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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.UniRule annotation

Catalytic activityi

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).UniRule annotation

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Biological processProtein biosynthesis

Enzyme and pathway databases

BioCyciCBUR227377:G1G0B-1968-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:CBU_1997
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000829551 – 314Methionyl-tRNA formyltransferaseAdd BLAST314

Proteomic databases

PRIDEiQ83AA8

Interactioni

Protein-protein interaction databases

STRINGi227377.CBU_1997

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 14Combined sources3
Helixi15 – 23Combined sources9
Beta strandi24 – 32Combined sources9
Helixi49 – 56Combined sources8
Beta strandi67 – 69Combined sources3
Helixi70 – 77Combined sources8
Beta strandi82 – 88Combined sources7
Helixi95 – 98Combined sources4
Beta strandi105 – 111Combined sources7
Turni113 – 116Combined sources4
Beta strandi117 – 119Combined sources3
Helixi121 – 128Combined sources8
Beta strandi131 – 139Combined sources9
Beta strandi142 – 145Combined sources4
Beta strandi149 – 156Combined sources8
Helixi163 – 187Combined sources25
Helixi197 – 199Combined sources3
Helixi208 – 211Combined sources4
Helixi219 – 228Combined sources10
Turni229 – 233Combined sources5
Beta strandi236 – 239Combined sources4
Beta strandi242 – 252Combined sources11
Beta strandi263 – 267Combined sources5
Beta strandi270 – 274Combined sources5
Beta strandi276 – 286Combined sources11
Helixi295 – 302Combined sources8
Helixi303 – 305Combined sources3
Turni308 – 310Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TQQX-ray2.00A1-314[»]
ProteinModelPortaliQ83AA8
SMRiQ83AA8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 114Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE Bacteria
COG0223 LUCA
HOGENOMiHOG000261177
KOiK00604
OMAiLRIVFMG

Family and domain databases

Gene3Di3.10.25.10, 1 hit
HAMAPiMF_00182 Formyl_trans, 1 hit
InterProiView protein in InterPro
IPR005794 Fmt
IPR005793 Formyl_trans_C
IPR037022 Formyl_trans_C_sf
IPR002376 Formyl_transf_N
IPR036477 Formyl_transf_N_sf
IPR011034 Formyl_transferase-like_C_sf
IPR001555 GART_AS
PfamiView protein in Pfam
PF02911 Formyl_trans_C, 1 hit
PF00551 Formyl_trans_N, 1 hit
SUPFAMiSSF50486 SSF50486, 1 hit
SSF53328 SSF53328, 1 hit
TIGRFAMsiTIGR00460 fmt, 1 hit
PROSITEiView protein in PROSITE
PS00373 GART, 1 hit

Sequencei

Sequence statusi: Complete.

Q83AA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKIVFAGT PQFAVPTLRA LIDSSHRVLA VYTQPDRPSG RGQKIMESPV
60 70 80 90 100
KEIARQNEIP IIQPFSLRDE VEQEKLIAMN ADVMVVVAYG LILPKKALNA
110 120 130 140 150
FRLGCVNVHA SLLPRWRGAA PIQRAILAGD RETGISIMQM NEGLDTGDVL
160 170 180 190 200
AKSACVISSE DTAADLHDRL SLIGADLLLE SLAKLEKGDI KLEKQDEASA
210 220 230 240 250
TYASKIQKQE ALIDWRKSAV EIARQVRAFN PTPIAFTYFE GQPMRIWRAT
260 270 280 290 300
VVDEKTDFEP GVLVDADKKG ISIAAGSGIL RLHQLQLPGK RVCSAGDFIN
310
AHGDKLIPGK TVFG
Length:314
Mass (Da):34,288
Last modified:June 1, 2003 - v1
Checksum:i11A4B3CCB9ED0AD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA Translation: AAO91486.1
RefSeqiNP_820972.1, NC_002971.3
WP_010958586.1, NZ_LM994641.1

Genome annotation databases

EnsemblBacteriaiAAO91486; AAO91486; CBU_1997
GeneIDi1209910
31484676
KEGGicbu:CBU_1997
PATRICifig|227377.7.peg.1984

Similar proteinsi

Entry informationi

Entry nameiFMT_COXBU
AccessioniPrimary (citable) accession number: Q83AA8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: June 1, 2003
Last modified: March 28, 2018
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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