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Protein

F420-dependent methylenetetrahydromethanopterin dehydrogenase

Gene

mtd

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible reduction of methenyl-H4MPT+ to methylene-H4MPT.1 Publication

Catalytic activityi

5,10-methylenetetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420.

Enzyme regulationi

Strictly dependent on the presence of salts for activity.

Temperature dependencei

Optimum temperature is 75 degrees Celsius.

Pathwayi: methanogenesis from CO(2)

This protein is involved in step 1 of the subpathway that synthesizes 5,10-methylene-5,6,7,8-tetrahydromethanopterin from 5,10-methenyl-5,6,7,8-tetrahydromethanopterin (coenzyme F420 route).
Proteins known to be involved in this subpathway in this organism are:
  1. F420-dependent methylenetetrahydromethanopterin dehydrogenase (mtd)
This subpathway is part of the pathway methanogenesis from CO(2), which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,10-methylene-5,6,7,8-tetrahydromethanopterin from 5,10-methenyl-5,6,7,8-tetrahydromethanopterin (coenzyme F420 route), the pathway methanogenesis from CO(2) and in One-carbon metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanogenesis, One-carbon metabolism

Enzyme and pathway databases

BRENDAi1.5.98.1. 3274.
UniPathwayiUPA00640; UER00695.

Names & Taxonomyi

Protein namesi
Recommended name:
F420-dependent methylenetetrahydromethanopterin dehydrogenase (EC:1.5.98.1)
Short name:
MTD
Alternative name(s):
Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase
Gene namesi
Name:mtd
Ordered Locus Names:MK0011
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
Proteomesi
  • UP000001826 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 283282F420-dependent methylenetetrahydromethanopterin dehydrogenasePRO_0000075039Add
BLAST

Interactioni

Subunit structurei

Homohexamer composed of a trimer of dimers.

Protein-protein interaction databases

STRINGi190192.MK0011.

Structurei

Secondary structure

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi15 – 195Combined sources
Helixi22 – 243Combined sources
Beta strandi31 – 399Combined sources
Helixi46 – 6318Combined sources
Beta strandi66 – 716Combined sources
Helixi78 – 8811Combined sources
Beta strandi90 – 923Combined sources
Beta strandi94 – 996Combined sources
Helixi100 – 1056Combined sources
Helixi106 – 1116Combined sources
Beta strandi115 – 1195Combined sources
Turni129 – 1313Combined sources
Helixi134 – 15017Combined sources
Helixi153 – 16917Combined sources
Helixi175 – 1773Combined sources
Beta strandi180 – 1834Combined sources
Helixi185 – 1906Combined sources
Helixi197 – 22226Combined sources
Helixi227 – 25731Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QV9X-ray1.54A/B/C1-283[»]
1U6IX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-283[»]
1U6JX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-283[»]
1U6KX-ray1.55A/B/C1-283[»]
3IQEX-ray1.80A/B/C/D/E/F1-283[»]
3IQFX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L1-283[»]
3IQZX-ray2.10A/B/C/D/E/F1-283[»]
ProteinModelPortaliP94951.
SMRiP94951. Positions 2-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP94951.

Family & Domainsi

Sequence similaritiesi

Belongs to the MTD family.Curated

Phylogenomic databases

eggNOGiarCOG04382. Archaea.
COG1927. LUCA.
HOGENOMiHOG000227051.
KOiK00319.
OMAiKGCFMTK.

Family and domain databases

HAMAPiMF_00058. MTD.
InterProiIPR002844. Methylene_DH.
[Graphical view]
PfamiPF01993. MTD. 1 hit.
[Graphical view]
PIRSFiPIRSF005627. MTD. 1 hit.
ProDomiPD017604. Methylene_DH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF102324. SSF102324. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P94951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVAKAIFIK CGNLGTSMMM DMLLDERADR EDVEFRVVGT SVKMDPECVE
60 70 80 90 100
AAVEMALDIA EDFEPDFIVY GGPNPAAPGP SKAREMLADS EYPAVIIGDA
110 120 130 140 150
PGLKVKDEME EQGLGYILVK PDAMLGARRE FLDPVEMAIY NADLMKVLAA
160 170 180 190 200
TGVFRVVQEA FDELIEKAKE DEISENDLPK LVIDRNTLLE REEFENPYAM
210 220 230 240 250
VKAMAALEIA ENVADVSVEG CFVEQDKERY VPIVASAHEM MRKAAELADE
260 270 280
ARELEKSNDA VLRTPHAPDG KVLSKRKFME DPE
Length:283
Mass (Da):31,382
Last modified:January 23, 2007 - v3
Checksum:iD2B778CB34D3034C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111C → E AA sequence (PubMed:8215796).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10251 Genomic DNA. Translation: CAA71298.1.
AE009439 Genomic DNA. Translation: AAM01228.1.

Genome annotation databases

EnsemblBacteriaiAAM01228; AAM01228; MK0011.
KEGGimka:MK0011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10251 Genomic DNA. Translation: CAA71298.1.
AE009439 Genomic DNA. Translation: AAM01228.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QV9X-ray1.54A/B/C1-283[»]
1U6IX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-283[»]
1U6JX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-283[»]
1U6KX-ray1.55A/B/C1-283[»]
3IQEX-ray1.80A/B/C/D/E/F1-283[»]
3IQFX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L1-283[»]
3IQZX-ray2.10A/B/C/D/E/F1-283[»]
ProteinModelPortaliP94951.
SMRiP94951. Positions 2-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190192.MK0011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM01228; AAM01228; MK0011.
KEGGimka:MK0011.

Phylogenomic databases

eggNOGiarCOG04382. Archaea.
COG1927. LUCA.
HOGENOMiHOG000227051.
KOiK00319.
OMAiKGCFMTK.

Enzyme and pathway databases

UniPathwayiUPA00640; UER00695.
BRENDAi1.5.98.1. 3274.

Miscellaneous databases

EvolutionaryTraceiP94951.

Family and domain databases

HAMAPiMF_00058. MTD.
InterProiIPR002844. Methylene_DH.
[Graphical view]
PfamiPF01993. MTD. 1 hit.
[Graphical view]
PIRSFiPIRSF005627. MTD. 1 hit.
ProDomiPD017604. Methylene_DH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF102324. SSF102324. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).

Entry informationi

Entry nameiMTD_METKA
AccessioniPrimary (citable) accession number: P94951
Secondary accession number(s): Q9UWL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.