Q46389 (ACSE_MOOTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

acsE

Organism

Moorella thermoacetica (Clostridium thermoaceticum)

Taxonomic identifier

1525 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	A [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate.
Cofactor	Calcium.
Subunit structure	Heterohexamer composed of 2 subunits of AcsC, 2 subunits of AcsD and 2 subunits of AcsE.
Sequence similarities	Belongs to the vitamin-B12 dependent methionine synthase family. Contains 1 pterin-binding domain.

Ontologies

Keywords
Biological process	Carbon dioxide fixation
Ligand	Calcium Cobalamin Cobalt Metal-binding
Molecular function	Methyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	pteridine-containing compound metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 262	262	5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase		PRO_0000422560
Regions
	Domain	1 – 246	246	Pterin-binding
	Region	202 – 203	2	Cobalamin binding
Sites
	Metal binding	184	1	Calcium 1
	Metal binding	222	1	Calcium 1; via carbonyl oxygen
	Metal binding	222	1	Calcium 2; via carbonyl oxygen
	Metal binding	224	1	Calcium 1
	Metal binding	224	1	Calcium 2
	Binding site	96	1	Methyltetrahydrofolate
	Binding site	160	1	Methyltetrahydrofolate
	Binding site	199	1	Methyltetrahydrofolate
	Binding site	202	1	Methyltetrahydrofolate
	Binding site	207	1	Methyltetrahydrofolate
	Site	199	1	Required for formation of the transition state
Experimental info
	Mutagenesis	199	1	N → A: 20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity.

Sequences

	Sequence		Length	Mass (Da)
	Q46389 [UniParc]. Last modified October 1, 2001. Version 2. Checksum: 62466A25D42496A1	FASTA	262	28,609
	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

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.

PIR

I40795.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q46389.

SMR

Q46389. Positions 1-262.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59668N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:METHCOCLTH-MONOMER.

Family and domain databases

Gene3D

3.20.20.20. 1 hit.

InterPro

IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]

Pfam

PF00809. Pterin_bind. 1 hit.
[Graphical view]

SUPFAM

SSF51717. DHP_synth_like. 1 hit.

PROSITE

PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q46389.

Entry information

Entry name

ACSE_MOOTH

Accession

Primary (citable) accession number: Q46389

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2013
Last sequence update:	October 1, 2001
Last modified:	May 29, 2013
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program