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P19499 (FRHB_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. 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:
Coenzyme F420 hydrogenase subunit beta

EC=1.12.98.1
Alternative name(s):
8-hydroxy-5-deazaflavin-reducing hydrogenase subunit beta
Short name=FRH
Gene names
Name:frhB
Ordered Locus Names:MTH_1297
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length281 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

H2 + oxidized coenzyme F420 = reduced coenzyme F420.

Cofactor

Nickel.

Iron-sulfur. There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.

FAD.

Subunit structure

Heterocomplex of the form (alpha1beta1gamma1)8.

Sequence similarities

Belongs to the FrhB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.3
Chain2 – 281280Coenzyme F420 hydrogenase subunit beta
PRO_0000159229

Experimental info

Sequence conflict41G → C Ref.2
Sequence conflict2301L → F in AAA72190. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19499 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 350DCEE9029C09E1

FASTA28130,771
        10         20         30         40         50         60 
MVLGTYKEIV SARSTDREIQ KLAQDGGIVT GLLAYALDEG IIEGAVVAGP GKEFWKPEPM 

        70         80         90        100        110        120 
VAMTSDELKA AAGTKYTFSP NVLMLKKAVR QYGIEKLGTV AIPCQTMGIR KAQTYPFGVR 

       130        140        150        160        170        180 
FVADKIKLLV GIYCMENFPY TSLQTFICEK LGLNMELVEK MDIGKGKFWV YTQDDVYTLP 

       190        200        210        220        230        240 
LKETHGYEQA GCKICKDYVA ELADVSTGSV GSPDGWSTVI TRTDSGDSIL KQAVEAGIFE 

       250        260        270        280 
TKPIEEVKPG LGLLEKLSAQ KKEKAEKNIA ARKEMGLPTP Y 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H."
Alex L.A., Reeve J.N., Orme-Johnson W.H., Walsh C.T.
Biochemistry 29:7237-7244(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31 AND 185-201.
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[2]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[3]"8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization."
Fox J.A., Livingston D.J., Orme-Johnson W.H., Walsh C.T.
Biochemistry 26:4219-4227(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-32.
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02914 Genomic DNA. Translation: AAA72190.1.
AE000666 Genomic DNA. Translation: AAB85777.1.
PIRD35620.
RefSeqNP_276416.1. NC_000916.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP19499. 1 interaction.
STRING187420.MTH1297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85777; AAB85777; MTH_1297.
GeneID1471014.
KEGGmth:MTH1297.

Phylogenomic databases

eggNOGCOG1035.
KOK00441.
OMAMENFPYN.
ProtClustDBPRK09325.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1299-MONOMER.

Family and domain databases

InterProIPR007516. Co_F420_Hydgase/DH_bsu_N.
IPR017679. Coenz_F420_hydrogenase_bsu.
IPR007525. FrhB_FdhB_C.
[Graphical view]
PfamPF04432. FrhB_FdhB_C. 1 hit.
PF04422. FrhB_FdhB_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR03289. frhB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFRHB_METTH
AccessionPrimary (citable) accession number: P19499
Secondary accession number(s): O27356
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 87 of the entry and version 4 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