[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. PubMed=9151968 [NCBI, ExPASy, EBI, Israel, Japan] Klein A.R., Thauer R.K.; "Overexpression of the coenzyme-F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase gene from the hyperthermophilic Methanopyrus kandleri."; Eur. J. Biochem. 245:386-391(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; DOI=10.1073/pnas.032671499; PubMed=11930014 [NCBI, ExPASy, EBI, Israel, Japan] Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.; "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."; Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
[3]	PROTEIN SEQUENCE OF 2-35, AND CHARACTERIZATION. STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; PubMed=8215796 [NCBI, ExPASy, EBI, Israel, Japan] Klein A.R., Koch J., Stetter K.O., Thauer R.K.; "Two N5,N10-methylenetetrahydromethanopterin dehydrogenases in the extreme thermophile Methanopyrus kandleri: characterization of the coenzyme F420-dependent enzyme."; Arch. Microbiol. 160:186-192(1993).
[4]	CRYSTALLIZATION. DOI=10.1107/S0907444903014896; PubMed=12925803 [NCBI, ExPASy, EBI, Israel, Japan] Hagemeier C.H., Shima S., Warkentin E., Thauer R.K., Ermler U.; "Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from Methanopyrus kandleri: the selenomethionine-labelled and non-labelled enzyme crystallized in two different forms."; Acta Crystallogr. D 59:1653-1655(2003).
[5]	X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS). DOI=10.1016/S0022-2836(03)00949-5; PubMed=14499608 [NCBI, ExPASy, EBI, Israel, Japan] Hagemeier C.H., Shima S., Thauer R.K., Bourenkov G., Bartunik H.D., Ermler U.; "Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quarternary structure."; J. Mol. Biol. 332:1047-1057(2003).

Comments

FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
CATALYTIC ACTIVITY: 5,10-methylenetetrahydromethanopterin + coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420.
ENZYME REGULATION: Strictly dependent on the presence of salts for activity.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Optimum temperature is 75 degrees Celsius;
PATHWAY: One-carbon metabolism; methanogenesis from carbone dioxide; 5,10-methylene-H(4)MPT from 5,10-methenyl-H(4)MPT (cofactor F420 route): step 1/1 .
SUBUNIT: Homohexamer composed of a trimer of dimers.
SIMILARITY: Belongs to the MTD 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

Y10251; CAA71298.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE010303; AAM01228.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_613298.1; -.

3D structure databases

PDB

1QV9; X-ray; 1.54 A; A/B/C=1-283.	[ExPASy / RCSB / EBI]
1U6I; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-283.	[ExPASy / RCSB / EBI]
1U6J; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-283.	[ExPASy / RCSB / EBI]
1U6K; X-ray; 1.55 A; A/B/C=1-283.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1QV9; -.
1U6I; -.
1U6J; -.
1U6K; -.

ModBase

P94951.

Enzyme and pathway databases

BioCyc

MKAN190192:MK0011-MON; -.

Ontologies

GO:0030268;	Molecular function: methylenetetrahydromethanopterin dehydrogenase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00058; -; 1.
PBIL [Tree]

InterPro

IPR002844; Methylene_DHase.
Graphical view of domain structure.

Pfam

PF01993; MTD; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005627; MTD; 1.

BLOCKS

P94951.

Genome annotation databases

1477313; -.

AE009439_GR; MK0011.

mka:MK0011; -.

fig|190192.1.peg.11; -.

Phylogenomic databases

HOGENOM

P94951; -.

Genome annotation databases

CMR

P94951; MK0011.

Other

ProtoNet

P94951.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 283`	`282`	`F420-dependent methylenetetrahydromethanopterin dehydrogenase.`	`PRO_0000075039`
`CONFLICT`	`11 11`		`C -> E (in Ref. 3; AA sequence).`
`STRAND`	`4 10`	`7`
`HELIX`	`15 19`	`5`
`HELIX`	`22 24`	`3`
`STRAND`	`31 39`	`9`
`HELIX`	`46 63`	`18`
`STRAND`	`66 71`	`6`
`HELIX`	`78 88`	`11`
`STRAND`	`90 92`	`3`
`STRAND`	`94 99`	`6`
`HELIX`	`100 105`	`6`
`HELIX`	`106 111`	`6`
`STRAND`	`115 119`	`5`
`TURN`	`129 131`	`3`
`HELIX`	`134 150`	`17`
`HELIX`	`153 169`	`17`
`HELIX`	`175 177`	`3`
`STRAND`	`180 183`	`4`
`HELIX`	`185 190`	`6`
`HELIX`	`197 222`	`26`
`HELIX`	`227 257`	`31`

Sequence information

Length: 283 AA [This is the length of the unprocessed precursor]

Molecular weight: 31382 Da [This is the MW of the unprocessed precursor]

CRC64: D2B778CB34D3034C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVAKAIFIK CGNLGTSMMM DMLLDERADR EDVEFRVVGT SVKMDPECVE AAVEMALDIA 

        70         80         90        100        110        120 
EDFEPDFIVY GGPNPAAPGP SKAREMLADS EYPAVIIGDA PGLKVKDEME EQGLGYILVK 

       130        140        150        160        170        180 
PDAMLGARRE FLDPVEMAIY NADLMKVLAA TGVFRVVQEA FDELIEKAKE DEISENDLPK 

       190        200        210        220        230        240 
LVIDRNTLLE REEFENPYAM VKAMAALEIA ENVADVSVEG CFVEQDKERY VPIVASAHEM 

       250        260        270        280 
MRKAAELADE ARELEKSNDA VLRTPHAPDG KVLSKRKFME DPE

P94951 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