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B0VAE0 (FMT_ACIBY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase

EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:ABAYE0022
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP By similarity. HAMAP-Rule MF_00182

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182

Sequence similarities

Belongs to the fmt family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslational initiation

Inferred from electronic annotation. Source: GOC

   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: HAMAP

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000098370

Regions

Region114 – 1174Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
B0VAE0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 4AC5C6E1E87B0BD8

FASTA32034,655
        10         20         30         40         50         60 
MKIIFAGTPE FAATALAALL KTSHEIIAVY TQPDRKAGRG QKLTPSPVKQ LALEHNIPVY 

        70         80         90        100        110        120 
QPLHFKASTE EGLAAQQELA ALGADVMVVA AYGLILPQAV LDTPKYGCLN IHGSLLPRWR 

       130        140        150        160        170        180 
GAAPIQRAIA TGDDETGITI MQMAAGLDTG DMMYKTYCPI TSEDTSATLH DKLAAQGATA 

       190        200        210        220        230        240 
ICAVLESEET LQKYLAEREV QDESLTVYAH KLVKSEARID WSMNAVQVDR NIRAFNPWPV 

       250        260        270        280        290        300 
AFIQLDENNA LRVWNSTISS QSKVNAQAGE IIAIDKQGVH VACGENTFIC LTSVQWPGGK 

       310        320 
ALNAQQIAQT QKLHVGQILP 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AYE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU459141 Genomic DNA. Translation: CAM85012.1.
RefSeqYP_001712019.1. NC_010410.1.

3D structure databases

ProteinModelPortalB0VAE0.
SMRB0VAE0. Positions 1-319.
ModBaseSearch...

Protein-protein interaction databases

STRING509173.ABAYE0022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM85012; CAM85012; ABAYE0022.
GeneID6003931.
KEGGaby:ABAYE0022.
PATRIC20723527. VBIAciBau69881_0125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.
ProtClustDBCLSK2307579.

Enzyme and pathway databases

BioCycABAU509173:GJXF-25-MONOMER.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPMF_00182. Formyl_trans.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
PROSITEPS00373. GART. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_ACIBY
AccessionPrimary (citable) accession number: B0VAE0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families