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Q46389

- ACSE_MOOTH

UniProt

Q46389 - ACSE_MOOTH

Protein

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase

Gene

acsE

Organism
Moorella thermoacetica (Clostridium thermoaceticum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 2 (01 Oct 2001)
      Previous versions | rss
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    Functioni

    Methyltransferase that mediates the transfer of a N5-methyl group of (6S)-methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation.3 Publications

    Catalytic activityi

    A [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate.3 Publications

    Cofactori

    Calcium.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei96 – 961Methyltetrahydrofolate2 Publications
    Binding sitei160 – 1601Methyltetrahydrofolate2 Publications
    Metal bindingi184 – 1841Calcium 12 Publications
    Binding sitei199 – 1991Methyltetrahydrofolate2 Publications
    Sitei199 – 1991Required for formation of the transition state
    Binding sitei202 – 2021Methyltetrahydrofolate2 Publications
    Binding sitei207 – 2071Methyltetrahydrofolate2 Publications
    Metal bindingi222 – 2221Calcium 1; via carbonyl oxygen2 Publications
    Metal bindingi222 – 2221Calcium 2; via carbonyl oxygen2 Publications
    Metal bindingi224 – 2241Calcium 12 Publications
    Metal bindingi224 – 2241Calcium 22 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. cobalamin binding Source: UniProtKB-KW
    3. methyltransferase activity Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. carbon fixation Source: UniProtKB
    2. pteridine-containing compound metabolic process Source: InterPro

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Carbon dioxide fixation

    Keywords - Ligandi

    Calcium, Cobalamin, Cobalt, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:METHCOCLTH-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase (EC:2.1.1.258)
    Alternative name(s):
    5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase
    Short name:
    MeTr
    Gene namesi
    Name:acsE
    OrganismiMoorella thermoacetica (Clostridium thermoaceticum)
    Taxonomic identifieri1525 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi199 – 1991N → A: 20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2622625-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferasePRO_0000422560Add
    BLAST

    Interactioni

    Subunit structurei

    Heterohexamer composed of 2 subunits of AcsC, 2 subunits of AcsD and 2 subunits of AcsE.2 Publications

    Protein-protein interaction databases

    DIPiDIP-59668N.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Helixi13 – 219
    Helixi24 – 3714
    Beta strandi40 – 456
    Helixi53 – 6513
    Beta strandi70 – 756
    Helixi79 – 8810
    Beta strandi93 – 986
    Helixi102 – 11413
    Beta strandi118 – 1236
    Helixi133 – 15018
    Helixi154 – 1563
    Beta strandi157 – 1604
    Turni166 – 1683
    Helixi172 – 18413
    Beta strandi192 – 1965
    Helixi197 – 2015
    Helixi207 – 22014
    Beta strandi225 – 2284
    Helixi233 – 24513
    Helixi255 – 2617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F6YX-ray2.20A/B1-262[»]
    2E7FX-ray2.20A/B1-262[»]
    2OGYX-ray2.30A/B1-262[»]
    4DJDX-ray2.38A/B1-262[»]
    4DJEX-ray3.50A/B1-262[»]
    4DJFX-ray3.03A/B1-262[»]
    ProteinModelPortaliQ46389.
    SMRiQ46389. Positions 1-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ46389.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 246246Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni202 – 2032Cobalamin binding

    Sequence similaritiesi

    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    InterProiIPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding.
    [Graphical view]
    PfamiPF00809. Pterin_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF51717. SSF51717. 1 hit.
    PROSITEiPS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q46389-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLIIGERING MFGDIKRAIQ ERDPAPVQEW ARRQEEGGAR ALDLNVGPAV    50
    QDKVSAMEWL VEVTQEVSNL TLCLDSTNIK AIEAGLKKCK NRAMINSTNA 100
    EREKVEKLFP LAVEHGAALI GLTMNKTGIP KDSDTRLAFA MELVAAADEF 150
    GLPMEDLYID PLILPANVAQ DHAPEVLKTL QQIKMLADPA PKTVLGLSNV 200
    SQNCQNRPLI NRTFLAMAMA CGLDAAIADA CDEALIETAA TAEILLNQTV 250
    YCDSFVKMFK TR 262
    Length:262
    Mass (Da):28,609
    Last modified:October 1, 2001 - v2
    Checksum:i62466A25D42496A1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34780 Genomic DNA. Translation: AAA53548.2.
    PIRiI40795.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34780 Genomic DNA. Translation: AAA53548.2 .
    PIRi I40795.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F6Y X-ray 2.20 A/B 1-262 [» ]
    2E7F X-ray 2.20 A/B 1-262 [» ]
    2OGY X-ray 2.30 A/B 1-262 [» ]
    4DJD X-ray 2.38 A/B 1-262 [» ]
    4DJE X-ray 3.50 A/B 1-262 [» ]
    4DJF X-ray 3.03 A/B 1-262 [» ]
    ProteinModelPortali Q46389.
    SMRi Q46389. Positions 1-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59668N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:METHCOCLTH-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q46389.

    Family and domain databases

    Gene3Di 3.20.20.20. 1 hit.
    InterProi IPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding.
    [Graphical view ]
    Pfami PF00809. Pterin_bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51717. SSF51717. 1 hit.
    PROSITEi PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum."
      Roberts D.L., Zhao S., Doukov T., Ragsdale S.W.
      J. Bacteriol. 176:6127-6130(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
      Strain: DSM 521.
    2. "Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase."
      Doukov T., Seravalli J., Stezowski J.J., Ragsdale S.W.
      Structure 8:817-830(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
    3. "Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases."
      Doukov T.I., Hemmi H., Drennan C.L., Ragsdale S.W.
      J. Biol. Chem. 282:6609-6618(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH METHYLTETRAHYDROFOLATE AND CALCIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF ASN-199.
    4. "Visualizing molecular juggling within a B12-dependent methyltransferase complex."
      Kung Y., Ando N., Doukov T.I., Blasiak L.C., Bender G., Seravalli J., Ragsdale S.W., Drennan C.L.
      Nature 484:265-269(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH ACSC; ACSD; METHYLTETRAHYDROFOLATE; COBALAMIN AND CALCIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiACSE_MOOTH
    AccessioniPrimary (citable) accession number: Q46389
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2013
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 64 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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