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Reviewed, UniProtKB/Swiss-Prot Q8TXY4 (MER_METKA)

Last modified February 9, 2010. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    5,10-methylenetetrahydromethanopterin reductase
    EC=1.5.99.11
Alternative name(s):
    Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase
    Methylene-H(4)MPT reductase
Gene names
Name: mer
Ordered Locus Names: MK0524
OrganismMethanopyrus kandleri [Complete proteome] [HAMAP]
Taxonomic identifier2320 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reversible reduction of methylene-H4MPT to methyl-H4MPT. HAMAP MF_01091

Catalytic activity

5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420. HAMAP MF_01091

Enzyme regulation

Requires the presence of relatively high concentrations of either sulfate or phosphate for maximal activity. HAMAP MF_01091

Pathway

One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 1/2. HAMAP MF_01091

Subunit structure

Homotetramer composed of two loosely associated dimers Probable. HAMAP MF_01091

Subcellular location

Cytoplasm HAMAP MF_01091.

Sequence similarities

Belongs to the mer family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 3493485,10-methylenetetrahydromethanopterin reductase HAMAP MF_01091
PRO_0000084808

Experimental info

Sequence conflict211H → A AA sequence Ref.3
Sequence conflict1621N → K in AAA92085. Ref.1
Sequence conflict1911D → N in AAA92085. Ref.1
Sequence conflict3441I → L in AAA92085. Ref.1

Secondary structure

........................................................... 349
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TXY4-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 12AF28EDF65F26F0

FASTA34937,501
        10         20         30         40         50         60 
MAEVSFGIEL LPDDKPTKIA HLIKVAEDNG FEYAWICDHY NNYSYMGVLT LAAVITSKIK 

        70         80         90        100        110        120 
LGPGITNPYT RHPLITASNI ATLDWISGGR AIIGMGPGDK ATFDKMGLPF PCKIPIWNPE 

       130        140        150        160        170        180 
AEDEVGPATA IREVKEVIYQ YLEGGPVEYE GKYVKTGTAD VNARSIQGSD IPFYMGAQGP 

       190        200        210        220        230        240 
IMLKTAGEIA DGVLVNASNP KDFEVAVPKI EEGAKEAGRS LDEIDVAAYT CFSIDKDEDK 

       250        260        270        280        290        300 
AIEATKIVVA FIVMGSPDVV LERHGIDTEK AEQIAEAIGK GDFGTAIGLV DEDMIEAFSI 

       310        320        330        340 
AGDPDTVVDK IEELLKAGVT QVVVGSPIGP DKEKAIELVG QEVIPHFKE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and growth phase-dependent transcription of the coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase-encoding genes from Methanobacterium thermoautotrophicum delta H and Methanopyrus kandleri."
Noelling J., Pihl T.D., Reeve J.N.
J. Bacteriol. 177:7238-7244(1995) [PubMed: 8522533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]"Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri."
Ma K., Linder D., Stetter K.O., Thauer R.K.
Arch. Microbiol. 155:593-600(1991) [PubMed: 1953299] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-27, CHARACTERIZATION.
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[4]"Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea."
Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U.
J. Mol. Biol. 300:935-950(2000) [PubMed: 10891279] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31567 Genomic DNA. Translation: AAA92085.1.
AE009439 Genomic DNA. Translation: AAM01739.1.
RefSeqNP_613809.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZWX-ray1.65A1-349[»]
ModBaseSearch...

Genome annotation databases

GeneID1476625.
GenomeReviewsGene locus MK0524 in contig AE009439_GR.
KEGGmka:MK0524.
NMPDRfig|190192.1.peg.522.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG497169.
OMALNEISDG.

Enzyme and pathway databases

BioCycMKAN190192:MK0524-MONOMER.
BRENDA1.5.99.11. 7577.

Family and domain databases

HAMAPMF_01091. F420_mer.
[Tree]
InterProIPR011251. Luciferase-like.
IPR019946. MeH4methanopterin_reductase.
[Graphical view]
Gene3DG3DSA:3.20.20.30. Luciferase_like. 1 hit.
TIGRFAMsTIGR03555. F420_mer. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMER_METKA
AccessionPrimary (citable) accession number: Q8TXY4
Secondary accession number(s): Q49598
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 53 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents