FPOH_METAC
ID FPOH_METAC Reviewed; 348 AA.
AC Q8TQP1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=MA_1499;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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 (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; AE010299; AAM04913.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TQP1; -.
DR SMR; Q8TQP1; -.
DR STRING; 188937.MA_1499; -.
DR EnsemblBacteria; AAM04913; AAM04913; MA_1499.
DR KEGG; mac:MA_1499; -.
DR HOGENOM; CLU_015134_0_1_2; -.
DR InParanoid; Q8TQP1; -.
DR OMA; WSGWASN; -.
DR PhylomeDB; Q8TQP1; -.
DR Proteomes; UP000002487; 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:0009060; P:aerobic respiration; IBA:GO_Central.
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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..348
FT /note="F(420)H(2) dehydrogenase subunit H"
FT /id="PRO_0000240121"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 348 AA; 38522 MW; 74B93F24ECAB0A5B CRC64;
MNIMIEIPEF IIPLIPWIRG VVGLVLVGAI FLGAMGAVWL ERKLSADIQF RYGPSRVGKF
GLLQLVADAI KLFTKEDMRP RNADRLLFDN APIFMMSSVF LMLVAIPVGA VFINGVEYPL
AVTEMDISVL YIEAMSAITI FGIFMIAYGS NNKYSLLGAF RNFARMVGYE VPLGITVVSV
AIMTGSLNIV EIASAQGLLW NIFLQPIGFI VFFIALMADM GRLPFDQNES EEELVAGWIT
EYTGMRFGLG FFAEYIHMIL GSFLVALLFL GGWNVPAFVA NNPVLGLIAP TGFFLLKTVL
VLMTIIGMRW AVPRFRIDQV VDLSWKRLLP LSLLNLVWAV GLGLYLGA
