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Reviewed, UniProtKB/Swiss-Prot P80489 (FRHA_METBF)

Last modified November 25, 2008. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Coenzyme F420 hydrogenase subunit alpha
    EC=1.12.98.1
Alternative name(s):
    8-hydroxy-5-deazaflavin-reducing hydrogenase subunit alpha
      Short name=FRH
Gene names
Name: frhA
Ordered Locus Names: Mbar_A0452
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.

Catalytic activity

H(2) + coenzyme F420 = reduced coenzyme F420.

Cofactor

Nickel.

Iron-sulfur.

FAD.

Subunit structure

Pentamer of two alpha chains, two beta chains and a gamma chain.

Subcellular location

Cell membrane; Peripheral membrane protein.

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
Chain2 – 456455Coenzyme F420 hydrogenase subunit alpha
PRO_0000199721

Sites

Metal binding631Nickel Potential
Metal binding661Nickel Potential
Metal binding4321Nickel Potential
Metal binding4351Nickel Potential

Sequences

Sequence LengthMass (Da)Tools
P80489-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EEFBD0E04511D667

FASTA45650,769
        10         20         30         40         50         60 
MTKVVEISPT TRLEGHSKLT LKVDDQGIVE RGDWLSITPV RGIEKLAIGK TMEQVPKIAS 

        70         80         90        100        110        120 
RVCGICPIAH TLASTEAMEA SIGCEIPTDA KLLRTILHAA NRIHSIALHN ILILPDFYIP 

       130        140        150        160        170        180 
GTEKKFNLFA NEQPARSVMA RIVRIREIAQ TIGAIAGGEA IHPSNPRIGG MYYNVSPRAK 

       190        200        210        220        230        240 
QKMADLAKEG LVLVHEQMEF MFDVIRNMQN REFVEVAGKQ IPLPKKLGYH NQGVMATASM 

       250        260        270        280        290        300 
YGSSSLDDNP TWDFTRWKET RPWDWYMGEV TIDLEDPSYP IGGTTKIGTK ANPQMEACTG 

       310        320        330        340        350        360 
VPTYDGQPVE VGPRARLATF KNFDEKGTFA QHIARQMEYP DCCYTILRCL DNLNTSGKVL 

       370        380        390        400        410        420 
ADHIPQGDGS MGWAANEAPR GSNIHLARVK DGKVLWYDML VPTTWNFPTC SRALTGAPWQ 

       430        440        450 
IAEMVVRAYD PCVSCATHMI VVNEEEKIVT QKLMQW 

« Hide

References

« Hide 'large scale' references
[1]"Two F420-reducing hydrogenases in Methanosarcina barkeri."
Vaupel M., Thauer R.K.
Arch. Microbiol. 169:201-205(1998) [PubMed: 9477253] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
J. Bacteriol. 188:7922-7931(2006) [PubMed: 16980466] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro."
Michel R., Massanz C., Kostka S., Richter M., Fiebig K.
Eur. J. Biochem. 233:727-735(1995) [PubMed: 8521835] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.

Cross-references

Sequence databases

Y13763 Genomic DNA. Translation: CAA74090.1.
CP000099 Genomic DNA. Translation: AAZ69434.1.
PIRS63483.
RefSeqYP_304014.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3624328.
GenomeReviewsGene locus Mbar_A0452 in contig CP000099_GR.
KEGGmba:Mbar_A0452.
NMPDRfig|269797.3.peg.630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP80489.

Enzyme and pathway databases

BioCycMBAR269797:MBAR_A0452-MON.
MetaCyc:MON-12647.

Family and domain databases

InterProIPR017682. Coenz_F420_hydrogenase_asu.
IPR001501. Ni-dep_hyd_lsu.
[Graphical view]
PfamPF00374. NiFeSe_Hases. 1 hit.
[Graphical view]
PROSITEPS00507. NI_HGENASE_L_1. 1 hit.
PS00508. NI_HGENASE_L_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRHA_METBF
AccessionPrimary (citable) accession number: P80489
Secondary accession number(s): O33165, Q46FA8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 56 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

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