FPOH_METMA
ID FPOH_METMA Reviewed; 350 AA.
AC Q8PU59; Q9P9F9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=F(420)H(2) dehydrogenase subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE EC=1.12.98.3;
DE AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit H;
DE AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit H;
DE Short=FPO subunit H;
DE AltName: Full=Methanophenazine hydrogenase subunit H;
DE AltName: Full=Methanosarcina-phenazine hydrogenase subunit H;
GN Name=fpoH {ECO:0000255|HAMAP-Rule:MF_01350}; OrderedLocusNames=MM_2487;
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: FPO complex is composed of at least 13 different subunits.
CC {ECO:0000269|PubMed:10751389}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01350};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF65735.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF228525; AAF65735.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE008384; AAM32183.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PU59; -.
DR SMR; Q8PU59; -.
DR STRING; 192952.MM_2487; -.
DR TCDB; 3.D.9.1.1; the h(+)-translocating f420h2 dehydrogenase (f420h2dh) family.
DR EnsemblBacteria; AAM32183; AAM32183; MM_2487.
DR KEGG; mma:MM_2487; -.
DR PATRIC; fig|192952.21.peg.2846; -.
DR eggNOG; arCOG01546; Archaea.
DR HOGENOM; CLU_015134_0_1_2; -.
DR OMA; WSGWASN; -.
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:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00667; COMPLEX1_ND1_1; 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..350
FT /note="F(420)H(2) dehydrogenase subunit H"
FT /id="PRO_0000240123"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 350 AA; 38443 MW; 21F9E161058612A6 CRC64;
MTFMAIEIPE FIVPFVPWIR GTVGLVLVGA IFLGGMAAVW IERKLSADIQ LRYGPSRVGK
FGLLQLVADA IKLFTKEDVR PGNADRFLYD NAPVFMLTSL FLMLVAIPVG AVFIDGNLYP
LAVTEMDISI LFIEAVSAIN IFGIFMAAYG SNNKYSLLGA FRNFARMIGY EVPLGIAIVS
VAVMTGSLNI IDITSAQGSF VWNIFLQPIG FVVFFIALMA DLGRLPFDQN ESEEELVAGW
VTEYTGMRFG LVFFAEYMHM ILGSFLVALL FLGGWNVPAF VANNAVLGLI APTGILLLKT
VLVLMTIIGM RWAVPRFRID QVVDMSWKKL LPLSLLNLAW AVGLGLYLGA
