EC 1.12.98.2
H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase
N(5),N(10)-methenyltetrahydromethanopterin hydrogenase
H(2)-dependent methylene-H(4)MPT dehydrogenase

Gene name

	Name:	hmd
	Synonyms:	mth

From

Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133)

[TaxID: 79929]

Taxonomy

Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1765081 [NCBI, ExPASy, EBI, Israel, Japan] Von Buenau R., Zirngibl C., Thauer R.K., Klein A.; "Hydrogen-forming and coenzyme-F420-reducing methylene tetrahydromethanopterin dehydrogenase are genetically distinct enzymes in Methanobacterium thermoautotrophicum (Marburg)."; Eur. J. Biochem. 202:1205-1208(1991).
[2]	CHARACTERIZATION. PubMed=1521540 [NCBI, ExPASy, EBI, Israel, Japan] Zirngibl C., van Dongen W., Schwoerer B., von Buenau R., Richter M., Klein A., Thauer R.K.; "H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea."; Eur. J. Biochem. 208:511-520(1992).

Comments

FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
CATALYTIC ACTIVITY: H₂ + 5,10-methenyltetrahydromethanopterin = H⁺ + 5,10-methylenetetrahydromethanopterin.
PATHWAY: One-carbon metabolism; methanogenesis from carbone dioxide; 5,10-methylene-H(4)MPT from 5,10-methenyl-H(4)MPT (hydrogen route): step 1/1 .
SIMILARITY: Belongs to the HMD 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

X59547; CAA42121.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S19705; S19705.

3D structure databases

ModBase

P32440.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0018537;	Molecular function: coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity (inferred from electronic annotation from InterPro).
GO:0047068;	Molecular function: N5,N10-methenyltetrahydromethanopterin hydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0019386;	Biological process: methanogenesis, from carbon dioxide (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01090; -; 1.
PBIL [Tree]

InterPro

IPR004889; HMD.
IPR010062; HMD_sub.
Graphical view of domain structure.

Pfam

PF03201; HMD; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01723; hmd_TIGR; 1.

Other

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

Keywords

Methanogenesis; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 344`	`344`	`5,10-methenyltetrahydromethanopterin hydrogenase.`	`PRO_0000218512`
`CONFLICT`	`74 75`		`DD -> EH (in Ref. 1; CAA42121).`
`CONFLICT`	`304 305`		`ID -> RY (in Ref. 1; CAA42121).`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 37704 Da [This is the MW of the unprocessed precursor]

CRC64: 5DA41A4BCA5ED64A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLAILGAGC YRTHAASGIT NFSRACEVAE MVGKPEIAMT HSTITMGAEL KELAGVDEVV 

        70         80         90        100        110        120 
VADPVFDNQF TVIDDFAYED VIEAHKEDPE NIMPQIREKV NEVAKELPKP PEGAIHFTHP 

       130        140        150        160        170        180 
EDLGFEITTD DREAVADADF IMTWFPKGDM QPDIINKFID DIKPGAIVTH ACTIPTTKFY 

       190        200        210        220        230        240 
KIFEQKHGDL VTKPETLNVT SYHPGAVPEM KGQVYIAEGY ASEDAIETLF ELGQKARGNA 

       250        260        270        280        290        300 
YRLPAELLGP VCDMCSALTA MTYACILSYR DSVTQVLGAP ASFAQMMAKE SLEQITALME 

       310        320        330        340 
KVGIDKMEEN LDPGALLGTA DSMNFGASAE ILPTVFEILE KRKK

P32440 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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