FPRA_METTH
ID FPRA_METTH Reviewed; 404 AA.
AC O27404; Q50531;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Coenzyme F420H(2) oxidase {ECO:0000305};
DE EC=1.5.3.22 {ECO:0000250|UniProtKB:Q50497};
DE AltName: Full=FMN protein FprA;
DE AltName: Full=Flavoprotein A {ECO:0000303|PubMed:7649162};
DE AltName: Full=Type A flavoprotein FprA;
GN Name=fpaA {ECO:0000303|PubMed:7649162}; Synonyms=fprA;
GN OrderedLocusNames=MTH_1350;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, AND INDUCTION.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=7649162; DOI=10.1111/j.1432-1033.1995.0628d.x;
RA Noelling J., Ishii M., Koch J., Pihl T.D., Reeve J.N., Thauer R.K.,
RA Hedderich R.;
RT "Characterization of a 45-kDa flavoprotein and evidence for a rubredoxin,
RT two proteins that could participate in electron transport from H2 to CO2 in
RT methanogenesis in Methanobacterium thermoautotrophicum.";
RL Eur. J. Biochem. 231:628-638(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [3]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=8376343; DOI=10.1128/jb.175.18.5970-5977.1993;
RA Woo G.-J., Wasserfallen A., Wolfe R.S.;
RT "Methyl viologen hydrogenase II, a new member of the hydrogenase family
RT from Methanobacterium thermoautotrophicum delta H.";
RL J. Bacteriol. 175:5970-5977(1993).
RN [4]
RP DISCUSSION OF FUNCTION.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9660187; DOI=10.1046/j.1432-1327.1998.2540325.x;
RA Wasserfallen A., Ragettli S., Jouanneau Y., Leisinger T.;
RT "A family of flavoproteins in the domains Archaea and Bacteria.";
RL Eur. J. Biochem. 254:325-332(1998).
CC -!- FUNCTION: Catalyzes the oxidation of F420H(2) with O(2) (By
CC similarity). May be involved in O(2) detoxification, reducing the
CC intracellular O(2) concentration to a level allowing growth at the
CC expense of methane formation (By similarity).
CC {ECO:0000250|UniProtKB:Q50497}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + 2 H2O
CC + 2 oxidized coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:39711,
CC Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:133980,
CC ChEBI:CHEBI:139511; EC=1.5.3.22;
CC Evidence={ECO:0000250|UniProtKB:Q50497};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q50497};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q50497};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q50497};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q50497};
CC -!- INDUCTION: By iron limitation. {ECO:0000269|PubMed:7649162}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a subunit of methylviologen
CC hydrolase II. {ECO:0000305|PubMed:8376343}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85827.1; Type=Erroneous initiation; 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; U21086; AAB53659.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85827.1; ALT_INIT; Genomic_DNA.
DR PIR; S66533; S66533.
DR RefSeq; WP_048061030.1; NC_000916.1.
DR AlphaFoldDB; O27404; -.
DR SMR; O27404; -.
DR STRING; 187420.MTH_1350; -.
DR EnsemblBacteria; AAB85827; AAB85827; MTH_1350.
DR GeneID; 1471067; -.
DR KEGG; mth:MTH_1350; -.
DR PATRIC; fig|187420.15.peg.1315; -.
DR HOGENOM; CLU_017490_0_0_2; -.
DR OMA; PEAPIYC; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005243; ROO; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Flavoprotein; FMN; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..404
FT /note="Coenzyme F420H(2) oxidase"
FT /id="PRO_0000216807"
FT DOMAIN 259..399
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 84
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 152
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 265..270
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 317..320
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 351..356
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT CONFLICT 20
FT /note="W -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="T -> A (in Ref. 1; AAB53659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 45460 MW; 8D3F3AEEDB0594B9 CRC64;
MKARAEKIAD GLYWTGVLDW DIRNYHGYTL QGTTYNAYLV FGDEGVALID NSYPGTFQEL
MARMEDAFNR EGREMRVDFI VQNHVERDHS GVLVELHRRF PEAEIHCTEV AVEGLLKHYP
ALEGTEFRTV KTGDSIDLGG RTLTFLEAPL LHWPDSMFTF LDTGILFSND AFGQHLCYPQ
RLDTEIPEYI LMDAAKKFYA NLITPLSKLV LRKFDEVKEL GLLDKIGMIA PSHGQIWTEP
MKIIEAYTAW ATGKVKKKVT VIYDTMHHST AMMAHAIAEG AMSEGADVRV YYLHEDDRSE
IVKDILDSHA IALGAPAIYD EPYPSVGDLL MYLRGLKFNR TGQRRAMVFG SMGGRGGATG
TMQKLLADAG FDVMEADEIY YVPNNEELDA CFEAGRRLAG DLNE
