ID   FRHG_METVO              Reviewed;         243 AA.
AC   Q00393;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Coenzyme F420 hydrogenase subunit gamma;
DE            EC=1.12.98.1;
DE   AltName: Full=8-hydroxy-5-deazaflavin-reducing hydrogenase subunit gamma;
DE            Short=FRH;
GN   Name=frhG; Synonyms=frcG;
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 FrhG family. {ECO:0000305}.
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DR   EMBL; X61201; CAA43498.1; -; Genomic_DNA.
DR   PIR; S16723; S16723.
DR   AlphaFoldDB; Q00393; -.
DR   SMR; Q00393; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050454; F:coenzyme F420 hydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   Gene3D; 3.40.50.700; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR017681; Coenz_F420_hydrogenase_gsu.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR03294; FrhG; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Repeat; Transport.
FT   CHAIN           1..243
FT                   /note="Coenzyme F420 hydrogenase subunit gamma"
FT                   /id="PRO_0000159234"
FT   DOMAIN          182..210
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          211..241
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         191
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   243 AA;  26040 MW;  8929559D9A0129AD CRC64;
     MVKIAHIHMS GCTGCLISLT DTYEKLLDIL GSVELVYALT LTGEKTEITE TDDKILIERD
     IPGGIDIALV EGSVCLDDHH SMDDILTTRK NSKKSLVALG ACAASGGVTR FRRVGQMSQP
     SHASFVPIGD VIKVDLALPG CPPSTESIVK LLTAALEGDM EYLEPFAEIA KYGKDACGCD
     VIKEVINKSL CMGCGTCAAA CQVNAIDMVE AKPNINSEFC IKCGICSAQC PRVRFPEIIR
     KLE