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Database: UniProt
Entry: P80491
LinkDB: P80491
Original site: P80491 
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   10-APR-2019, entry version 119.
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.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   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
CC       acceptor coenzyme F420, and the artificial one-electron acceptor
CC       methylviologen.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2 + oxidized coenzyme F420-(gamma-Glu)(n) =
CC         reduced coenzyme F420-(gamma-Glu)(n); Xref=Rhea:RHEA:23760,
CC         Rhea:RHEA-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};
DR   EMBL; Y13763; CAA74092.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ69432.1; ALT_INIT; Genomic_DNA.
DR   PIR; S63485; S63485.
DR   ProteinModelPortal; 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   eggNOG; COG1941; LUCA.
DR   HOGENOM; HOG000236993; -.
DR   KO; K00443; -.
DR   BioCyc; MetaCyc:MONOMER-12649; -.
DR   BRENDA; 1.12.98.1; 3250.
DR   Proteomes; UP000008156; Chromosome.
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; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Repeat; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:8521835}.
FT   CHAIN         2    259       Coenzyme F420 hydrogenase subunit gamma.
FT                                /FTId=PRO_0000159231.
FT   DOMAIN      180    208       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      209    238       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       189    189       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       192    192       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       195    195       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       199    199       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       218    218       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       221    221       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       224    224       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       228    228       Iron-sulfur 1 (4Fe-4S). {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
//
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