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Q9KVU4 (FMT_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:VC_0045
OrganismVibrio cholerae
Taxonomic identifier666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 315315Methionyl-tRNA formyltransferase HAMAP MF_00182
PRO_0000083080

Regions

Region113 – 1164Tetrahydrofolate (THF) binding By similarity

Secondary structure

1 ............................................... 315
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KVU4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D4244B566330CFB1

FASTA31534,200
        10         20         30         40         50         60 
MSQSLRIVFA GTPDFAARHL AALLSSEHEI IAVYTQPERP AGRGKKLTAS PVKTLALEHN 

        70         80         90        100        110        120 
VPVYQPENFK SDESKQQLAA LNADLMVVVA YGLLLPKVVL DTPKLGCINV HGSILPRWRG 

       130        140        150        160        170        180 
AAPIQRSIWA GDSETGVTIM QMDVGLDTGD MLKIATLPIE ASDTSASMYD KLAELGPQAL 

       190        200        210        220        230        240 
LECLQDIAQG TAVAVKQDDG LANYAHKLSK EEARINWSDA ATHIERCIRA FNPWPMSHFE 

       250        260        270        280        290        300 
VAENSIKVWQ ARVETRAVTQ TPGTIIQADK SGIYVATGQD VLVLESLQIP GKKALPVQDI 

       310 
LNARADWFSV GSQLS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003852 Genomic DNA. Translation: AAF93223.1.
PIRH82372.
RefSeqNP_229704.1. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q0IX-ray1.89A1-315[»]
ProteinModelPortalQ9KVU4.
SMRQ9KVU4. Positions 2-314.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2614441.
GenomeReviewsGene locus VC_0045 in contig AE003852_GR.
KEGGvch:VC0045.
PATRIC20079138. VBIVibCho83274_0044.
TIGRVC_0045.

Phylogenomic databases

HOGENOMHBG571560.
OMAIMQMDEG.
PhylomeDBQ9KVU4.
ProtClustDBPRK00005.

Family and domain databases

HAMAPMF_00182. Formyl_trans.
[Tree]
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
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.
KOK00604.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_VIBCH
AccessionPrimary (citable) accession number: Q9KVU4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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