F420-dependent methylenetetrahydromethanopterin dehydrogenase

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Reviewed, UniProtKB/Swiss-Prot P94951 (MTD_METKA)

Last modified November 25, 2008. Version 64. History...

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

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Names and origin

Protein names

Recommended name:
    F420-dependent methylenetetrahydromethanopterin dehydrogenase
      Short name=MTD
    EC=1.5.99.9
Alternative name(s):
    Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase

Gene names

Name:	mtd
Ordered Locus Names:	MK0011

Organism

Methanopyrus kandleri [Complete proteome] [HAMAP]

Taxonomic identifier

2320 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

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Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (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.
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 structure	Homohexamer composed of a trimer of dimers.
Sequence similarities	Belongs to the MTD family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 75 degrees Celsius.

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Ontologies

Keywords
Biological process	Methanogenesis One-carbon metabolism
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ferredoxin hydrogenase activity Inferred from electronic annotation. Source: InterPro methylenetetrahydromethanopterin dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 283

282

F420-dependent methylenetetrahydromethanopterin dehydrogenase

PRO_0000075039

Experimental info

Sequence conflict

C → E AA sequence Ref.3

Secondary structure

283

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P94951-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D2B778CB34D3034C
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FASTA

283

31,382

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Overexpression of the coenzyme-F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase gene from the hyperthermophilic Methanopyrus kandleri." Klein A.R., Thauer R.K. Eur. J. Biochem. 245:386-391(1997) [PubMed: 9151968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." 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. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[3]	"Two N5,N10-methylenetetrahydromethanopterin dehydrogenases in the extreme thermophile Methanopyrus kandleri: characterization of the coenzyme F420-dependent enzyme." Klein A.R., Koch J., Stetter K.O., Thauer R.K. Arch. Microbiol. 160:186-192(1993) [PubMed: 8215796] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-35, CHARACTERIZATION. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[4]	"Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from Methanopyrus kandleri: the selenomethionine-labelled and non-labelled enzyme crystallized in two different forms." Hagemeier C.H., Shima S., Warkentin E., Thauer R.K., Ermler U. Acta Crystallogr. D 59:1653-1655(2003) [PubMed: 12925803] [Abstract] Cited for: CRYSTALLIZATION.
[5]	"Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quarternary structure." Hagemeier C.H., Shima S., Thauer R.K., Bourenkov G., Bartunik H.D., Ermler U. J. Mol. Biol. 332:1047-1057(2003) [PubMed: 14499608] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

Y10251 Genomic DNA. Translation: CAA71298.1.
AE010303 Genomic DNA. Translation: AAM01228.1.

RefSeq

NP_613298.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QV9	X-ray	1.54	A/B/C	1-283	[»]
1U6I	X-ray	2.20	A/B/C/D/E/F/G/H/I/J/K/L	1-283	[»]
1U6J	X-ray	2.40	A/B/C/D/E/F/G/H/I/J/K/L	1-283	[»]
1U6K	X-ray	1.55	A/B/C	1-283	[»]

ModBase

Search...

Genome annotation databases

GeneID

1477313.

GenomeReviews

Gene locus MK0011 in contig AE009439_GR.

KEGG

mka:MK0011.

NMPDR

fig|190192.1.peg.11.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P94951.

Enzyme and pathway databases

BioCyc

MKAN190192:MK0011-MON.

Family and domain databases

HAMAP

MF_00058.
[Tree]

InterPro

IPR002844. Methylene_DHase.
[Graphical view]

Pfam

PF01993. MTD. 1 hit.
[Graphical view]

PIRSF

PIRSF005627. MTD. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

MTD_METKA

Accession

Primary (citable) accession number: P94951
Secondary accession number(s): Q9UWL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents