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O51091 (FMT_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. 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:BB_0064
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length312 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 MF_00182

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) + H2O = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP MF_00182

Sequence similarities

Belongs to the fmt family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Methionyl-tRNA formyltransferase HAMAP MF_00182
PRO_0000082925

Regions

Region107 – 1104Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
O51091 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 084FBF42F727ACBB

FASTA31235,107
        10         20         30         40         50         60 
MKIFFVSSSS IALEVFKEIV KHYEVVGVLT LPDRPKGRGQ KLSQNVIKSE AIARNIKVLD 

        70         80         90        100        110        120 
PLILDDNVLN LVRDLNPDLM LVFSYGKIFK KEFLDLFPKG CINVHPSLLP KYRGVSPIQS 

       130        140        150        160        170        180 
AILNGDCVSG VTIQSMALEM DSGNILVQKN FKIRSYDTSH DISKLVSSLS PSLVLEALEK 

       190        200        210        220        230        240 
ISKGFLGIPQ KSSEATFCSF LKKESGFIDF NLSAFEIKNK INACNPWPLV RVRLDYNDII 

       250        260        270        280        290        300 
FHRADFLEVD LYKERKIGEI VDFNPEKGLF VNTGKGILLL LEVQRPGRKV LDFKSFYNGS 

       310 
RQLIGQVFSS IE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000783 Genomic DNA. Translation: AAC66446.1.
PIRH70107.
RefSeqNP_212198.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51091.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000008950; EBBORP00000008280; EBBORG00000008949.
GeneID1194900.
GenomeReviewsGene locus BB_0064 in contig AE000783_GR.
KEGGbbu:BB0064.
NMPDRfig|224326.1.peg.448.
PATRIC20556733. VBIBorBur75917_0462.
TIGRBB_0064.

Phylogenomic databases

GeneTreeEBGT00050000007279.
HOGENOMHBG571560.
OMAVENEKSH.
ProtClustDBCLSK507328.

Enzyme and pathway databases

BioCycBBUR224326:BB_0064-MONOMER.

Family and domain databases

HAMAPMF_00182. Formyl_trans.
[Tree]
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
Gene3DG3DSA:3.10.25.10. Formyl_trans_C. 1 hit.
G3DSA:3.40.50.170. Formyl_transf_N. 1 hit.
PANTHERPTHR11138. Met_tRNA_Form_TA-like. 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_BORBU
AccessionPrimary (citable) accession number: O51091
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 80 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

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