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Q81WH2

- FMT_BACAN

UniProt

Q81WH2 - FMT_BACAN

Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    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

    1. methionyl-tRNA formyltransferase activity Source: UniProtKB-HAMAP
    2. methyltransferase activity Source: InterPro

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    BioCyciANTHRA:FMT-MONOMER.
    BANT260799:GJAJ-3775-MONOMER.
    BANT261594:GJ7F-3892-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
    ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Methionyl-tRNA formyltransferasePRO_0000082910Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi198094.BA_4004.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi13 – 2210
    Beta strandi26 – 316
    Turni39 – 424
    Helixi48 – 558
    Helixi69 – 7810
    Beta strandi81 – 877
    Helixi94 – 974
    Beta strandi104 – 1107
    Beta strandi114 – 1185
    Helixi120 – 1267
    Beta strandi130 – 1389
    Beta strandi148 – 1558
    Helixi162 – 18524
    Helixi196 – 1983
    Helixi207 – 2104
    Helixi218 – 2269
    Turni227 – 2326
    Beta strandi234 – 2385
    Beta strandi241 – 25212
    Beta strandi261 – 2655
    Beta strandi270 – 2723
    Beta strandi275 – 28713
    Helixi295 – 3017

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IQFX-ray2.40A/B/C/D1-314[»]
    ProteinModelPortaliQ81WH2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 1134Tetrahydrofolate (THF) bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the Fmt family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0223.
    HOGENOMiHOG000261177.
    KOiK00604.
    OMAiQRFKIYE.
    OrthoDBiEOG6B09WV.

    Family and domain databases

    Gene3Di3.10.25.10. 1 hit.
    3.40.50.170. 1 hit.
    HAMAPiMF_00182. Formyl_trans.
    InterProiIPR005794. 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]
    PANTHERiPTHR11138. PTHR11138. 1 hit.
    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

    MIKVVFMGTP DFSVPVLRRL IEDGYDVIGV VTQPDRPVGR KKVLTPTPVK    50
    VEAEKHGIPV LQPLRIREKD EYEKVLALEP DLIVTAAFGQ IVPNEILEAP 100
    KYGCINVHAS LLPELRGGAP IHYAIMEGKE KTGITIMYMV EKLDAGDILT 150
    QVEVEIEERE TTGSLFDKLS EAGAHLLSKT VPLLIQGKLE PIKQNEEEVT 200
    FAYNIKREQE KIDWTKTGEE VYNHIRGLNP WPVAYTTLAG QVVKVWWGEK 250
    VPVTKSAEAG TIVAIEEDGF VVATGNETGV KITELQPSGK KRMSCSQFLR 300
    GTKPEIGTKL GENA 314
    Length:314
    Mass (Da):34,736
    Last modified:June 1, 2003 - v1
    Checksum:i8E81D02492DABEE2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_020645.1. NC_007530.2.
    YP_029968.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP27732; AAP27732; BA_4004.
    AAT33120; AAT33120; GBAA_4004.
    AAT56019; AAT56019; BAS3717.
    GeneIDi1086742.
    2816238.
    2852995.
    KEGGiban:BA_4004.
    bar:GBAA_4004.
    bat:BAS3717.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP27732.1 .
    AE017334 Genomic DNA. Translation: AAT33120.1 .
    AE017225 Genomic DNA. Translation: AAT56019.1 .
    RefSeqi NP_846246.1. NC_003997.3.
    YP_020645.1. NC_007530.2.
    YP_029968.1. NC_005945.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IQF X-ray 2.40 A/B/C/D 1-314 [» ]
    ProteinModelPortali Q81WH2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198094.BA_4004.

    Protocols and materials databases

    DNASUi 1086742.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP27732 ; AAP27732 ; BA_4004 .
    AAT33120 ; AAT33120 ; GBAA_4004 .
    AAT56019 ; AAT56019 ; BAS3717 .
    GeneIDi 1086742.
    2816238.
    2852995.
    KEGGi ban:BA_4004.
    bar:GBAA_4004.
    bat:BAS3717.

    Phylogenomic databases

    eggNOGi COG0223.
    HOGENOMi HOG000261177.
    KOi K00604.
    OMAi QRFKIYE.
    OrthoDBi EOG6B09WV.

    Enzyme and pathway databases

    BioCyci ANTHRA:FMT-MONOMER.
    BANT260799:GJAJ-3775-MONOMER.
    BANT261594:GJ7F-3892-MONOMER.

    Family and domain databases

    Gene3Di 3.10.25.10. 1 hit.
    3.40.50.170. 1 hit.
    HAMAPi MF_00182. Formyl_trans.
    InterProi IPR005794. 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 ]
    PANTHERi PTHR11138. PTHR11138. 1 hit.
    Pfami PF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    TIGRFAMsi TIGR00460. fmt. 1 hit.
    PROSITEi PS00373. GART. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
      Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
      , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
      Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames / isolate Porton.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames ancestor.
    3. "Complete genome sequence of Bacillus anthracis Sterne."
      Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sterne.

    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: October 1, 2014
    This is version 86 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

    External Data

    Dasty 3