ID   FRHA_METVO              Reviewed;         398 AA.
AC   Q00390;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
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; Synonyms=frcA;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=1603063; DOI=10.1007/bf00587582;
RA   Halboth S., Klein A.;
RT   "Methanococcus voltae harbors four gene clusters potentially encoding two
RT   [NiFe] and two [NiFeSe] hydrogenases, each of the cofactor F420-reducing or
RT   F420-non-reducing types.";
RL   Mol. Gen. Genet. 233:217-224(1992).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBUNIT: Complex of alpha, beta and gamma subunits.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; X61201; CAA43496.1; -; Genomic_DNA.
DR   PIR; S16721; S16721.
DR   AlphaFoldDB; Q00390; -.
DR   SMR; Q00390; -.
DR   PRIDE; Q00390; -.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Metal-binding; Nickel; Oxidoreductase.
FT   CHAIN           1..398
FT                   /note="Coenzyme F420 hydrogenase subunit alpha"
FT                   /id="PRO_0000199724"
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         386
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         389
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   398 AA;  44612 MW;  696C95DD94C4EE83 CRC64;
     MGKTVEINPT TRHEGHTKLV LKVDDDGIVE KGNYLSVTPV RGFEKFLVGK PAEFAPIAVS
     RFCGICPIAH ATSAVEAIED ACGIVPPKDG LLLRELTGLG NKMHSHPLHE FLIAPDFIPE
     KDRVEYITRI QQMRKTGQYI VDTIGGEAIH APNIKVGGML KSITPSAVSK IYYKCKEFEK
     LAKEQVEYLI PIFENRTLVD GTEIPEKLGY HDFGYLATDS TYGNRENIEQ KKVHEYTPYD
     VYEKEVAVQA CQLFQEYNGR LMEVGPRARF AKFHDFKEKG AMAIHIARAY ENVIHVKRAM
     EIIEELNVDG LTRAKDPILG DGEKLGLGVH EAARGHNTHQ ASIDEKGRIT YYNAIVATTW
     NIPLIGKAVE AHYKFAEHVV RAYDPCVSCA TQHDILRL