FPOF_METMA
ID FPOF_METMA Reviewed; 346 AA.
AC Q8PZ67; Q9P9F1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=F(420)H(2) dehydrogenase subunit F;
DE EC=1.12.98.3 {ECO:0000269|Ref.1};
DE EC=1.5.7.2 {ECO:0000269|PubMed:21306561};
DE AltName: Full=Coenzyme F420 oxidoreductase (ferredoxin);
DE AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit F;
DE AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit F;
DE Short=FPO subunit F;
DE AltName: Full=Methanophenazine hydrogenase subunit F;
DE AltName: Full=Methanosarcina-phenazine hydrogenase subunit F;
GN Name=fpoF; OrderedLocusNames=MM_0627;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RA Abken H.-J., Deppenmeier U.;
RT "Purification and properties of an F420H2 dehydrogenase from Methanosarcina
RT mazei Go1.";
RL FEMS Microbiol. Lett. 154:231-237(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN THE PROTON TRANSLOCATION,
RP SUBUNIT, COFACTOR, AND NOMENCLATURE.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=10751389; DOI=10.1074/jbc.m000650200;
RA Baumer S., Ide T., Jacobi C., Johann A., Gottschalk G., Deppenmeier U.;
RT "The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven
RT proton pump closely related to NADH dehydrogenases.";
RL J. Biol. Chem. 275:17968-17973(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21306561; DOI=10.1111/j.1742-4658.2011.08048.x;
RA Welte C., Deppenmeier U.;
RT "Re-evaluation of the function of the F420 dehydrogenase in electron
RT transport of Methanosarcina mazei.";
RL FEBS J. 278:1277-1287(2011).
CC -!- FUNCTION: Component of the F(420)H(2) dehydrogenase (FPO complex) which
CC is part of the energy-conserving F(420)H(2):heterodisulfide
CC oxidoreductase system. The membrane-bound electron transfer system of
CC the complex plays an important role in the metabolism of methylotrophic
CC methanogens when the organisms grow on methanol or methylamines.
CC Catalyzes the oxidation of methanophenazine to dihydromethanophenazine.
CC It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S)
CC centers, to methanophenazine (an electron carrier in the membrane). It
CC couples the redox reaction to proton translocation (for every two
CC electrons transferred, two hydrogen ions are translocated across the
CC cytoplasmic membrane), and thus conserves the redox energy in a proton
CC gradient. It also catalyzes the oxidation of F(420)H(2) with quinones
CC such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone
CC and tetramethyl-p-benzoquinone. Might have a dual function, acting as
CC an electron input module when connected to the membrane integral Fpo
CC complex, or as a soluble single subunit, being involved in the
CC reoxydation of reduced ferredoxin in the cytoplasm (PubMed:21306561).
CC {ECO:0000269|PubMed:10751389, ECO:0000269|PubMed:21306561,
CC ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + methanophenazine = dihydromethanophenazine;
CC Xref=Rhea:RHEA:24436, ChEBI:CHEBI:18276, ChEBI:CHEBI:29118,
CC ChEBI:CHEBI:50375; EC=1.12.98.3; Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 oxidized [2Fe-2S]-[ferredoxin] + reduced coenzyme F420-
CC (gamma-L-Glu)(n) = 3 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) +
CC 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:42324, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:12939, Rhea:RHEA-
CC COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.7.2;
CC Evidence={ECO:0000269|PubMed:21306561};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:21306561};
CC Note=Binds 2 [4Fe-4S] cluster. {ECO:0000269|PubMed:21306561};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:21306561};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for F(420)H(2) (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|Ref.1};
CC KM=2 uM for oxidized F(420) {ECO:0000269|PubMed:21306561};
CC KM=0.5 uM for reduced ferredoxin {ECO:0000269|PubMed:21306561};
CC Vmax=17 umol/min/mg enzyme (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|Ref.1};
CC Vmax=0.225 umol/min/mg enzyme with ferredoxin as substrate
CC {ECO:0000269|PubMed:21306561};
CC Note=Measured for the whole complex.;
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 39 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: The FPO complex is composed of at least 13 different subunits.
CC {ECO:0000269|PubMed:10751389}.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:21306561}. Cytoplasm {ECO:0000269|PubMed:21306561}.
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DR EMBL; AF228526; AAF65743.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM30323.1; -; Genomic_DNA.
DR RefSeq; WP_011032578.1; NC_003901.1.
DR AlphaFoldDB; Q8PZ67; -.
DR SMR; Q8PZ67; -.
DR STRING; 192952.MM_0627; -.
DR TCDB; 3.D.9.1.1; the h(+)-translocating f420h2 dehydrogenase (f420h2dh) family.
DR EnsemblBacteria; AAM30323; AAM30323; MM_0627.
DR GeneID; 44086160; -.
DR KEGG; mma:MM_0627; -.
DR PATRIC; fig|192952.21.peg.739; -.
DR eggNOG; arCOG02650; Archaea.
DR HOGENOM; CLU_037958_0_0_2; -.
DR OMA; GVPCQAH; -.
DR BioCyc; MetaCyc:MON-12227; -.
DR BRENDA; 1.12.98.3; 3270.
DR BRENDA; 1.5.7.2; 3270.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051911; F:Methanosarcina-phenazine hydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N.
DR InterPro; IPR045220; FRHB/FDHB/HCAR-like.
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 PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Methanogenesis; Methanol utilization;
KW Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..346
FT /note="F(420)H(2) dehydrogenase subunit F"
FT /id="PRO_0000423960"
FT DOMAIN 5..34
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 46..76
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT CONFLICT 251
FT /note="A -> E (in Ref. 2; AAF65743)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="C -> S (in Ref. 2; AAF65743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38359 MW; 07E213442D9D2E56 CRC64;
MPPKIAEVIQ HDVCAACGAC EAVCPIGAVT VKKAAEIRDP NDLSLYEKGA AFQVCEGCLT
CSRICPVVDG FIENELLNVR KFFGAKSKDN AGSQDGGVTS GILKALFNKG EIDCAVGITR
NENWEPEVVL LTSAEDVERT RGTKYTSDPV VAALREAFEK YDRIAVVGVP CQAHAARLIR
ENVNEKIVLI IGLLCMESFH HDVMLDKIIP EIMKVNVRDI VKMEFTKGKF WVYTKDGEVH
SVPIKDIAKY ARNPCHHCCD YTSVFADISV GSVGAPDGWN SVFIRTEIGE KYFDMVRDEM
EIMEDPKPGL ELVGKLIEMK RKGNAEHFQE VCKEFSFETG IRSETV
