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Protein

Chloramphenicol acetyltransferase

Gene

cat

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 sitei193 – 1931Proton acceptor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

BRENDAi2.3.1.28. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Chloramphenicol acetyltransferase (EC:2.3.1.28)
Short name:
CAT
Gene namesi
Name:cat
Encoded oniPlasmid JR66B1 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Biotechnological usei

This protein is used as a marker in many commonly used cloning vectors, such as pACYC184.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Chloramphenicol acetyltransferasePRO_0000165865Add
BLAST

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

MINTiMINT-1528209.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Helixi13 – 153Combined sources
Helixi19 – 257Combined sources
Turni26 – 294Combined sources
Beta strandi31 – 4010Combined sources
Helixi42 – 509Combined sources
Helixi55 – 6713Combined sources
Helixi71 – 733Combined sources
Beta strandi74 – 785Combined sources
Beta strandi81 – 866Combined sources
Beta strandi89 – 968Combined sources
Turni97 – 1004Combined sources
Beta strandi101 – 1066Combined sources
Helixi113 – 12715Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi140 – 1478Combined sources
Beta strandi154 – 1618Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi182 – 19211Combined sources
Turni193 – 1953Combined sources
Helixi198 – 21417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NOCX-ray2.60B1-219[»]
1PD5X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-219[»]
1Q23X-ray2.18A/B/C/D/E/F/G/H/I/J/K/L1-219[»]
3U9BX-ray3.20A/B/C/D/E/F/G/H/I1-219[»]
3U9FX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/R/S1-219[»]
ProteinModelPortaliP62577.
SMRiP62577. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62577.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK19271.

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.

P62577-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKITGYTT VDISQWHRKE HFEAFQSVAQ CTYNQTVQLD ITAFLKTVKK
60 70 80 90 100
NKHKFYPAFI HILARLMNAH PEFRMAMKDG ELVIWDSVHP CYTVFHEQTE
110 120 130 140 150
TFSSLWSEYH DDFRQFLHIY SQDVACYGEN LAYFPKGFIE NMFFVSANPW
160 170 180 190 200
VSFTSFDLNV ANMDNFFAPV FTMGKYYTQG DKVLMPLAIQ VHHAVCDGFH
210
VGRMLNELQQ YCDEWQGGA
Length:219
Mass (Da):25,663
Last modified:July 21, 1986 - v1
Checksum:i02C92576273FA18B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00623 Genomic DNA. Translation: CAA23900.1.
V00622 Genomic DNA. Translation: CAA23899.1.
PIRiA93220. XXECC1.
RefSeqiWP_000412211.1. NZ_LRWR01000030.1.
YP_001096419.1. NC_009133.1.
YP_001816591.1. NC_010558.1.
YP_008995272.1. NC_023277.2.
YP_008997430.1. NC_023289.2.
YP_009068571.1. NC_025141.1.
YP_009071093.1. NC_025179.1.
YP_009071408.1. NC_025181.1.
YP_025721.1. NC_005923.1.

Genome annotation databases

GeneIDi18157747.
18157952.
20491703.
20493165.
20495808.
23335835.
2847485.
4924744.
6276004.
KEGGiag:CAA23899.
pg:18157747.
pg:18157952.
pg:20491703.
pg:20493165.
pg:20495808.
pg:2847485.
pg:4924744.
pg:6276004.

Cross-referencesi

Web resourcesi

Wikipedia

Chloramphenicol acetyltransferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00623 Genomic DNA. Translation: CAA23900.1.
V00622 Genomic DNA. Translation: CAA23899.1.
PIRiA93220. XXECC1.
RefSeqiWP_000412211.1. NZ_LRWR01000030.1.
YP_001096419.1. NC_009133.1.
YP_001816591.1. NC_010558.1.
YP_008995272.1. NC_023277.2.
YP_008997430.1. NC_023289.2.
YP_009068571.1. NC_025141.1.
YP_009071093.1. NC_025179.1.
YP_009071408.1. NC_025181.1.
YP_025721.1. NC_005923.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NOCX-ray2.60B1-219[»]
1PD5X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-219[»]
1Q23X-ray2.18A/B/C/D/E/F/G/H/I/J/K/L1-219[»]
3U9BX-ray3.20A/B/C/D/E/F/G/H/I1-219[»]
3U9FX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/R/S1-219[»]
ProteinModelPortaliP62577.
SMRiP62577. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1528209.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18157747.
18157952.
20491703.
20493165.
20495808.
23335835.
2847485.
4924744.
6276004.
KEGGiag:CAA23899.
pg:18157747.
pg:18157952.
pg:20491703.
pg:20493165.
pg:20495808.
pg:2847485.
pg:4924744.
pg:6276004.

Phylogenomic databases

KOiK19271.

Enzyme and pathway databases

BRENDAi2.3.1.28. 2026.

Miscellaneous databases

EvolutionaryTraceiP62577.

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. "Primary structure of a chloramphenicol acetyltransferase specified by R plasmids."
    Shaw W.V., Packman L.C., Burleigh B.D., Dell A., Morris H.R., Hartley B.S.
    Nature 282:870-872(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Plasmid: JR66B
  2. "Nucleotide sequence analysis of the chloramphenicol resistance transposon Tn9."
    Alton N.K., Vapnek D.
    Nature 282:864-869(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Transposon: Tn9.
  3. "The DNA sequence of an IS/-flanked transposon coding for resistance to chloramphenicol and fusidic acid."
    Marcoli R., Iida S., Bickle T.A.
    FEBS Lett. 110:11-14(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Transposon: TnCAM204.
  4. "The structure of nitric oxide synthase oxygenase domain and inhibitor complexes."
    Crane B.R., Arvai A.S., Gachhui R., Wu C., Ghosh D.K., Getzoff E.D., Stuehr D.J., Tainer J.A.
    Science 278:425-431(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 5-217 IN COMPLEX WITH NOS2.

Entry informationi

Entry nameiCAT_ECOLX
AccessioniPrimary (citable) accession number: P62577
Secondary accession number(s): P00483
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Transposon Tncam204 is derived from the R plasmid NR1.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid, Transposable element

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.