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Reviewed, UniProtKB/Swiss-Prot P94954 (MCH_METKA)

Last modified June 16, 2009. Version 72. 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:
    Methenyltetrahydromethanopterin cyclohydrolase
    EC=3.5.4.27
Alternative name(s):
    Methenyl-H4MPT cyclohydrolase
Gene names
Name: mch
Ordered Locus Names: MK0625
OrganismMethanopyrus kandleri [Complete proteome] [HAMAP]
Taxonomic identifier2320 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length316 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 interconversion of 5-formyl-H4MPT to methenyl-H4MPT+. HAMAP MF_00486

Catalytic activity

5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = 5-formyl-5,6,7,8-tetrahydromethanopterin. HAMAP MF_00486

Pathway

One-carbon metabolism; methanogenesis from carbone dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 3/3. HAMAP MF_00486

Subunit structure

Homotrimer. HAMAP MF_00486

Subcellular location

Cytoplasm. HAMAP MF_00486

Sequence similarities

Belongs to the MCH family.

Ontologies

Keywords
   Biological processMethanogenesis
One-carbon metabolism
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmethenyltetrahydromethanopterin cyclohydrolase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP MF_00486
Chain2 – 316315Methenyltetrahydromethanopterin cyclohydrolase HAMAP MF_00486
PRO_0000140882

Secondary structure

................................................................. 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P94954-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: D6D4097DE6BE0500

FASTA31634,044
        10         20         30         40         50         60 
MVSVNENALP LVERMIERAE LLNVEVQELE NGTTVIDCGV EAAGGFEAGL LFSEVCMGGL 

        70         80         90        100        110        120 
ATVELTEFEH DGLCLPAVQV TTDHPAVSTL AAQKAGWQVQ VGDYFAMGSG PARALALKPK 

       130        140        150        160        170        180 
ETYEEIDYED DADVAILCLE SSELPDEDVA EHVADECGVD PENLYLLVAP TASIVGSVQV 

       190        200        210        220        230        240 
SARVVETGLY KLLEVLEYDV TRVKYATGTA PIAPVADDDG EAMGRTNDCI LYGGTVYLYV 

       250        260        270        280        290        300 
EGDDELPEVV EELPSEASED YGKPFMKIFE EADYDFYKID PGVFAPARVV VNDLSTGKTY 

       310 
TAGEINVDVL KESFGL 

« Hide

References

« Hide 'large scale' references
[1]"Overproduction and one-step purification of the N5,N10-methenyltetrahydromethanopterin cyclohydrolase (Mch) from the hyperthermophilic Methanopyrus kandleri."
Vaupel M., Vorholt J.A., Thauer R.K.
Extremophiles 2:15-22(1998) [PubMed: 9676239] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[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]"The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri."
Grabarse W., Vaupel M., Vorholt J.A., Shima S., Thauer R.K., Wittershagen A., Bourenkov G., Bartunik H.D., Ermler U.
Structure 7:1257-1268(1999) [PubMed: 10545331] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

Y08849 Genomic DNA. Translation: CAA70072.1. Different initiation.
AE010355 Genomic DNA. Translation: AAM01840.1. Different initiation.
PIRT45099.
RefSeqNP_613910.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QLMX-ray2.00A1-314[»]
ModBaseSearch...

Genome annotation databases

GeneID1476726.
GenomeReviewsGene locus MK0625 in contig AE009439_GR.
KEGGmka:MK0625.
NMPDRfig|190192.1.peg.623.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP94954.

Enzyme and pathway databases

BioCycMKAN190192:MK0625-MON.
BRENDA3.5.4.27. 7577.

Family and domain databases

HAMAPMF_00486.
[Tree]
InterProIPR003209. METHMP_CycHdrlase.
[Graphical view]
PfamPF02289. MCH. 1 hit.
[Graphical view]
ProDomPD011637. Cyclohydrolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03120. one_C_mch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMCH_METKA
AccessionPrimary (citable) accession number: P94954
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 72 of the entry and version 4 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