FRHB_METBF
ID FRHB_METBF Reviewed; 291 AA.
AC P80490; O33168; Q46FB1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=Mbar_A0449;
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 1-25.
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 -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}.
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DR EMBL; Y13763; CAA74093.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ69431.1; -; Genomic_DNA.
DR PIR; S63484; S63484.
DR RefSeq; WP_011305483.1; NC_007355.1.
DR AlphaFoldDB; P80490; -.
DR SMR; P80490; -.
DR STRING; 269797.Mbar_A0449; -.
DR EnsemblBacteria; AAZ69431; AAZ69431; Mbar_A0449.
DR GeneID; 3624325; -.
DR KEGG; mba:Mbar_A0449; -.
DR eggNOG; arCOG02651; Archaea.
DR HOGENOM; CLU_037958_0_0_2; -.
DR OMA; REYGCEK; -.
DR OrthoDB; 49654at2157; -.
DR BioCyc; MetaCyc:MON-12648; -.
DR BRENDA; 1.12.98.1; 3250.
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.
FT CHAIN 1..291
FT /note="Coenzyme F420 hydrogenase subunit beta"
FT /id="PRO_0000159225"
SQ SEQUENCE 291 AA; 32281 MW; 4061CC460D39EC63 CRC64;
MIEDPYLGKY VTCVSARSTD KEILKKAQDG GIATALMVYA LEEGFIDGTI VAGEGDKPWQ
PKPEVAMTRE EILKARGTRY SISPQISWLK EATRSFGLDK VGVTGVCCQM QAVRKAQLYP
INMRDVPGKV AFTVGLFCME NFPYKSLQSI VEDHANQSLG SVKKMEITKG KFWVYTERGN
VATVPLKATH KYEQPGCHVC LDYVSNLADI STGSVGSPDG WSTVFIRTKV GNEIWSKAVA
DGMFETKPIE EVKPGLDLLR KLAKEKIEKN QKTVEERKTF GVNKGLRNPY A