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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Bacillus anthracis
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

Enzyme and pathway databases

BioCyciANTHRA:FMT-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:BA_4004, GBAA_4004, BAS3717
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000829101 – 314Methionyl-tRNA formyltransferaseAdd BLAST314

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_4004.

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi13 – 22Combined sources10
Beta strandi26 – 31Combined sources6
Turni39 – 42Combined sources4
Helixi48 – 55Combined sources8
Helixi69 – 78Combined sources10
Beta strandi81 – 87Combined sources7
Helixi94 – 97Combined sources4
Beta strandi104 – 110Combined sources7
Beta strandi114 – 118Combined sources5
Helixi120 – 126Combined sources7
Beta strandi130 – 138Combined sources9
Beta strandi148 – 155Combined sources8
Helixi162 – 185Combined sources24
Helixi196 – 198Combined sources3
Helixi207 – 210Combined sources4
Helixi218 – 226Combined sources9
Turni227 – 232Combined sources6
Beta strandi234 – 238Combined sources5
Beta strandi241 – 252Combined sources12
Beta strandi261 – 265Combined sources5
Beta strandi270 – 272Combined sources3
Beta strandi275 – 287Combined sources13
Helixi295 – 301Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IQFX-ray2.40A/B/C/D1-314[»]
ProteinModelPortaliQ81WH2.
SMRiQ81WH2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 113Tetrahydrofolate (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.

Q81WH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKVVFMGTP DFSVPVLRRL IEDGYDVIGV VTQPDRPVGR KKVLTPTPVK
60 70 80 90 100
VEAEKHGIPV LQPLRIREKD EYEKVLALEP DLIVTAAFGQ IVPNEILEAP
110 120 130 140 150
KYGCINVHAS LLPELRGGAP IHYAIMEGKE KTGITIMYMV EKLDAGDILT
160 170 180 190 200
QVEVEIEERE TTGSLFDKLS EAGAHLLSKT VPLLIQGKLE PIKQNEEEVT
210 220 230 240 250
FAYNIKREQE KIDWTKTGEE VYNHIRGLNP WPVAYTTLAG QVVKVWWGEK
260 270 280 290 300
VPVTKSAEAG TIVAIEEDGF VVATGNETGV KITELQPSGK KRMSCSQFLR
310
GTKPEIGTKL GENA
Length:314
Mass (Da):34,736
Last modified:June 1, 2003 - v1
Checksum:i8E81D02492DABEE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP27732.1.
AE017334 Genomic DNA. Translation: AAT33120.1.
AE017225 Genomic DNA. Translation: AAT56019.1.
RefSeqiNP_846246.1. NC_003997.3.
WP_000598790.1. NZ_LHUO01000006.1.
YP_029968.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP27732; AAP27732; BA_4004.
AAT33120; AAT33120; GBAA_4004.
AAT56019; AAT56019; BAS3717.
GeneIDi1086742.
2852995.
KEGGiban:BA_4004.
bar:GBAA_4004.
bat:BAS3717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP27732.1.
AE017334 Genomic DNA. Translation: AAT33120.1.
AE017225 Genomic DNA. Translation: AAT56019.1.
RefSeqiNP_846246.1. NC_003997.3.
WP_000598790.1. NZ_LHUO01000006.1.
YP_029968.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IQFX-ray2.40A/B/C/D1-314[»]
ProteinModelPortaliQ81WH2.
SMRiQ81WH2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_4004.

Protocols and materials databases

DNASUi1086742.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP27732; AAP27732; BA_4004.
AAT33120; AAT33120; GBAA_4004.
AAT56019; AAT56019; BAS3717.
GeneIDi1086742.
2852995.
KEGGiban:BA_4004.
bar:GBAA_4004.
bat:BAS3717.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciANTHRA:FMT-MONOMER.

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_BACAN
AccessioniPrimary (citable) accession number: Q81WH2
Secondary accession number(s): Q6HUM0, Q6KNV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 99 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.