FPOB_METMA
ID FPOB_METMA Reviewed; 184 AA.
AC F1SVH7; Q7LWJ5; Q9P9G2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=F(420)H(2) dehydrogenase subunit B;
DE EC=1.12.98.3;
DE AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit B;
DE AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit B;
DE Short=FPO subunit B;
DE AltName: Full=Methanophenazine hydrogenase subunit B;
DE AltName: Full=Methanosarcina-phenazine hydrogenase subunit B;
GN Name=fpoB; OrderedLocusNames=MM_2490;
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, COFACTOR, AND SUBSTRATE SPECIFICITY.
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], PROTEIN SEQUENCE, FUNCTION IN THE PROTON
RP TRANSLOCATION, SUBUNIT, COFACTOR, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
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 {ECO:0000269|PubMed:10751389}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AF228525; AAF65732.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM32186.1; -; Genomic_DNA.
DR RefSeq; WP_011034408.1; NC_003901.1.
DR AlphaFoldDB; F1SVH7; -.
DR SMR; F1SVH7; -.
DR STRING; 192952.MM_2490; -.
DR TCDB; 3.D.9.1.1; the h(+)-translocating f420h2 dehydrogenase (f420h2dh) family.
DR EnsemblBacteria; AAM32186; AAM32186; MM_2490.
DR GeneID; 44087882; -.
DR GeneID; 66135451; -.
DR KEGG; mma:MM_2490; -.
DR PATRIC; fig|192952.21.peg.2849; -.
DR eggNOG; arCOG01554; Archaea.
DR HOGENOM; CLU_055737_7_3_2; -.
DR OMA; AGWVRKS; -.
DR BioCyc; MetaCyc:MON-12224; -.
DR BRENDA; 1.12.98.3; 3270.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Methanogenesis; Methanol utilization; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..184
FT /note="F(420)H(2) dehydrogenase subunit B"
FT /id="PRO_0000423962"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 184 AA; 20732 MW; ECBA93704B27CF17 CRC64;
MGEVKETKTN NSKENPEEEV PGVITTTTSA IHNFLKKTKA QDIINWGRKN SLWFMTQPMG
CCGVEMIATG CAHYDTDRFG IIPRNSPRHA DVMIISGYVT KKYLPALKRL WDQMPAPKWV
IAMGDCAISG GPFYESYSTV QNIDEIFPID VYIPGCPPRP EALIQGFVEL QEKIKARKDR
GTEY
