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P60227 (MVHA_METTM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F420-non-reducing hydrogenase subunit A

EC=1.12.99.-
Alternative name(s):
Methyl viologen-reducing hydrogenase subunit alpha
Short name=MVH subunit A
Gene names
Name:mvhA
Ordered Locus Names:MTBMA_c15170
OrganismMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of a complex that provides reducing equivalents for heterodisulfide reductase. Ref.3

Cofactor

Nickel Potential.

Subunit structure

The F420-non-reducing hydrogenase is composed of three subunits; mvhA, mvhD and mvhG. It forms a complex with the heterodisulfide reductase (hdr). Ref.2

Sequence similarities

Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 472471F420-non-reducing hydrogenase subunit A
PRO_0000199727

Sites

Metal binding611Nickel Potential
Metal binding641Nickel Potential
Metal binding4421Nickel Potential
Metal binding4451Nickel Potential

Experimental info

Sequence conflict111R → L AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P60227 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 5993E7AC4BC0579F

FASTA47252,839
        10         20         30         40         50         60 
MVKLTMEPVT RIEGHAKITV HLDDAGNVED TRLHVMEFRG FEKFLQGRPI EEAPRIVPRI 

        70         80         90        100        110        120 
CGICDVQHHL AAAKAVDACF GFEPDDVLPA AYKMREIMNW GSYMHSHGLH FYFLAAPDFI 

       130        140        150        160        170        180 
AGKDRKTRNV FQIIKDAPDV ALQAIELRKN ALEIVRATGG RPIHPTSSTP GGISTELDDE 

       190        200        210        220        230        240 
TQKDLLQKAQ RNVELAEATL ELAVPIFEEN IDLVNSLGNI ETYHTGLVKN GVWDVYDGIV 

       250        260        270        280        290        300 
RIKDKEGNLF REFKPADYAD TIAEHVKPYS WLKFPYIKDL GYPDGVYRVS PLSRLNVADK 

       310        320        330        340        350        360 
MPDAAPKAQD YFKEFQDKFG YAQQTLLYHW ARLIEVLACA ECAADALEGD LSGEKFPDSL 

       370        380        390        400        410        420 
ERQAGDGVGI VEAPRGTLTH HYTCDENGLI TKANIVVATI QNNPAMEMGI QKVAQDYIKP 

       430        440        450        460        470 
GVEVDDKIFN LMEMVIRAYD PCLSCATHTI DSQMRLATLE VYDSEGDLVK RI 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
J. Bacteriol. 192:5850-5851(2010) [PubMed: 20802048] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[2]"H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties."
Setzke E., Hedderich R., Heiden S., Thauer R.K.
Eur. J. Biochem. 220:139-148(1994) [PubMed: 8119281] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18, SUBUNIT, ASSOCIATION WITH HETERODISULFIDE REDUCTASE.
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[3]"Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis."
Stojanowic A., Mander G.J., Duin E.C., Hedderich R.
Arch. Microbiol. 180:194-203(2003) [PubMed: 12856108] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH HETERODISULFIDE REDUCTASE.
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001710 Genomic DNA. Translation: ADL59096.1.
RefSeqYP_003850409.1. NC_014408.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9705226.
GenomeReviewsGene locus MTBMA_c15170 in contig CP001710_GR.
KEGGmmg:MTBMA_c15170.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAEVRGFEK.

Family and domain databases

InterProIPR001501. Ni-dep_hyd_lsu.
IPR018194. Ni-dep_hyd_lsu_Ni_BS.
[Graphical view]
KOK14126.
PfamPF00374. NiFeSe_Hases. 2 hits.
[Graphical view]
PROSITEPS00507. NI_HGENASE_L_1. 1 hit.
PS00508. NI_HGENASE_L_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMVHA_METTM
AccessionPrimary (citable) accession number: P60227
Secondary accession number(s): D9PXZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 30, 2010
Last modified: November 16, 2011
This is version 26 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families