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Q46389

- ACSE_MOOTH

UniProt

Q46389 - ACSE_MOOTH

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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

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

GO - Biological processi

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

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 [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:
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 29, 2014
This is version 65 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