FRHG_METBF
ID FRHG_METBF Reviewed; 259 AA.
AC P80491; O33167; Q46FB0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
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; OrderedLocusNames=Mbar_A0450;
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 2-20.
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 FrhG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ69432.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y13763; CAA74092.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ69432.1; ALT_INIT; Genomic_DNA.
DR PIR; S63485; S63485.
DR AlphaFoldDB; P80491; -.
DR SMR; P80491; -.
DR STRING; 269797.Mbar_A0450; -.
DR EnsemblBacteria; AAZ69432; AAZ69432; Mbar_A0450.
DR KEGG; mba:Mbar_A0450; -.
DR eggNOG; arCOG02473; Archaea.
DR HOGENOM; CLU_075477_0_0_2; -.
DR BioCyc; MetaCyc:MON-12649; -.
DR BRENDA; 1.12.98.1; 3250.
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; 2.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR03294; FrhG; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8521835"
FT CHAIN 2..259
FT /note="Coenzyme F420 hydrogenase subunit gamma"
FT /id="PRO_0000159231"
FT DOMAIN 180..208
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 209..238
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 259 AA; 28241 MW; 46C4AE265B6146BF CRC64;
MTNKIKIGHV HMSGCTGCLV SLADNNLGLI KILDDYADLV YCLTLADVRH IPEMDVALVE
GSVCLQDHES VEDIKETRKK SKIVVALGSC ACYGNITRFS RGGQHNQPQH ESYLPIGDLI
DVDVYIPGCP PSPELIRNVA VMAYLLLEGN EEQKELAGKY LKPLMDLAKR GTSGCFCDLM
YDVINQGLCM GCGTCAASCP VHAITLEFGK PQGERDLCIK CGSCYGACPR SFFNLDVIPE
FENINEIIAN ALKEGESDD
