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Q46389 (ACSE_MOOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:acsE
OrganismMoorella thermoacetica (Clostridium thermoaceticum)
Taxonomic identifier1525 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3 Ref.4

Catalytic activity

A [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate. Ref.1 Ref.3 Ref.4

Cofactor

Calcium. Ref.3 Ref.4

Subunit structure

Heterohexamer composed of 2 subunits of AcsC, 2 subunits of AcsD and 2 subunits of AcsE. Ref.4

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2622625-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase
PRO_0000422560

Regions

Domain1 – 246246Pterin-binding
Region202 – 2032Cobalamin binding

Sites

Metal binding1841Calcium 1
Metal binding2221Calcium 1; via carbonyl oxygen
Metal binding2221Calcium 2; via carbonyl oxygen
Metal binding2241Calcium 1
Metal binding2241Calcium 2
Binding site961Methyltetrahydrofolate
Binding site1601Methyltetrahydrofolate
Binding site1991Methyltetrahydrofolate
Binding site2021Methyltetrahydrofolate
Binding site2071Methyltetrahydrofolate
Site1991Required for formation of the transition state

Experimental info

Mutagenesis1991N → A: 20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity. Ref.3

Secondary structure

......................................... 262
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q46389 [UniParc].

Last modified October 1, 2001. Version 2.
Checksum: 62466A25D42496A1

FASTA26228,609
        10         20         30         40         50         60 
MLIIGERING MFGDIKRAIQ ERDPAPVQEW ARRQEEGGAR ALDLNVGPAV QDKVSAMEWL 

        70         80         90        100        110        120 
VEVTQEVSNL TLCLDSTNIK AIEAGLKKCK NRAMINSTNA EREKVEKLFP LAVEHGAALI 

       130        140        150        160        170        180 
GLTMNKTGIP KDSDTRLAFA MELVAAADEF GLPMEDLYID PLILPANVAQ DHAPEVLKTL 

       190        200        210        220        230        240 
QQIKMLADPA PKTVLGLSNV SQNCQNRPLI NRTFLAMAMA CGLDAAIADA CDEALIETAA 

       250        260 
TAEILLNQTV YCDSFVKMFK TR 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34780 Genomic DNA. Translation: AAA53548.2.
PIRI40795.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ46389.
SMRQ46389. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59668N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:METHCOCLTH-MONOMER.

Family and domain databases

Gene3D3.20.20.20. 1 hit.
InterProIPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]
PfamPF00809. Pterin_bind. 1 hit.
[Graphical view]
SUPFAMSSF51717. SSF51717. 1 hit.
PROSITEPS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ46389.

Entry information

Entry nameACSE_MOOTH
AccessionPrimary (citable) accession number: Q46389
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: October 1, 2001
Last modified: October 16, 2013
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references