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B2HIZ6 (B2HIZ6_MYCMM) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Name:nat EMBL ACC43459.1
Ordered Locus Names:MMAR_5055 EMBL ACC43459.1
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] EMBL ACC43459.1
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region220 – 2256Azide 2 binding PDB 4C5P
Region252 – 2532Sulfate binding PDB 4C5P

Sites

Binding site341Sulfate; via carbonyl oxygen PDB 4C5P
Binding site701Coenzyme A PDB 2VFC
Binding site971Coenzyme A PDB 2VFC
Binding site1321Coenzyme A; via amide nitrogen PDB 2VFC
Binding site1521Coenzyme A PDB 2VFC
Binding site1881Azide 1; via carbonyl oxygen PDB 4C5P
Binding site2121Sulfate PDB 4C5P
Binding site2201Coenzyme A PDB 2VFC
Binding site2291Coenzyme A PDB 2VFC

Sequences

Sequence LengthMass (Da)Tools
B2HIZ6 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 7A8CBC3B199A1B91

FASTA28030,635
        10         20         30         40         50         60 
MALDLTGYLD RINYRGATDP TLDVLRDLVS AHTGAIAFEN LDPLMGVPVD DLSAEALADK 

        70         80         90        100        110        120 
LVDRRRGGYC YEHNGLIGYV LAELGYRVRR LAGRVVWLAP PDAPTPAQTH TVLAVTFPGC 

       130        140        150        160        170        180 
QGPYLVDVGF GGMTPTAPLR LETGTVQQTA LEPYRLDDRG DGLVLQAMVR DEWQALYEFS 

       190        200        210        220        230        240 
TLTRPQVDLR VGSWFVSTHP TSHFVTGLMA ATVADDARWN LMGRNLAIHR RGGTEKILLE 

       250        260        270        280 
DAAAVVDTLG DRFGINVADV GERGRLEARI DKVCFGAENR 

« Hide

References

« Hide 'large scale' references
[1]"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis."
Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. expand/collapse author list , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.
Genome Res. 18:729-741(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-535 / M.
[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) IN COMPLEX WITH AZIDE AND SULFATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000854 Genomic DNA. Translation: ACC43459.1.
RefSeqYP_001853314.1. NC_010612.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VFBX-ray2.00A1-280[»]
2VFCX-ray2.70A/B1-280[»]
3LTWX-ray2.10A1-280[»]
4B55X-ray2.70A1-280[»]
4C5PX-ray1.59A1-280[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216594.MMAR_5055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC43459; ACC43459; MMAR_5055.
GeneID6229346.
KEGGmmi:MMAR_5055.
PATRIC18071517. VBIMycMar75906_5415.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2162.
HOGENOMHOG000205436.
KOK00622.
OMAPATHTLM.
OrthoDBEOG6D2KV2.

Enzyme and pathway databases

BioCycMMAR216594:GJOB-5097-MONOMER.

Family and domain databases

InterProIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERPTHR11786. PTHR11786. 1 hit.
PfamPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceB2HIZ6.

Entry information

Entry nameB2HIZ6_MYCMM
AccessionPrimary (citable) accession number: B2HIZ6
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 11, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)