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Protein

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

Gene

acsE

Organism
Moorella thermoacetica (Clostridium thermoaceticum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Ca2+2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96Methyltetrahydrofolate2 Publications1
Binding sitei160Methyltetrahydrofolate2 Publications1
Metal bindingi184Calcium 12 Publications1
Binding sitei199Methyltetrahydrofolate2 Publications1
Sitei199Transition state stabilizer1
Binding sitei202Methyltetrahydrofolate2 Publications1
Binding sitei207Methyltetrahydrofolate2 Publications1
Metal bindingi222Calcium 1; via carbonyl oxygen2 Publications1
Metal bindingi222Calcium 2; via carbonyl oxygen2 Publications1
Metal bindingi224Calcium 12 Publications1
Metal bindingi224Calcium 22 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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.
BRENDAi2.1.1.258. 1528.

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)DescriptionActionsGraphical viewLength
Mutagenesisi199N → A: 20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004225601 – 2625-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferaseAdd BLAST262

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.
STRINGi264732.Moth_1197.

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi13 – 21Combined sources9
Helixi24 – 37Combined sources14
Beta strandi40 – 45Combined sources6
Helixi53 – 65Combined sources13
Beta strandi70 – 75Combined sources6
Helixi79 – 88Combined sources10
Beta strandi93 – 98Combined sources6
Helixi102 – 114Combined sources13
Beta strandi118 – 123Combined sources6
Helixi133 – 150Combined sources18
Helixi154 – 156Combined sources3
Beta strandi157 – 160Combined sources4
Turni166 – 168Combined sources3
Helixi172 – 184Combined sources13
Beta strandi192 – 196Combined sources5
Helixi197 – 201Combined sources5
Helixi207 – 220Combined sources14
Beta strandi225 – 228Combined sources4
Helixi233 – 245Combined sources13
Helixi255 – 261Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46389.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 246Pterin-bindingPROSITE-ProRule annotationAdd BLAST246

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni202 – 203Cobalamin binding2

Sequence similaritiesi

Contains 1 pterin-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107VP5. Bacteria.
COG1410. LUCA.

Family and domain databases

Gene3Di3.20.20.20. 1 hit.
InterProiIPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding_dom.
[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

        10         20         30         40         50
MLIIGERING MFGDIKRAIQ ERDPAPVQEW ARRQEEGGAR ALDLNVGPAV
60 70 80 90 100
QDKVSAMEWL VEVTQEVSNL TLCLDSTNIK AIEAGLKKCK NRAMINSTNA
110 120 130 140 150
EREKVEKLFP LAVEHGAALI GLTMNKTGIP KDSDTRLAFA MELVAAADEF
160 170 180 190 200
GLPMEDLYID PLILPANVAQ DHAPEVLKTL QQIKMLADPA PKTVLGLSNV
210 220 230 240 250
SQNCQNRPLI NRTFLAMAMA CGLDAAIADA CDEALIETAA TAEILLNQTV
260
YCDSFVKMFK TR
Length:262
Mass (Da):28,609
Last modified:October 1, 2001 - v2
Checksum:i62466A25D42496A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34780 Genomic DNA. Translation: AAA53548.2.
PIRiI40795.
RefSeqiWP_011392711.1. NZ_CP012370.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34780 Genomic DNA. Translation: AAA53548.2.
PIRiI40795.
RefSeqiWP_011392711.1. NZ_CP012370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59668N.
STRINGi264732.Moth_1197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107VP5. Bacteria.
COG1410. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:METHCOCLTH-MONOMER.
BRENDAi2.1.1.258. 1528.

Miscellaneous databases

EvolutionaryTraceiQ46389.

Family and domain databases

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

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: November 2, 2016
This is version 76 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

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.