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FPOJ_METMA
ID   FPOJ_METMA              Reviewed;         176 AA.
AC   Q8PU61; Q9P9F7;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=F(420)H(2) dehydrogenase subunit J;
DE            EC=1.12.98.3;
DE   AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit J;
DE   AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit J;
DE            Short=FPO subunit J;
DE   AltName: Full=Methanophenazine hydrogenase subunit J;
DE   AltName: Full=Methanosarcina-phenazine hydrogenase subunit J;
GN   Name=fpoJ; OrderedLocusNames=MM_2485;
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, SUBSTRATE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
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, 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   -!- 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       FpoA, FpoH, FpoJ, FpoK, FpoL, FpoM and FpoN proteins constitute the
CC       membrane sector of the complex. {ECO:0000269|PubMed:10751389}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM32181.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF228525; AAF65737.1; -; Genomic_DNA.
DR   EMBL; AE008384; AAM32181.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q8PU61; -.
DR   SMR; Q8PU61; -.
DR   STRING; 192952.MM_2485; -.
DR   TCDB; 3.D.9.1.1; the h(+)-translocating f420h2 dehydrogenase (f420h2dh) family.
DR   EnsemblBacteria; AAM32181; AAM32181; MM_2485.
DR   KEGG; mma:MM_2485; -.
DR   PATRIC; fig|192952.21.peg.2844; -.
DR   eggNOG; arCOG04654; Archaea.
DR   HOGENOM; CLU_170071_2_0_2; -.
DR   BRENDA; 1.12.98.3; 3270.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051911; F:Methanosarcina-phenazine hydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1200; -; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Electron transport; Membrane; Methanogenesis;
KW   Methanol utilization; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..176
FT                   /note="F(420)H(2) dehydrogenase subunit J"
FT                   /id="PRO_0000423955"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   176 AA;  18513 MW;  8B77B00F02A3F9A1 CRC64;
     MIDPGTVGAA LETAVFGLLA LVTVFFAIFV VIAKDVVRAG LALIMCMFGV AGLYILLNAQ
     FLGVIQVLVY IGAIGVLILF AVMLTKREIG GGPVQINRPL AFLVCLLFVA VVVTGAFGTS
     WNTVSELPEN PADPSNIEGI GMLIFTHFVA PFEVLSIVLL ASLIGAIYMA KGEGNR
 
 
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