FPOO_METMA
ID FPOO_METMA Reviewed; 131 AA.
AC F1SVE1; Q7LWK2; Q9P9F2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=F(420)H(2) dehydrogenase subunit O;
DE EC=1.12.98.3;
DE AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit O;
DE AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit O;
DE Short=FPO subunit O;
DE AltName: Full=Methanophenazine hydrogenase subunit O;
DE AltName: Full=Methanosarcina-phenazine hydrogenase subunit O;
GN Name=fpoO; OrderedLocusNames=MM_2479;
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).
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. {ECO:0000269|PubMed:10751389,
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
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 Vmax=17 umol/min/mg enzyme (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|Ref.1};
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 -!- SIMILARITY: Belongs to the FpoO family. {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; AF228525; AAF65742.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM32175.1; -; Genomic_DNA.
DR RefSeq; WP_011034397.1; NC_003901.1.
DR AlphaFoldDB; F1SVE1; -.
DR STRING; 192952.MM_2479; -.
DR TCDB; 3.D.9.1.1; the h(+)-translocating f420h2 dehydrogenase (f420h2dh) family.
DR EnsemblBacteria; AAM32175; AAM32175; MM_2479.
DR GeneID; 24865360; -.
DR KEGG; mma:MM_2479; -.
DR PATRIC; fig|192952.21.peg.2837; -.
DR eggNOG; arCOG04959; Archaea.
DR HOGENOM; CLU_165880_0_0_2; -.
DR OMA; MTDCDLC; -.
DR BRENDA; 1.12.98.3; 3270.
DR Proteomes; UP000000595; Chromosome.
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; IPR018288; F420H2-DH_FpoO.
DR Pfam; PF10621; FpoO; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Methanogenesis; Methanol utilization; Oxidoreductase; Reference proteome;
KW Transport.
FT CHAIN 1..131
FT /note="F(420)H(2) dehydrogenase subunit O"
FT /id="PRO_0000423961"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
SQ SEQUENCE 131 AA; 15019 MW; 91F6FE52F2CF2E20 CRC64;
MTDCDLCGKG IPTVIPVRTY PPLLRFAYPE GVWKGLCETC LDSAQKTYLE VNRNHTSCRR
GKCSLCGSKT GVFSVELQIP DFSKGIVRKD VDVCYRCLKL VDEAYIRYKR EQIEQDHEQG
RIHGHEHVHP H
