BLT1_ECOLX
ID BLT1_ECOLX Reviewed; 291 AA.
AC Q47066;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Beta-lactamase Toho-1;
DE EC=3.5.2.6;
DE Flags: Precursor;
GN Name=bla;
OS Escherichia coli.
OG Plasmid pMTY001.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TUH12191; PLASMID=pMTY001;
RX PubMed=8619581; DOI=10.1128/aac.39.10.2269;
RA Ishii Y., Ohno A., Taguchi H., Imajo S., Ishiguro M., Matsuzawa H.;
RT "Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A
RT beta-lactamase isolated from Escherichia coli.";
RL Antimicrob. Agents Chemother. 39:2269-2275(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-169.
RC STRAIN=TUH12191; PLASMID=pMTY001;
RX PubMed=9925786; DOI=10.1006/jmbi.1998.2432;
RA Ibuka A., Taguchi A., Ishiguro M., Fushinobu S., Ishii Y., Kamitori S.,
RA Okuyama K., Yamaguchi K., Konno M., Matsuzawa H.;
RT "Crystal structure of the E166A mutant of extended-spectrum beta-lactamase
RT Toho-1 at 1.8 A resolution.";
RL J. Mol. Biol. 285:2079-2087(1999).
CC -!- FUNCTION: Has strong cefotaxime-hydrolyzing activity.
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.
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; D37830; BAA07082.1; -; Genomic_DNA.
DR PIR; JP0074; JP0074.
DR RefSeq; WP_063860054.1; NG_048995.1.
DR PDB; 1BZA; X-ray; 1.80 A; A=30-290.
DR PDB; 1IYO; X-ray; 1.80 A; A=30-291.
DR PDB; 1IYP; X-ray; 2.00 A; A=30-291.
DR PDB; 1IYQ; X-ray; 2.10 A; A=30-291.
DR PDB; 1IYS; X-ray; 1.65 A; A=31-291.
DR PDB; 1WE4; X-ray; 1.70 A; A=30-291.
DR PDB; 2WYX; Neutron; 2.10 A; A=33-288.
DR PDB; 2XQZ; Neutron; 2.10 A; A=32-291.
DR PDB; 2XR0; X-ray; 2.20 A; A=32-291.
DR PDB; 2ZQ7; X-ray; 0.94 A; A=30-291.
DR PDB; 2ZQ8; X-ray; 1.03 A; A=30-291.
DR PDB; 2ZQ9; X-ray; 1.07 A; A=30-291.
DR PDB; 2ZQA; X-ray; 0.95 A; A=30-291.
DR PDB; 2ZQC; X-ray; 1.07 A; A=30-291.
DR PDB; 2ZQD; X-ray; 1.19 A; A=30-291.
DR PDB; 4BD0; X-ray; 1.21 A; A=31-291.
DR PDB; 4BD1; Neutron; 2.00 A; A=31-291.
DR PDB; 4C3Q; Neutron; 2.20 A; A=31-291.
DR PDB; 4X69; X-ray; 1.42 A; A/B=30-291.
DR PDB; 5KMW; X-ray; 1.10 A; A=33-288.
DR PDB; 5KSC; Neutron; 2.10 A; A=31-291.
DR PDB; 6C78; Neutron; 1.75 A; A=32-291.
DR PDB; 6C79; X-ray; 1.10 A; A=32-291.
DR PDB; 6C7A; X-ray; 1.05 A; A=32-291.
DR PDB; 6U58; Other; 1.90 A; A=31-291.
DR PDBsum; 1BZA; -.
DR PDBsum; 1IYO; -.
DR PDBsum; 1IYP; -.
DR PDBsum; 1IYQ; -.
DR PDBsum; 1IYS; -.
DR PDBsum; 1WE4; -.
DR PDBsum; 2WYX; -.
DR PDBsum; 2XQZ; -.
DR PDBsum; 2XR0; -.
DR PDBsum; 2ZQ7; -.
DR PDBsum; 2ZQ8; -.
DR PDBsum; 2ZQ9; -.
DR PDBsum; 2ZQA; -.
DR PDBsum; 2ZQC; -.
DR PDBsum; 2ZQD; -.
DR PDBsum; 4BD0; -.
DR PDBsum; 4BD1; -.
DR PDBsum; 4C3Q; -.
DR PDBsum; 4X69; -.
DR PDBsum; 5KMW; -.
DR PDBsum; 5KSC; -.
DR PDBsum; 6C78; -.
DR PDBsum; 6C79; -.
DR PDBsum; 6C7A; -.
DR PDBsum; 6U58; -.
DR AlphaFoldDB; Q47066; -.
DR SMR; Q47066; -.
DR ChEMBL; CHEMBL1697675; -.
DR DrugBank; DB08375; (2R)-2-[(1R)-1-[[(2Z)-2-(2-Amino-1,3-thiazol-4-yl)-2-methoxyiminoacetyl]amino]-2-oxoethyl]-5-methylidene-2H-1,3-thiazine-4-carboxylic acid.
DR DrugBank; DB03450; Cephalothin Group.
DR KEGG; ag:BAA07082; -.
DR BRENDA; 3.5.2.6; 2026.
DR SABIO-RK; Q47066; -.
DR EvolutionaryTrace; Q47066; -.
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; -; 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; PTHR35333; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Hydrolase; Plasmid; Signal.
FT SIGNAL 1..29
FT CHAIN 30..291
FT /note="Beta-lactamase Toho-1"
FT /id="PRO_0000016994"
FT ACT_SITE 73
FT /note="Acyl-ester intermediate"
FT BINDING 237..239
FT /ligand="substrate"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5KMW"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2ZQ8"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:2ZQ7"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:2ZQ7"
SQ SEQUENCE 291 AA; 31447 MW; 83FC0CD9CD41E7C0 CRC64;
MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV ALINTADNSQ
ILYRADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI KKSDLVNYNP IAEKHVNGTM
TLAELGAAAL QYSDNTAMNK LIAHLGGPDK VTAFARSLGD ETFRLDRTEP TLNTAIPGDP
RDTTTPLAMA QTLKNLTLGK ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWVVGDKTGS
GDYGTTNDIA VIWPENHAPL VLVTYFTQPE QKAERRRDIL AAAAKIVTHG F
