Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei73Acyl-ester intermediate1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1697675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000001699430 – 291Beta-lactamase Toho-1Add BLAST262

Proteomic databases

PRIDEiQ47066.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 43Combined sources11
Beta strandi46 – 54Combined sources9
Turni55 – 57Combined sources3
Beta strandi60 – 64Combined sources5
Helixi72 – 75Combined sources4
Helixi76 – 87Combined sources12
Helixi93 – 95Combined sources3
Beta strandi97 – 99Combined sources3
Helixi102 – 104Combined sources3
Helixi112 – 115Combined sources4
Beta strandi118 – 121Combined sources4
Helixi122 – 131Combined sources10
Helixi135 – 145Combined sources11
Helixi148 – 157Combined sources10
Helixi171 – 173Combined sources3
Helixi186 – 198Combined sources13
Beta strandi199 – 202Combined sources4
Helixi204 – 215Combined sources12
Turni221 – 223Combined sources3
Helixi224 – 227Combined sources4
Beta strandi232 – 241Combined sources10
Turni242 – 244Combined sources3
Beta strandi245 – 253Combined sources9
Beta strandi255 – 257Combined sources3
Beta strandi260 – 267Combined sources8
Helixi277 – 288Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X69X-ray1.42A/B30-291[»]
ProteinModelPortaliQ47066.
SMRiQ47066.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47066.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni237 – 239Substrate binding3

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

KOiK18767.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A.
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.
RefSeqiWP_063860054.1. NG_048995.1.

Genome annotation databases

KEGGiag:BAA07082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37830 Genomic DNA. Translation: BAA07082.1.
PIRiJP0074.
RefSeqiWP_063860054.1. NG_048995.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X69X-ray1.42A/B30-291[»]
ProteinModelPortaliQ47066.
SMRiQ47066.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL1697675.

Proteomic databases

PRIDEiQ47066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA07082.

Phylogenomic databases

KOiK18767.

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.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 88 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

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 one 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.