FPOH_METBF
ID FPOH_METBF Reviewed; 346 AA.
AC Q466B1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=Mbar_A3408;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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 (By similarity). {ECO:0000250}.
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;
CC -!- SUBUNIT: FPO complex is composed of at least 13 different subunits.
CC FpoAHJKLMN proteins constitute the membrane sector of the complex (By
CC similarity). {ECO:0000250}.
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}.
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DR EMBL; CP000099; AAZ72281.1; -; Genomic_DNA.
DR RefSeq; WP_011308320.1; NC_007355.1.
DR AlphaFoldDB; Q466B1; -.
DR SMR; Q466B1; -.
DR STRING; 269797.Mbar_A3408; -.
DR EnsemblBacteria; AAZ72281; AAZ72281; Mbar_A3408.
DR GeneID; 3624655; -.
DR KEGG; mba:Mbar_A3408; -.
DR eggNOG; arCOG01546; Archaea.
DR HOGENOM; CLU_015134_0_1_2; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 88886at2157; -.
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 3: Inferred from homology;
KW Cell membrane; Electron transport; Membrane; Methanogenesis;
KW Methanol utilization; Oxidoreductase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..346
FT /note="F(420)H(2) dehydrogenase subunit H"
FT /id="PRO_0000240122"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 346 AA; 38027 MW; E8F183F644315504 CRC64;
MTVVIPEYIT PLIPWVRGIV GLVLIGVIFM GAMGAVWLER KLSADIQTRM GPCRVGKYGL
LQLVADAIKL FTKEDLKPLN ADSLLFNNAN IFMLGSVFLM LVALPVGAVF INGVEYPLAV
TQMDISVLYI EAVSALSIFG IFMVAYGSNN KYSLLGAFRN FARMVGYEVP LGITVISVAA
MTGSLNIVDI STAQGLHWNI FLQPLGCFVF FVSLMADMGR LPFDQNESEE ELIAGWITEY
CGMRFGLGFF AEYIHMILGS FLVALLFLGG WNVPGFIANN SFFGIIVPTG FLIVKVVFVL
MVIIGLRWAV PRFRIDQVVD LSWKKLLPLA LLNLVWAVGL GLYLGA
