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Protein

Chloramphenicol acetyltransferase 3

Gene

cat3

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme is an effector of chloramphenicol resistance in bacteria.

Catalytic activityi

Acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Proton acceptor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance

Names & Taxonomyi

Protein namesi
Recommended name:
Chloramphenicol acetyltransferase 3 (EC:2.3.1.28)
Alternative name(s):
Chloramphenicol acetyltransferase III
Short name:
CAT-III
Gene namesi
Name:cat3
Encoded oniPlasmid IncK R3870 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Chemistry

DrugBankiDB00446. Chloramphenicol.
DB02703. Fusidic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Chloramphenicol acetyltransferase 3PRO_0000165877Add
BLAST

Proteomic databases

PRIDEiP00484.

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi8 – 103Combined sources
Helixi14 – 229Combined sources
Beta strandi27 – 359Combined sources
Helixi37 – 448Combined sources
Helixi50 – 6213Combined sources
Helixi66 – 683Combined sources
Beta strandi69 – 735Combined sources
Beta strandi76 – 816Combined sources
Beta strandi84 – 918Combined sources
Turni92 – 954Combined sources
Beta strandi96 – 1016Combined sources
Helixi108 – 12215Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi136 – 1449Combined sources
Beta strandi166 – 1705Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi178 – 18811Combined sources
Turni189 – 1913Combined sources
Helixi194 – 20815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIAX-ray2.50A1-213[»]
1CLAX-ray2.34A1-213[»]
1QCAX-ray2.20A1-213[»]
2CLAX-ray2.35A1-213[»]
3CLAX-ray1.75A1-213[»]
4CLAX-ray2.00A1-213[»]
ProteinModelPortaliP00484.
SMRiP00484. Positions 1-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00484.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR023213. CAT-like_dom.
IPR018372. Chloramphenicol_AcTrfase_AS.
IPR001707. Cmp_AcTrfase.
[Graphical view]
PfamiPF00302. CAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000440. CAT. 1 hit.
ProDomiPD002660. Cmp_AcTrfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01059. CAT. 1 hit.
[Graphical view]
PROSITEiPS00100. CAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00484-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYTKFDVKN WVRREHFEFY RHRLPCGFSL TSKIDITTLK KSLDDSAYKF
60 70 80 90 100
YPVMIYLIAQ AVNQFDELRM AIKDDELIVW DSVDPQFTVF HQETETFSAL
110 120 130 140 150
SCPYSSDIDQ FMVNYLSVME RYKSDTKLFP QGVTPENHLN ISALPWVNFD
160 170 180 190 200
SFNLNVANFT DYFAPIITMA KYQQEGDRLL LPLSVQVHHA VCDGFHVARF
210
INRLQELCNS KLK
Length:213
Mass (Da):24,994
Last modified:August 1, 1988 - v1
Checksum:i4A96839AB590CB1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07848 Genomic DNA. Translation: CAA30695.1.
PIRiA00567. XXECC3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07848 Genomic DNA. Translation: CAA30695.1.
PIRiA00567. XXECC3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIAX-ray2.50A1-213[»]
1CLAX-ray2.34A1-213[»]
1QCAX-ray2.20A1-213[»]
2CLAX-ray2.35A1-213[»]
3CLAX-ray1.75A1-213[»]
4CLAX-ray2.00A1-213[»]
ProteinModelPortaliP00484.
SMRiP00484. Positions 1-213.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB00446. Chloramphenicol.
DB02703. Fusidic Acid.

Proteomic databases

PRIDEiP00484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00484.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR023213. CAT-like_dom.
IPR018372. Chloramphenicol_AcTrfase_AS.
IPR001707. Cmp_AcTrfase.
[Graphical view]
PfamiPF00302. CAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000440. CAT. 1 hit.
ProDomiPD002660. Cmp_AcTrfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01059. CAT. 1 hit.
[Graphical view]
PROSITEiPS00100. CAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence analysis and overexpression of the gene encoding a type III chloramphenicol acetyltransferase."
    Murray I.A., Hawkins A.R., Keyte J.W., Shaw W.V.
    Biochem. J. 252:173-179(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Structure of chloramphenicol acetyltransferase at 1.75-A resolution."
    Leslie A.G.W., Moody P.C.E., Shaw W.V.
    Proc. Natl. Acad. Sci. U.S.A. 85:4133-4137(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
  3. "Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75-A resolution."
    Leslie A.G.W.
    J. Mol. Biol. 213:167-186(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

Entry informationi

Entry nameiCAT3_ECOLX
AccessioniPrimary (citable) accession number: P00484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: November 26, 2014
This is version 94 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, Direct protein sequencing, 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.