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Protein
Submitted name:

Arylamine N-acetyltransferase Nat

Gene

nat

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Coenzyme ACombined sources
Binding sitei97 – 971Coenzyme ACombined sources
Binding sitei132 – 1321Coenzyme A; via amide nitrogenCombined sources
Binding sitei152 – 1521Coenzyme ACombined sources
Binding sitei220 – 2201Coenzyme ACombined sources
Binding sitei229 – 2291Coenzyme ACombined sources

GO - Molecular functioni

  1. acetyltransferase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

TransferaseImported

Enzyme and pathway databases

BioCyciMMAR216594:GJOB-5097-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Arylamine N-acetyltransferase NatImported
Gene namesi
Name:natImported
Ordered Locus Names:MMAR_5055Imported
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)Imported
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000001190 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi216594.MMAR_5055.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VFBX-ray2.00A1-280[»]
2VFCX-ray2.70A/B1-280[»]
3LTWX-ray2.10A1-280[»]
4B55X-ray2.70A1-280[»]
4C5PX-ray1.59A1-280[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiB2HIZ6.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2162.
HOGENOMiHOG000205436.
KOiK00622.
OMAiHPVPFNG.
OrthoDBiEOG6D2KV2.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2HIZ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALDLTGYLD RINYRGATDP TLDVLRDLVS AHTGAIAFEN LDPLMGVPVD
60 70 80 90 100
DLSAEALADK LVDRRRGGYC YEHNGLIGYV LAELGYRVRR LAGRVVWLAP
110 120 130 140 150
PDAPTPAQTH TVLAVTFPGC QGPYLVDVGF GGMTPTAPLR LETGTVQQTA
160 170 180 190 200
LEPYRLDDRG DGLVLQAMVR DEWQALYEFS TLTRPQVDLR VGSWFVSTHP
210 220 230 240 250
TSHFVTGLMA ATVADDARWN LMGRNLAIHR RGGTEKILLE DAAAVVDTLG
260 270 280
DRFGINVADV GERGRLEARI DKVCFGAENR
Length:280
Mass (Da):30,635
Last modified:June 10, 2008 - v1
Checksum:i7A8CBC3B199A1B91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC43459.1.
RefSeqiYP_001853314.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC43459; ACC43459; MMAR_5055.
KEGGimmi:MMAR_5055.
PATRICi18071517. VBIMycMar75906_5415.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC43459.1.
RefSeqiYP_001853314.1. NC_010612.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VFBX-ray2.00A1-280[»]
2VFCX-ray2.70A/B1-280[»]
3LTWX-ray2.10A1-280[»]
4B55X-ray2.70A1-280[»]
4C5PX-ray1.59A1-280[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_5055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC43459; ACC43459; MMAR_5055.
KEGGimmi:MMAR_5055.
PATRICi18071517. VBIMycMar75906_5415.

Phylogenomic databases

eggNOGiCOG2162.
HOGENOMiHOG000205436.
KOiK00622.
OMAiHPVPFNG.
OrthoDBiEOG6D2KV2.

Enzyme and pathway databases

BioCyciMMAR216594:GJOB-5097-MONOMER.

Miscellaneous databases

EvolutionaryTraceiB2HIZ6.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-535 / MImported.
  2. "Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase."
    Fullam E., Westwood I.M., Anderton M.C., Lowe E.D., Sim E., Noble M.E.
    J. Mol. Biol. 375:178-191(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COENZYME A.
  3. "Probing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active site."
    Abuhammad A.M., Lowe E.D., Fullam E., Noble M., Garman E.F., Sim E.
    Protein Cell 1:384-392(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
  4. "Piperidinols that show anti-tubercular activity as inhibitors of arylamine N-acetyltransferase: an essential enzyme for mycobacterial survival inside macrophages."
    Abuhammad A., Fullam E., Lowe E.D., Staunton D., Kawamura A., Westwood I.M., Bhakta S., Garner A.C., Wilson D.L., Seden P.T., Davies S.G., Russell A.J., Garman E.F., Sim E.
    PLoS ONE 7:e52790-e52790(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
  5. "Arylamine N-Acetyltransferases from Mycobacteria: Investigations of a Potential Target for Anti- Tubercular Therapy."
    Abuhammad A.
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).

Entry informationi

Entry nameiB2HIZ6_MYCMM
AccessioniPrimary (citable) accession number: B2HIZ6
Entry historyi
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: April 29, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.