ID   FRHA_METJA              Reviewed;         415 AA.
AC   Q60338;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=MJ0029;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Reduces the physiological low-potential two-electron acceptor
CC       coenzyme F420, and the artificial one-electron acceptor methylviologen.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC         Evidence={ECO:0000250};
CC       Note=There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the
CC       FRH. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterocomplex of the form (alpha(1)beta(1)gamma(1))(8).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A64299; A64299.
DR   AlphaFoldDB; Q60338; -.
DR   SMR; Q60338; -.
DR   InParanoid; Q60338; -.
DR   OMA; HGIASCE; -.
DR   PhylomeDB; Q60338; -.
DR   Proteomes; UP000000805; 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; 1.
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;
KW   Reference proteome.
FT   CHAIN           1..415
FT                   /note="Coenzyme F420 hydrogenase subunit alpha"
FT                   /id="PRO_0000199722"
FT   BINDING         68
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         71
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         391
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         394
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   415 AA;  46784 MW;  8DD9A94CBABE35C4 CRC64;
     MEVNFVTNRI EIAPTTRHEG HAKLILEVDE EGIVNKAYYL NTTPVRGFET MLKGKPAEFA
     PIAVMRICGI CQTTHGIASC EAIENAIDCE VPDDGLLLRE LVGIGNRLHS HPLHHLLTID
     DFLKPDETDL KIELIKLIQR MRKVGQLVVD IVGGEGIHPP NIVIGGMRTN ITERAKSRLY
     YALRQYEKDA YELYEKYTEL IERYLEEIGI PDLGAHEYPY IATHTTYGDR YAINWDDVTE
     IPAQRYYDDE EAKQTTTIQI PLYAGVPAEG GPRARMVKFG NFREGGSAMD INIARAQENL
     GAVYRALEIL DELDLNGKTR AEVEYKDGFG IGVHEAPRAT NTHMAEVGKD GKIKSYRIIA
     ASTWNFPIVE KAIEGYPQQY AEVIMRAYDI CASCATHVIV KDEETKEIIE VRKML