[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7649177 [NCBI, ExPASy, EBI, Israel, Japan] Vaupel M., Thauer R.K.; "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."; Eur. J. Biochem. 231:773-778(1995).
[2]	PROTEIN SEQUENCE OF 1-31. DOI=10.1007/BF00245355; PubMed=1953299 [NCBI, ExPASy, EBI, Israel, Japan] Ma K., Linder D., Stetter K.O., Thauer R.K.; "Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri."; Arch. Microbiol. 155:593-600(1991).
[3]	CHARACTERIZATION. PubMed=2379499 [NCBI, ExPASy, EBI, Israel, Japan] Ma K., Thauer R.K.; "Purification and properties of N5, N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg)."; Eur. J. Biochem. 191:187-193(1990).
[4]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1006/jmbi.2000.3909; PubMed=10891279 [NCBI, ExPASy, EBI, Israel, Japan] Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U.; "Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea."; J. Mol. Biol. 300:935-950(2000).

Comments

FUNCTION: Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.
CATALYTIC ACTIVITY: 5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420.
PATHWAY: One-carbon metabolism; methanogenesis from carbone dioxide; methyl-CoM from 5,10-methylene-H(4)MPT: step 1/2 .
SUBUNIT: Homotetramer (Probable).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the mer family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X86477; CAA60203.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S66529; S66529.

3D structure databases

PDB

1F07; X-ray; 2.00 A; A/B/C/D=1-321.

[ExPASy / RCSB / EBI]

1F07; -.

Q50744; 1-321.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0018537;	Molecular function: coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01091; -; 1.
PBIL [Tree]

InterPro

IPR011251; Luciferase-like_bac.
IPR016048; Luciferase_mOase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.30; Luciferase_like; 1.

Pfam

PF00296; Bac_luciferase; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; Methanogenesis; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 321`	`321`	`5,10-methylenetetrahydromethanopterin reductase.`	`PRO_0000084812`
`CONFLICT`	`15 15`		`K -> W (in Ref. 2; AA sequence).`
`STRAND`	`2 7`	`6`
`STRAND`	`9 11`	`3`
`HELIX`	`13 25`	`13`
`STRAND`	`30 33`	`4`
`HELIX`	`42 51`	`10`
`STRAND`	`57 63`	`7`
`STRAND`	`65 68`	`4`
`HELIX`	`70 83`	`14`
`STRAND`	`90 92`	`3`
`HELIX`	`97 102`	`6`
`HELIX`	`110 125`	`16`
`STRAND`	`142 145`	`4`
`STRAND`	`148 151`	`4`
`HELIX`	`155 164`	`10`
`STRAND`	`166 170`	`5`
`HELIX`	`175 191`	`17`
`HELIX`	`196 198`	`3`
`STRAND`	`199 209`	`11`
`HELIX`	`213 229`	`17`
`HELIX`	`233 238`	`6`
`HELIX`	`245 253`	`9`
`TURN`	`254 256`	`3`
`HELIX`	`258 263`	`6`
`HELIX`	`267 273`	`7`
`STRAND`	`275 277`	`3`
`HELIX`	`279 291`	`13`
`STRAND`	`296 303`	`8`
`HELIX`	`307 319`	`13`

Sequence information

Length: 321 AA [This is the length of the unprocessed precursor]

Molecular weight: 33488 Da [This is the MW of the unprocessed precursor]

CRC64: 473DB8BD37486D43 [This is a checksum on the sequence]

        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

Q50744 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools