Reviewed, UniProtKB/Swiss-Prot P19496 (FRHA_METTH)

Names and origin

Protein names

Recommended 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:	MTH_1300

Organism

Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	405 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/(alpha1beta1gamma1) unit of the FRH. FAD.
Subunit structure	Heterocomplex of the form (alpha1beta1gamma1)8.
Sequence similarities	Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.

Ontologies

Keywords
Ligand	FAD Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro coenzyme F420 hydrogenase activity Inferred from electronic annotation. Source: EC ferredoxin hydrogenase activity Inferred from electronic annotation. Source: InterPro iron-sulfur cluster binding Inferred from electronic annotation. Source: InterPro nickel ion binding 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
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 405	404	Coenzyme F420 hydrogenase subunit alpha		PRO_0000199723
Sites
	Metal binding	63	1	Nickel Potential
	Metal binding	66	1	Nickel Potential
	Metal binding	380	1	Nickel Potential
	Metal binding	383	1	Nickel Potential

Sequences

	Sequence		Length	Mass (Da)
	P19496-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BB1C7C7F577CE1AB	FASTA	405	44,802
	10 20 30 40 50 60 MSERIVISPT SRQEGHAELV MEVDDEGIVT KGRYFSITPV RGLEKIVTGK APETAPVIVQ 70 80 90 100 110 120 RICGVCPIPH TLASVEAIDD SLDIEVPKAG RLLRELTLAA HHVNSHAIHH FLIAPDFVPE 130 140 150 160 170 180 NLMADAINSV SEIRKNAQYV VDMVAGEGIH PSDVRIGGMA DNITELARKR LYARLKQLKP 190 200 210 220 230 240 KVDEHVELMI GLIEDKGLPK GLGVHNQPTL ASHQIYGDRT KFDLDRFTEV MPESWYDDPE 250 260 270 280 290 300 IAKRACSTIP LYDGRNVEVG PRARMVEFQG FKERGVVAQH VARALEMKTA LARAIEILDE 310 320 330 340 350 360 LDTSAPVRAD FDERGTGKLG VGAIEGPRGL DVHMAQVENG KIQFYSALVP TTWNIPTMGP 370 380 390 400 ATEGFHHEYG PHVIRAYDPC LSCATHVMVV DDEDRSVIRD EMVRL

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: 2207102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: 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: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 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: 3663585] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-31. Strain: Delta H.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02914 Genomic DNA. Translation: AAA72187.1. AE000666 Genomic DNA. Translation: AAB85780.1. Different initiation.
PIR	A35620.
RefSeq	NP_276419.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P19496.
Genome annotation databases
GeneID	1471017.
GenomeReviews	Gene locus MTH_1300 in contig AE000666_GR.
KEGG	mth:MTH1300.
NMPDR	fig|187420.1.peg.1274.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P19496.
OMA	RHEGHSK
Enzyme and pathway databases
BioCyc	MTHE187420:MTH1300-MON.
BRENDA	1.12.98.1. 270.
Family and domain databases
InterPro	IPR017682. Coenz_F420_hydrogenase_asu. IPR001501. Ni-dep_hyd_lsu. IPR018194. Ni-dep_hyd_lsu_Ni_BS. [Graphical view]
Pfam	PF00374. NiFeSe_Hases. 1 hit. [Graphical view]
TIGRFAMs	TIGR03295. frhA. 1 hit.
PROSITE	PS00507. NI_HGENASE_L_1. 1 hit. PS00508. NI_HGENASE_L_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FRHA_METTH

Accession

Primary (citable) accession number: P19496

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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