N., Eguchi H., Kuboki A., Ito T., RA Meguro M., Nakata T., Sugimoto K.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP AMINO ACID NUMBERING SCHEME. RX PubMed=2039479; DOI=10.1042/bj2760269; RA Ambler R.P., Coulson A.F., Frere J.M., Ghuysen J.M., Joris B., Forsman M., RA Levesque R.C., Tiraby G., Waley S.G.; RT "A standard numbering scheme for the class A beta-lactamases."; RL Biochem. J. 276:269-270(1991). CC -!- FUNCTION: Hydrolyzes broad-spectrum beta-lactam antibiotics. Active CC against cephalosporins such as cefuroxime and cefotaxime. 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 -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- MISCELLANEOUS: The class A beta-lactamase family has a specific amino- CC acid numbering system, sometimes called Ambler or ABL numbering and CC often misspelt as Amber. A multiple sequence alignment was used to CC derive a consensus sequence and then the consensus was numbered taking CC into account insertions and deletions. This allows use of identical CC numbers, e.g. for active site residues, despite differences in protein CC length. UniProt always uses natural numbering of residues, hence there CC appear to be differences in numbering between this entry and some CC papers. {ECO:0000305|PubMed:2039479}. 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; X80128; CAA56427.1; -; Genomic_DNA. DR EMBL; D37831; BAA07084.1; -; Genomic_DNA. DR PIR; S51044; S51044. DR PDB; 1HZO; X-ray; 1.75 A; A/B=30-300. DR SMR; P52664; -. DR STRING; 585.DR95_683; -. DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid. DR DrugBank; DB01598; Imipenem. DR EvolutionaryTrace; P52664; -. 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-LACTAMASE-TYPE TRANSPEPTIDASE FOLD CONTAINING PROTEIN; 1. DR Pfam; PF13354; Beta-lactamase2; 1. DR PRINTS; PR00118; BLACTAMASEA. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR NCBIfam; NF033103; bla_class_A; 1. DR PROSITE; PS00146; BETA_LACTAMASE_A; 1. 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:InterPro. DR AlphaFoldDB; P52664; -. DR MDposit; P52664; -. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Hydrolase; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..300 FT /note="Beta-lactamase" FT /id="PRO_0000017008" FT ACT_SITE 75 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10101" FT BINDING 239..241 FT /ligand="substrate" FT /evidence="ECO:0000250" FT VARIANT 13 FT /note="T -> A (in strain: 5E78-1)" FT VARIANT 23 FT /note="V -> A (in strain: 5E78-1)" FT VARIANT 30..31 FT /note="NT -> DN (in strain: 5E78-1)" FT VARIANT 40 FT /note="S -> N (in strain: 5E78-1)" FT VARIANT 58 FT /note="E -> K (in strain: 5E78-1)" FT VARIANT 88 FT /note="E -> A (in strain: 5E78-1)" FT VARIANT 119 FT /note="V -> T (in strain: 5E78-1)" FT VARIANT 123 FT /note="S -> T (in strain: 5E78-1)" FT VARIANT 126 FT /note="Q -> E (in strain: 5E78-1)" FT VARIANT 224 FT /note="H -> N (in strain: 5E78-1)" FT VARIANT 235 FT /note="I -> V (in strain: 5E78-1)" FT VARIANT 257 FT /note="K -> E (in strain: 5E78-1)" FT VARIANT 283 FT /note="V -> A (in strain: 5E78-1)" FT VARIANT 286 FT /note="T -> A (in strain: 5E78-1)" FT HELIX 34..46 FT /evidence="ECO:0007829|PDB:1HZO" FT STRAND 48..56 FT /evidence="ECO:0007829|PDB:1HZO" FT TURN 57..60 FT /evidence="ECO:0007829|PDB:1HZO" FT STRAND 61..66 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 78..91 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:1HZO" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 124..133 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 137..147 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 150..159 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 188..199 FT /evidence="ECO:0007829|PDB:1HZO" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 206..217 FT /evidence="ECO:0007829|PDB:1HZO" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:1HZO" FT STRAND 234..243 FT /evidence="ECO:0007829|PDB:1HZO" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:1HZO" FT STRAND 247..255 FT /evidence="ECO:0007829|PDB:1HZO" FT STRAND 262..269 FT /evidence="ECO:0007829|PDB:1HZO" FT HELIX 279..294 FT /evidence="ECO:0007829|PDB:1HZO" SQ SEQUENCE 300 AA; 32992 MW; 2719AF2464F1CD77 CRC64; MTMFKTTFRQ TATIAVSLIS LLVSPMLWAN TNNTIEEQLS TLEKYSQGRL GVALINTEDN SQITYRGEER FAMASTSKVM AVAAVLKESE KQAGLLDKNI TIKKSDLVAY SPITEKHLVT GMSLAQLSAA TLQYSDNTAM NKILDYLGGP AKVTQFARSI NDVTYRLDRK EPELNTAIHG DPRDTTSPIA MAKSLQALTL GDALGQSQRQ QLVTWLKGNT TGDHSIKAGL PKHWIVGDKT GSGDYGTTND IAVIWPKNHA PLILVVYFTQ QEQDAKYRKD IIVKATEIVT KEISNSPQTK //