ID   FRHB_METTH              Reviewed;         281 AA.
AC   P19499; O27356;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Coenzyme F420 hydrogenase subunit beta;
DE            EC=1.12.98.1;
DE   AltName: Full=8-hydroxy-5-deazaflavin-reducing hydrogenase subunit beta;
DE            Short=FRH;
GN   Name=frhB; OrderedLocusNames=MTH_1297;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31 AND
RP   185-201.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=2207102; DOI=10.1021/bi00483a011;
RA   Alex L.A., Reeve J.N., Orme-Johnson W.H., Walsh C.T.;
RT   "Cloning, sequence determination, and expression of the genes encoding the
RT   subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing
RT   hydrogenase from Methanobacterium thermoautotrophicum delta H.";
RL   Biochemistry 29:7237-7244(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-32.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=3663585; DOI=10.1021/bi00388a007;
RA   Fox J.A., Livingston D.J., Orme-Johnson W.H., Walsh C.T.;
RT   "8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium
RT   thermoautotrophicum: 1. Purification and characterization.";
RL   Biochemistry 26:4219-4227(1987).
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       Note=There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBUNIT: Heterocomplex of the form (alpha(1)beta(1)gamma(1))(8).
CC   -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J02914; AAA72190.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB85777.1; -; Genomic_DNA.
DR   PIR; D35620; D35620.
DR   RefSeq; WP_010876912.1; NC_000916.1.
DR   AlphaFoldDB; P19499; -.
DR   SMR; P19499; -.
DR   IntAct; P19499; 1.
DR   STRING; 187420.MTH_1297; -.
DR   EnsemblBacteria; AAB85777; AAB85777; MTH_1297.
DR   GeneID; 1471014; -.
DR   KEGG; mth:MTH_1297; -.
DR   PATRIC; fig|187420.15.peg.1268; -.
DR   HOGENOM; CLU_037958_0_0_2; -.
DR   OMA; REYGCEK; -.
DR   BRENDA; 1.12.98.1; 3256.
DR   Proteomes; UP000005223; Chromosome.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N.
DR   InterPro; IPR045220; FRHB/FDHB/HCAR-like.
DR   InterPro; IPR017679; FrhB_archaea.
DR   InterPro; IPR007525; FrhB_FdhB_C.
DR   PANTHER; PTHR31332; PTHR31332; 1.
DR   Pfam; PF04432; FrhB_FdhB_C; 1.
DR   Pfam; PF04422; FrhB_FdhB_N; 1.
DR   TIGRFAMs; TIGR03289; frhB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2207102,
FT                   ECO:0000269|PubMed:3663585"
FT   CHAIN           2..281
FT                   /note="Coenzyme F420 hydrogenase subunit beta"
FT                   /id="PRO_0000159229"
FT   CONFLICT        4
FT                   /note="G -> C (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="L -> F (in Ref. 1; AAA72190)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  30771 MW;  350DCEE9029C09E1 CRC64;
     MVLGTYKEIV SARSTDREIQ KLAQDGGIVT GLLAYALDEG IIEGAVVAGP GKEFWKPEPM
     VAMTSDELKA AAGTKYTFSP NVLMLKKAVR QYGIEKLGTV AIPCQTMGIR KAQTYPFGVR
     FVADKIKLLV GIYCMENFPY TSLQTFICEK LGLNMELVEK MDIGKGKFWV YTQDDVYTLP
     LKETHGYEQA GCKICKDYVA ELADVSTGSV GSPDGWSTVI TRTDSGDSIL KQAVEAGIFE
     TKPIEEVKPG LGLLEKLSAQ KKEKAEKNIA ARKEMGLPTP Y