FRHA_METTH
ID FRHA_METTH Reviewed; 405 AA.
AC P19496;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Coenzyme F420 hydrogenase subunit alpha;
DE EC=1.12.98.1;
DE AltName: Full=8-hydroxy-5-deazaflavin-reducing hydrogenase subunit alpha;
DE Short=FRH;
GN Name=frhA; OrderedLocusNames=MTH_1300;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=2207102; DOI=10.1021/bi00483a011;
RA Alex L.A., Reeve J.N., Orme-Johnson W.H., Walsh C.T.;
RT "Cloning, sequence determination, and expression of the genes encoding the
RT subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing
RT hydrogenase from Methanobacterium thermoautotrophicum delta H.";
RL Biochemistry 29:7237-7244(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-31.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=3663585; DOI=10.1021/bi00388a007;
RA Fox J.A., Livingston D.J., Orme-Johnson W.H., Walsh C.T.;
RT "8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium
RT thermoautotrophicum: 1. Purification and characterization.";
RL Biochemistry 26:4219-4227(1987).
CC -!- FUNCTION: Reduces the physiological low-potential two-electron acceptor
CC coenzyme F420, and the artificial one-electron acceptor methylviologen.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced
CC coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:23760, Rhea:RHEA-
CC COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18276, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC EC=1.12.98.1;
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC -!- COFACTOR:
CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC Note=There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the
CC FRH.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Heterocomplex of the form (alpha(1)beta(1)gamma(1))(8).
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J02914; AAA72187.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85780.1; ALT_INIT; Genomic_DNA.
DR PIR; A35620; A35620.
DR RefSeq; WP_048061018.1; NC_000916.1.
DR AlphaFoldDB; P19496; -.
DR SMR; P19496; -.
DR IntAct; P19496; 2.
DR STRING; 187420.MTH_1300; -.
DR EnsemblBacteria; AAB85780; AAB85780; MTH_1300.
DR GeneID; 1471017; -.
DR KEGG; mth:MTH_1300; -.
DR PATRIC; fig|187420.15.peg.1271; -.
DR HOGENOM; CLU_044556_1_0_2; -.
DR OMA; FMPDFTR; -.
DR BRENDA; 1.12.98.1; 3256.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0050454; F:coenzyme F420 hydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; -; 1.
DR InterPro; IPR017682; Coenz_F420_hydrogenase_asu.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR Pfam; PF00374; NiFeSe_Hases; 2.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR03295; frhA; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Metal-binding; Nickel;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3663585"
FT CHAIN 2..405
FT /note="Coenzyme F420 hydrogenase subunit alpha"
FT /id="PRO_0000199723"
FT BINDING 63
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 380
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 383
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 44802 MW; BB1C7C7F577CE1AB CRC64;
MSERIVISPT SRQEGHAELV MEVDDEGIVT KGRYFSITPV RGLEKIVTGK APETAPVIVQ
RICGVCPIPH TLASVEAIDD SLDIEVPKAG RLLRELTLAA HHVNSHAIHH FLIAPDFVPE
NLMADAINSV SEIRKNAQYV VDMVAGEGIH PSDVRIGGMA DNITELARKR LYARLKQLKP
KVDEHVELMI GLIEDKGLPK GLGVHNQPTL ASHQIYGDRT KFDLDRFTEV MPESWYDDPE
IAKRACSTIP LYDGRNVEVG PRARMVEFQG FKERGVVAQH VARALEMKTA LARAIEILDE
LDTSAPVRAD FDERGTGKLG VGAIEGPRGL DVHMAQVENG KIQFYSALVP TTWNIPTMGP
ATEGFHHEYG PHVIRAYDPC LSCATHVMVV DDEDRSVIRD EMVRL
