FPOM_METMA
ID FPOM_METMA Reviewed; 495 AA.
AC F1SVH9; Q7LWK0; Q9P9F4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=F(420)H(2) dehydrogenase subunit M;
DE EC=1.12.98.3;
DE AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit M;
DE AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit M;
DE Short=FPO subunit M;
DE AltName: Full=Methanophenazine hydrogenase subunit M;
DE AltName: Full=Methanosarcina-phenazine hydrogenase subunit M;
GN Name=fpoM; OrderedLocusNames=MM_2481;
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 4 family. {ECO:0000305}.
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DR EMBL; AE008384; AAM32177.1; -; Genomic_DNA.
DR EMBL; AF228525; AAF65740.1; -; Genomic_DNA.
DR RefSeq; WP_011034399.1; NC_003901.1.
DR AlphaFoldDB; F1SVH9; -.
DR SMR; F1SVH9; -.
DR STRING; 192952.MM_2481; -.
DR TCDB; 3.D.9.1.1; the h(+)-translocating f420h2 dehydrogenase (f420h2dh) family.
DR EnsemblBacteria; AAM32177; AAM32177; MM_2481.
DR GeneID; 44087873; -.
DR GeneID; 66135442; -.
DR KEGG; mma:MM_2481; -.
DR PATRIC; fig|192952.21.peg.2839; -.
DR eggNOG; arCOG01538; Archaea.
DR HOGENOM; CLU_007100_4_4_2; -.
DR OMA; ITRWGNQ; -.
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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 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..495
FT /note="F(420)H(2) dehydrogenase subunit M"
FT /id="PRO_0000423958"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 53973 MW; F288A37630CAFA00 CRC64;
MLPVASLLIL VPLIFAVVTF FTKTKQLAAG FGFLGSLATL GLTLYAYLNF DSSTAAMQFY
ESVSWIPFLG VNYSVGIDGV SMPLILLNAI VIPFMILFTW KEEMESPNRF YGLILTMQAA
VIGVFVALDF VVFYIFWELT LVPLFFIVNL WGGANRAHAS YKFFIYTHVA SLVMLLGIFG
LFYTALNQTG VPTFDIRELI AQFQFFEPGL MKDGIFLAIL FGFLAKLPAF PFHSWLPDAY
SEAPTAGSIL FILLKIGGYG LFRISLPMLP NTGSPQLMIM ILGLLGSVSI LYGALLALRQ
KDLKRMIAYS SLSHMGYVIL GSAGLVTLSV SGAMFQQFSH GLIMSIMFMS AGAIQTAAGT
RIINELGGLA KKMPMLTVAM MVGFMASLGL PGLTGFIAEF LVLTFTFTNL PVFVVIALLA
IVVTAGYHLW AMQRAMFGVY NEKLGDVRDI NSIQVFSMAV IALLVLYFGL NPSPVLDMMI
NNSEAIVSLA AGMGV
