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Reviewed, UniProtKB/Swiss-Prot Q50744 (MER_METTM)

Last modified February 9, 2010. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    5,10-methylenetetrahydromethanopterin reductase
    EC=1.5.99.11
Alternative name(s):
    Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase
    Methylene-H(4)MPT reductase
Gene names
Name: mer
OrganismMethanobacterium thermoautotrophicum (strain Marburg / DSM 2133)
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reversible reduction of methylene-H4MPT to methyl-H4MPT. HAMAP MF_01091

Catalytic activity

5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420. HAMAP MF_01091

Pathway

One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 1/2. HAMAP MF_01091

Subunit structure

Homotetramer Probable. HAMAP MF_01091

Subcellular location

Cytoplasm HAMAP MF_01091.

Sequence similarities

Belongs to the mer family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3213215,10-methylenetetrahydromethanopterin reductase HAMAP MF_01091
PRO_0000084812

Experimental info

Sequence conflict151K → W AA sequence Ref.2

Secondary structure

....................................................... 321
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q50744-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 473DB8BD37486D43

FASTA32133,488
        10         20         30         40         50         60 
MKFGIEFVPN EPIEKIVKLV KLAEDVGFEY AWITDHYNNK NVYETLALIA EGTETIKLGP 

        70         80         90        100        110        120 
GVTNPYVRSP AITASAIATL DELSNGRATL GIGPGDKATF DALGIEWVKP VSTIRDAIAM 

       130        140        150        160        170        180 
MRTLLAGEKT ESGAQLMGVK AVQEKIPIYM GAQGPMMLKT AGEISDGALI NASNPKDFEA 

       190        200        210        220        230        240 
AVPLIKEGAE AAGKSIADID VAAYTCCSID EDAAAAANAA KIVVAFIAAG SPPPVFERHG 

       250        260        270        280        290        300 
LPADTGKKFG ELLGKGDFGG AIGAVDDALM EAFSVVGTPD EFIPKIEALG EMGVTQYVAG 

       310        320 
SPIGPDKEKS IKLLGEVIAS F 

« Hide

References

[1]"Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase (Mer) from Methanobacterium thermoautotrophicum strain Marburg -- cloning, sequencing, transcriptional analysis, and functional expression in Escherichia coli of the mer gene."
Vaupel M., Thauer R.K.
Eur. J. Biochem. 231:773-778(1995) [PubMed: 7649177] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri."
Ma K., Linder D., Stetter K.O., Thauer R.K.
Arch. Microbiol. 155:593-600(1991) [PubMed: 1953299] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-31.
[3]"Purification and properties of N5, N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg)."
Ma K., Thauer R.K.
Eur. J. Biochem. 191:187-193(1990) [PubMed: 2379499] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea."
Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U.
J. Mol. Biol. 300:935-950(2000) [PubMed: 10891279] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86477 Genomic DNA. Translation: CAA60203.1.
PIRS66529.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F07X-ray2.00A/B/C/D1-321[»]
ModBaseSearch...

Family and domain databases

HAMAPMF_01091. F420_mer.
[Tree]
InterProIPR011251. Luciferase-like.
IPR019946. MeH4methanopterin_reductase.
[Graphical view]
Gene3DG3DSA:3.20.20.30. Luciferase_like. 1 hit.
TIGRFAMsTIGR03555. F420_mer. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMER_METTM
AccessionPrimary (citable) accession number: Q50744
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents