ID   FRHA_METBF              Reviewed;         456 AA.
AC   P80489; O33165; Q46FA8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 132.
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=Mbar_A0452;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9477253; DOI=10.1007/s002030050561;
RA   Vaupel M., Thauer R.K.;
RT   "Two F420-reducing hydrogenases in Methanosarcina barkeri.";
RL   Arch. Microbiol. 169:201-205(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-21.
RX   PubMed=8521835; DOI=10.1111/j.1432-1033.1995.727_3.x;
RA   Michel R., Massanz C., Kostka S., Richter M., Fiebig K.;
RT   "Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive
RT   hydrogenase from Methanosarcina barkeri Fusaro.";
RL   Eur. J. Biochem. 233:727-735(1995).
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: Pentamer of two alpha chains, two beta chains and a gamma
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; Y13763; CAA74090.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ69434.1; -; Genomic_DNA.
DR   PIR; S63483; S63483.
DR   RefSeq; WP_011305486.1; NC_007355.1.
DR   AlphaFoldDB; P80489; -.
DR   SMR; P80489; -.
DR   STRING; 269797.Mbar_A0452; -.
DR   EnsemblBacteria; AAZ69434; AAZ69434; Mbar_A0452.
DR   GeneID; 3624328; -.
DR   KEGG; mba:Mbar_A0452; -.
DR   eggNOG; arCOG01549; Archaea.
DR   HOGENOM; CLU_044556_1_0_2; -.
DR   OMA; MATDLIY; -.
DR   OrthoDB; 32760at2157; -.
DR   BioCyc; MetaCyc:MON-12647; -.
DR   BRENDA; 1.12.98.1; 3250.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Cell membrane; Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW   Metal-binding; Nickel; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8521835"
FT   CHAIN           2..456
FT                   /note="Coenzyme F420 hydrogenase subunit alpha"
FT                   /id="PRO_0000199721"
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         432
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         435
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   456 AA;  50769 MW;  EEFBD0E04511D667 CRC64;
     MTKVVEISPT TRLEGHSKLT LKVDDQGIVE RGDWLSITPV RGIEKLAIGK TMEQVPKIAS
     RVCGICPIAH TLASTEAMEA SIGCEIPTDA KLLRTILHAA NRIHSIALHN ILILPDFYIP
     GTEKKFNLFA NEQPARSVMA RIVRIREIAQ TIGAIAGGEA IHPSNPRIGG MYYNVSPRAK
     QKMADLAKEG LVLVHEQMEF MFDVIRNMQN REFVEVAGKQ IPLPKKLGYH NQGVMATASM
     YGSSSLDDNP TWDFTRWKET RPWDWYMGEV TIDLEDPSYP IGGTTKIGTK ANPQMEACTG
     VPTYDGQPVE VGPRARLATF KNFDEKGTFA QHIARQMEYP DCCYTILRCL DNLNTSGKVL
     ADHIPQGDGS MGWAANEAPR GSNIHLARVK DGKVLWYDML VPTTWNFPTC SRALTGAPWQ
     IAEMVVRAYD PCVSCATHMI VVNEEEKIVT QKLMQW