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Protein

Beta-lactamase Toho-1

Gene

bla

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has strong cefotaxime-hydrolyzing activity.

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Acyl-ester intermediate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

BRENDAi3.5.2.6. 2026.
SABIO-RKQ47066.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase Toho-1 (EC:3.5.2.6)
Gene namesi
Name:bla
Encoded oniPlasmid pMTY0012 Publications
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 291262Beta-lactamase Toho-1PRO_0000016994Add
BLAST

Proteomic databases

PRIDEiQ47066.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4311Combined sources
Beta strandi46 – 549Combined sources
Turni55 – 573Combined sources
Beta strandi60 – 645Combined sources
Helixi72 – 754Combined sources
Helixi76 – 8712Combined sources
Helixi93 – 953Combined sources
Beta strandi97 – 993Combined sources
Helixi102 – 1043Combined sources
Helixi112 – 1154Combined sources
Beta strandi118 – 1214Combined sources
Helixi122 – 13110Combined sources
Helixi135 – 14511Combined sources
Helixi148 – 15710Combined sources
Helixi171 – 1733Combined sources
Helixi186 – 19813Combined sources
Beta strandi199 – 2024Combined sources
Helixi204 – 21512Combined sources
Turni221 – 2233Combined sources
Helixi224 – 2274Combined sources
Beta strandi232 – 24110Combined sources
Turni242 – 2443Combined sources
Beta strandi245 – 2539Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi260 – 2678Combined sources
Helixi277 – 28812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZAX-ray1.80A30-290[»]
1IYOX-ray1.80A30-291[»]
1IYPX-ray2.00A30-291[»]
1IYQX-ray2.10A30-291[»]
1IYSX-ray1.65A31-291[»]
1WE4X-ray1.70A30-291[»]
2WYXneutron diffraction2.10A33-288[»]
2XQZneutron diffraction2.10A32-291[»]
2XR0X-ray2.20A32-291[»]
2ZQ7X-ray0.94A30-291[»]
2ZQ8X-ray1.03A30-291[»]
2ZQ9X-ray1.07A30-291[»]
2ZQAX-ray0.95A30-291[»]
2ZQCX-ray1.07A30-291[»]
2ZQDX-ray1.19A30-291[»]
4BD0X-ray1.21A31-291[»]
4BD1neutron diffraction2.00A31-291[»]
4C3Qneutron diffraction2.20A31-291[»]
ProteinModelPortaliQ47066.
SMRiQ47066. Positions 31-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47066.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni237 – 2393Substrate binding

Sequence similaritiesi

Belongs to the class-A beta-lactamase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q47066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV
60 70 80 90 100
ALINTADNSQ ILYRADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI
110 120 130 140 150
KKSDLVNYNP IAEKHVNGTM TLAELGAAAL QYSDNTAMNK LIAHLGGPDK
160 170 180 190 200
VTAFARSLGD ETFRLDRTEP TLNTAIPGDP RDTTTPLAMA QTLKNLTLGK
210 220 230 240 250
ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWVVGDKTGS GDYGTTNDIA
260 270 280 290
VIWPENHAPL VLVTYFTQPE QKAERRRDIL AAAAKIVTHG F
Length:291
Mass (Da):31,447
Last modified:November 1, 1996 - v1
Checksum:i83FC0CD9CD41E7C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37830 Genomic DNA. Translation: BAA07082.1.
PIRiJP0074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37830 Genomic DNA. Translation: BAA07082.1.
PIRiJP0074.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZAX-ray1.80A30-290[»]
1IYOX-ray1.80A30-291[»]
1IYPX-ray2.00A30-291[»]
1IYQX-ray2.10A30-291[»]
1IYSX-ray1.65A31-291[»]
1WE4X-ray1.70A30-291[»]
2WYXneutron diffraction2.10A33-288[»]
2XQZneutron diffraction2.10A32-291[»]
2XR0X-ray2.20A32-291[»]
2ZQ7X-ray0.94A30-291[»]
2ZQ8X-ray1.03A30-291[»]
2ZQ9X-ray1.07A30-291[»]
2ZQAX-ray0.95A30-291[»]
2ZQCX-ray1.07A30-291[»]
2ZQDX-ray1.19A30-291[»]
4BD0X-ray1.21A31-291[»]
4BD1neutron diffraction2.00A31-291[»]
4C3Qneutron diffraction2.20A31-291[»]
ProteinModelPortaliQ47066.
SMRiQ47066. Positions 31-291.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL1697675.

Proteomic databases

PRIDEiQ47066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.2.6. 2026.
SABIO-RKQ47066.

Miscellaneous databases

EvolutionaryTraceiQ47066.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli."
    Ishii Y., Ohno A., Taguchi H., Imajo S., Ishiguro M., Matsuzawa H.
    Antimicrob. Agents Chemother. 39:2269-2275(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: TUH12191.
    Plasmid: pMTY001
  2. "Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution."
    Ibuka A., Taguchi A., Ishiguro M., Fushinobu S., Ishii Y., Kamitori S., Okuyama K., Yamaguchi K., Konno M., Matsuzawa H.
    J. Mol. Biol. 285:2079-2087(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-169.
    Strain: TUH12191.
    Plasmid: pMTY001

Entry informationi

Entry nameiBLT1_ECOLX
AccessioniPrimary (citable) accession number: Q47066
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.