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O28076

- FTR_ARCFU

UniProt

O28076 - FTR_ARCFU

Protein

Formylmethanofuran--tetrahydromethanopterin formyltransferase

Gene

ftr

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a formyl group from 5-formyl tetrahydromethanopterin (5-formyl-H4MPT) to methanofuran (MFR) so as to produce formylmethanofuran (formyl-MFR) and tetrahydromethanopterin (H4MPT).1 Publication

    Catalytic activityi

    Formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin.

    Pathwayi

    GO - Molecular functioni

    1. formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. lactate oxidation Source: UniProtKB-UniPathway
    2. one-carbon metabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Enzyme and pathway databases

    BioCyciAFUL224325:GJBC-2252-MONOMER.
    UniPathwayiUPA00701.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formylmethanofuran--tetrahydromethanopterin formyltransferase (EC:2.3.1.101)
    Alternative name(s):
    H4MPT formyltransferase
    Gene namesi
    Name:ftr
    Ordered Locus Names:AF_2207
    OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
    Taxonomic identifieri224325 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
    ProteomesiUP000002199: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297Formylmethanofuran--tetrahydromethanopterin formyltransferasePRO_0000138115Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi224325.AF2207.

    Structurei

    Secondary structure

    1
    297
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Beta strandi12 – 2615
    Helixi30 – 4112
    Turni47 – 493
    Beta strandi53 – 608
    Helixi62 – 643
    Beta strandi71 – 8010
    Helixi81 – 9515
    Turni96 – 983
    Beta strandi103 – 1075
    Beta strandi112 – 1154
    Helixi117 – 1215
    Helixi122 – 1254
    Beta strandi130 – 1345
    Beta strandi137 – 1437
    Beta strandi145 – 1539
    Beta strandi155 – 17218
    Helixi173 – 18816
    Helixi198 – 2003
    Beta strandi202 – 2043
    Beta strandi207 – 2093
    Helixi222 – 2243
    Helixi226 – 2283
    Helixi229 – 2324
    Beta strandi243 – 25311
    Helixi254 – 26815
    Beta strandi274 – 2785
    Turni283 – 2853
    Beta strandi288 – 2925
    Helixi293 – 2953

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M5HX-ray2.00A/B/C/D/E/F/G/H1-297[»]
    ProteinModelPortaliO28076.
    SMRiO28076. Positions 1-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO28076.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FTR family.Curated

    Phylogenomic databases

    eggNOGiCOG2037.
    KOiK00672.
    OMAiLERIGQC.

    Family and domain databases

    Gene3Di3.30.70.520. 2 hits.
    HAMAPiMF_00579. FTR.
    InterProiIPR014053. ForMFR_H4MPT_ForTrfase.
    IPR002770. ForMFR_H4MPT_ForTrfase_C.
    IPR023447. ForMFR_H4MPT_ForTrfase_fd-like.
    IPR022667. ForMFR_H4MPT_ForTrfase_N.
    [Graphical view]
    PfamiPF01913. FTR. 1 hit.
    PF02741. FTR_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006414. Ftr_formyl_trnsf. 1 hit.
    SUPFAMiSSF55112. SSF55112. 2 hits.
    TIGRFAMsiTIGR03119. one_C_fhcD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O28076-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVNGVEVEE TFAEAFDIKI ARVLITGYDY YWAWVAANEA TGFGTSVIMC    50
    PAEAGIEIKA KPSETPDGRP GYYIQICHMS KKGLEEQLLA RLGQCVLTAP 100
    TTAVFNGLPD AEEKFDTGFK LKFFADGYEK EVEVGGRKCW AVPMMEGDFI 150
    IENDIGYTNG IAGGNFFIMA ETQPSALAAA KAAVDAISDV EGVITPFPGG 200
    IVASGSKVGA NKYKFLKAST NEKFAPSIRD QVEGTQIPEG VKAVYEIVIN 250
    GLNADAIKEA TRVGILAATK IPGVVKITAG NYGGKLGKHI INLNELF 297
    Length:297
    Mass (Da):31,762
    Last modified:January 1, 1998 - v1
    Checksum:i1466551AFFE97E4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321Missing AA sequence (PubMed:1483480)Curated
    Sequence conflicti32 – 321Missing AA sequence (PubMed:8481089)Curated
    Sequence conflicti34 – 341W → I AA sequence (PubMed:1483480)Curated
    Sequence conflicti34 – 341W → I AA sequence (PubMed:8481089)Curated
    Sequence conflicti43 – 431F → T AA sequence (PubMed:8481089)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89046.1.
    PIRiG69525.
    RefSeqiNP_071032.1. NC_000917.1.
    WP_010879696.1. NC_000917.1.

    Genome annotation databases

    EnsemblBacteriaiAAB89046; AAB89046; AF_2207.
    GeneIDi1485436.
    KEGGiafu:AF2207.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89046.1 .
    PIRi G69525.
    RefSeqi NP_071032.1. NC_000917.1.
    WP_010879696.1. NC_000917.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M5H X-ray 2.00 A/B/C/D/E/F/G/H 1-297 [» ]
    ProteinModelPortali O28076.
    SMRi O28076. Positions 1-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224325.AF2207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB89046 ; AAB89046 ; AF_2207 .
    GeneIDi 1485436.
    KEGGi afu:AF2207.

    Phylogenomic databases

    eggNOGi COG2037.
    KOi K00672.
    OMAi LERIGQC.

    Enzyme and pathway databases

    UniPathwayi UPA00701 .
    BioCyci AFUL224325:GJBC-2252-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O28076.

    Family and domain databases

    Gene3Di 3.30.70.520. 2 hits.
    HAMAPi MF_00579. FTR.
    InterProi IPR014053. ForMFR_H4MPT_ForTrfase.
    IPR002770. ForMFR_H4MPT_ForTrfase_C.
    IPR023447. ForMFR_H4MPT_ForTrfase_fd-like.
    IPR022667. ForMFR_H4MPT_ForTrfase_N.
    [Graphical view ]
    Pfami PF01913. FTR. 1 hit.
    PF02741. FTR_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006414. Ftr_formyl_trnsf. 1 hit.
    SUPFAMi SSF55112. SSF55112. 2 hits.
    TIGRFAMsi TIGR03119. one_C_fhcD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
      Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
      , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
      Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
    2. "Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri."
      Breitung J., Borner G., Scholz S., Linder D., Stetter K.O., Thauer R.K.
      Eur. J. Biochem. 210:971-981(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-48.
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
    3. "Formylmethanofuran: tetrahydromethanopterin formyltransferase and N5,N10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea."
      Schworer B., Breitung J., Klein A.R., Stetter K.O., Thauer R.K.
      Arch. Microbiol. 159:225-232(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-48, FUNCTION.
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
    4. "Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship."
      Mamat B., Roth A., Grimm C., Ermler U., Tziatzios C., Schubert D., Thauer R.K., Shima S.
      Protein Sci. 11:2168-2178(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiFTR_ARCFU
    AccessioniPrimary (citable) accession number: O28076
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 100 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, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3