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Q9K1K6 (FMT_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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:NMB0111
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length308 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 – 308308Methionyl-tRNA formyltransferase HAMAP MF_00182
PRO_0000083004

Regions

Region110 – 1134Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K1K6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: FB4E816824BE0511

FASTA30832,901
        10         20         30         40         50         60 
MKVIFAGTPD FAAAALRAVA AAGFEIPLVL TQPDRPKGRG MQLTAPPVKQ AALELGLRVE 

        70         80         90        100        110        120 
QPEKLRNNAE ALQMLKEVEA DVMVVAAYGL ILPQEVLDTP KHGCLNIHAS LLPRWRGAAP 

       130        140        150        160        170        180 
IQRAIEAGDA ETGVCIMQMD IGLDTGDVVS EHRYAIQPTD TANEVHDALM EIGAAAVVAD 

       190        200        210        220        230        240 
LQQLQSKGRL NAVKQPEEGV TYAQKLSKEE ARIDWSKSAA VIERKIRAFN PVPAAWVEYQ 

       250        260        270        280        290        300 
GKPMKIRRAE VVAQQGAAGE VLSCSADGLV VACGENALKI TELQPAGGRR MNIAAFAAGR 


HIEAGAKL 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF40570.1.
PIRF81238.
RefSeqNP_273169.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ9K1K6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000010492; EBNEIP00000010112; EBNEIG00000010492.
GeneID902215.
GenomeReviewsGene locus NMB0111 in contig AE002098_GR.
KEGGnme:NMB0111.
NMPDRfig|122586.1.peg.103.
PATRIC20355235. VBINeiMen85645_0151.
TIGRNMB0111.

Phylogenomic databases

GeneTreeEBGT00050000021252.
HOGENOMHBG571560.
OMAIMQMDEG.
ProtClustDBCLSK877398.

Enzyme and pathway databases

BioCycNMEN122586:NMB_0111-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.
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_NEIMB
AccessionPrimary (citable) accession number: Q9K1K6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 67 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