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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

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.
OMAiGCINSHA.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

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_CCYB01000066.1.

Genome annotation databases

EnsemblBacteriaiAAO91486; AAO91486; CBU_1997.
GeneIDi1209910.
KEGGicbu:CBU_1997.
PATRICi17932735. VBICoxBur82552_1984.

Cross-referencesi

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_CCYB01000066.1.

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...

Protein-protein interaction databases

STRINGi227377.CBU_1997.

Proteomic databases

PRIDEiQ83AA8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO91486; AAO91486; CBU_1997.
GeneIDi1209910.
KEGGicbu:CBU_1997.
PATRICi17932735. VBICoxBur82552_1984.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_COXBU
AccessioniPrimary (citable) accession number: Q83AA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.