Reviewed, UniProtKB/Swiss-Prot P60227 (MVHA_METTM)

Names and origin

Protein names

Recommended 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

Organism

Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133)

Taxonomic identifier

79929 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	17 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Part of a complex that provides reducing equivalents for heterodisulfide reductase. Ref.2
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.1
Sequence similarities	Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.

Ontologies

Keywords
Ligand	Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›17	›17	F420-non-reducing hydrogenase subunit A		PRO_0000199727
Experimental info
	Non-terminal residue	17	1

Sequences

	Sequence		Length	Mass (Da)
	P60227-1 [UniParc]. Last modified January 16, 2004. Version 1. Checksum: C9AC068FA6024A73	FASTA	17	1,837
	10 VKLTMEPVTL IEGXAXI

References

[1]	"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, SUBUNIT, ASSOCIATION WITH HETERODISULFIDE REDUCTASE.
[2]	"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.

Cross-references

3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR018194. Ni-dep_hyd_lsu_Ni_BS. [Graphical view]
PROSITE	PS00507. NI_HGENASE_L_1. Partial match. PS00508. NI_HGENASE_L_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MVHA_METTM

Accession

Primary (citable) accession number: P60227

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	May 5, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)