P19499 (FRHB_METTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter › Methanobacterium thermoformicicum

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 + 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.

Ontologies

Keywords
Ligand	Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular_function	coenzyme F420 hydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW nickel cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1 Ref.3
	Chain	2 – 281	280	Coenzyme F420 hydrogenase subunit beta		PRO_0000159229
Experimental info
	Sequence conflict	4	1	G → C Ref.2
	Sequence conflict	230	1	L → F in AAA72190. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P19499 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 350DCEE9029C09E1	FASTA	281	30,771
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	D35620.
RefSeq	NP_276416.1. NC_000916.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P19499. 1 interaction.
STRING	187420.MTH1297.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB85777; AAB85777; MTH_1297.
GeneID	1471014.
KEGG	mth:MTH1297.
Phylogenomic databases
eggNOG	COG1035.
KO	K00441.
OMA	MENFPYN.
ProtClustDB	PRK09325.
Enzyme and pathway databases
BioCyc	MTHE187420:GJNM-1299-MONOMER.
Family and domain databases
InterPro	IPR007516. Co_F420_Hydgase/DH_bsu_N. IPR017679. Coenz_F420_hydrogenase_bsu. IPR007525. FrhB_FdhB_C. [Graphical view]
Pfam	PF04432. FrhB_FdhB_C. 1 hit. PF04422. FrhB_FdhB_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR03289. frhB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FRHB_METTH

Accession

Primary (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:	May 1, 2013
This is version 85 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program