FRHG_METTH
ID FRHG_METTH Reviewed; 236 AA.
AC P19498; O27357;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 146.
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=MTH_1298;
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.
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 2-15.
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 FrhG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85778.1; Type=Erroneous initiation; Evidence={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; AAA72189.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85778.1; ALT_INIT; Genomic_DNA.
DR PIR; C35620; C35620.
DR AlphaFoldDB; P19498; -.
DR SMR; P19498; -.
DR IntAct; P19498; 1.
DR STRING; 187420.MTH_1298; -.
DR EnsemblBacteria; AAB85778; AAB85778; MTH_1298.
DR KEGG; mth:MTH_1298; -.
DR PATRIC; fig|187420.15.peg.1269; -.
DR HOGENOM; CLU_075477_0_0_2; -.
DR OMA; HESFVPI; -.
DR BRENDA; 1.12.98.1; 3256.
DR Proteomes; UP000005223; 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; 1.
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; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2207102,
FT ECO:0000269|PubMed:3663585"
FT CHAIN 2..236
FT /note="Coenzyme F420 hydrogenase subunit gamma"
FT /id="PRO_0000159233"
FT DOMAIN 172..200
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 201..230
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 181
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="H -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="A -> Q (in Ref. 1; AAA72189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 25817 MW; 47F9B17C5D98768D CRC64;
MAEENAKPRI GYIHLSGCTG DAMSLTENYD ILAELLTNMV DIVYGQTLVD LWEMPEMDLA
LVEGSVCLQD EHSLHELKEL REKAKLVCAF GSCAATGCFT RYSRGGQQAQ PSHESFVPIA
DLIDVDLAIP GCPPSPEIIA KAVVALLNND MEYLQPMLDL AGYTEACGCD LQTKVVNQGL
CTGCGTCAMA CQTRALDMTN GRPELNSDRC IKCGICYVQC PRSWWPEEQI KKELGL
