ID   Q2NES4_METST            Unreviewed;       406 AA.
AC   Q2NES4;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Coenzyme F420 hydrogenase subunit alpha {ECO:0000256|NCBIfam:TIGR03295};
DE            EC=1.12.98.1 {ECO:0000256|NCBIfam:TIGR03295};
GN   Name=frhA {ECO:0000313|EMBL:ABC57679.1};
GN   OrderedLocusNames=Msp_1302 {ECO:0000313|EMBL:ABC57679.1};
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC57679.1, ECO:0000313|Proteomes:UP000001931};
RN   [1] {ECO:0000313|EMBL:ABC57679.1, ECO:0000313|Proteomes:UP000001931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC   {ECO:0000313|Proteomes:UP000001931};
RX   PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000256|RuleBase:RU003896}.
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DR   EMBL; CP000102; ABC57679.1; -; Genomic_DNA.
DR   RefSeq; WP_011406878.1; NC_007681.1.
DR   AlphaFoldDB; Q2NES4; -.
DR   STRING; 339860.Msp_1302; -.
DR   GeneID; 3856135; -.
DR   GeneID; 41325872; -.
DR   KEGG; mst:Msp_1302; -.
DR   eggNOG; arCOG01549; Archaea.
DR   HOGENOM; CLU_044556_1_0_2; -.
DR   OrthoDB; 42371at2157; -.
DR   Proteomes; UP000001931; 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; Cytochrome-c3 Hydrogenase, chain B; 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   NCBIfam; TIGR03295; frhA; 1.
DR   PANTHER; PTHR43600:SF1; COENZYME F420 HYDROGENASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43600; COENZYME F420 HYDROGENASE, SUBUNIT ALPHA; 1.
DR   Pfam; PF27537; HoxH; 1.
DR   Pfam; PF00374; NiFeSe_Hases; 2.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601501-1,
KW   ECO:0000256|RuleBase:RU003896};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601501-1, ECO:0000256|RuleBase:RU003896};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003896};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001931}.
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         63
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         66
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         66
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         381
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         384
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         387
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   406 AA;  44981 MW;  1A231969814038D9 CRC64;
     MSETIVISPT SRQEGHAELS MEVDENGIVT TGRYFSITPV RGIEKMVIGK RPETAPVLVQ
     RICGVCPVTH TLASVEAIDD SLKIEVPQAG RILREMCLNA HMINSHAIHH FLVAPDFVPD
     NQYKEVVKNI STIRKNAQYV EDTVGGEGIH PSDIRIGGMA HNITKNTKNK IKTRISGMMK
     LLEEHVETMA GLIEDKDFPD KLGAHNQPVF ASDNTYGSKN NLSINEIEEI LPSSWYDLPD
     IGERACSQIP LYKGNVVETG PRARASKFRK FKEVGVKAQH LARAQEMINS AEKILELVDK
     LDTSAQVMAD YTLEGTNRLG VGVIEGPRGT NIHSAKISPE GYISYYNAIV PTTWNIPTMG
     LATEGFHHEY APHVIRAYDP CLSCATHMIV KDDETKEVLK DDMVQL
//