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Q9ABE9 (FMT_CAUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. 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:CC_0279
OrganismCaulobacter crescentus (strain ATCC 19089 / CB15) [Reference proteome] [HAMAP]
Taxonomic identifier190650 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

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-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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_0000082941

Regions

Region109 – 1124Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ABE9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E3818F37280D7FF3

FASTA30832,531
        10         20         30         40         50         60 
MRIAFLGTPD FAVTCLAELV ASGHEIVCVY SQPPAPRGRG QDLKPSPVHA FAEGLGLPVR 

        70         80         90        100        110        120 
TPVSMKTPEE IAAFQALDLD AAVVVAFGQI LVKDVLEAPK HGCFNLHASL LPRWRGAAPI 

       130        140        150        160        170        180 
QRAIMAGDAV TGVQVMRMSE GLDEGPILMS QQVAIADDDT AASLHDKLAA VGARLLPVAL 

       190        200        210        220        230        240 
AAIEREVVQE TPQAEDGVTY AKKIKSAEAR IDWTRPAAEI DRHIRGLSPF PGAWFEAPSE 

       250        260        270        280        290        300 
KGPVRVKALL SRVEAASGVA GTTLDDALLI ACGEGSIRLL KAQREGKGVQ DAQTFTRGFP 


IATGTVLA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005673 Genomic DNA. Translation: AAK22266.1.
PIRF87283.
RefSeqNP_419098.1. NC_002696.2.

3D structure databases

ProteinModelPortalQ9ABE9.
SMRQ9ABE9. Positions 1-293.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK22266; AAK22266; CC_0279.
GeneID942377.
KEGGccr:CC_0279.
PATRIC21297478. VBICauCre124313_0277.

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.
ProtClustDBCLSK889816.

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_CAUCR
AccessionPrimary (citable) accession number: Q9ABE9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 73 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