FPRA_METJA
ID FPRA_METJA Reviewed; 416 AA.
AC Q58158;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
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;
DE AltName: Full=Type A flavoprotein FprA;
GN Name=fprA; OrderedLocusNames=MJ0748;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP DISCUSSION OF FUNCTION.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
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 -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {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; L77117; AAB98741.1; -; Genomic_DNA.
DR PIR; D64393; D64393.
DR RefSeq; WP_010870253.1; NC_000909.1.
DR AlphaFoldDB; Q58158; -.
DR SMR; Q58158; -.
DR STRING; 243232.MJ_0748; -.
DR EnsemblBacteria; AAB98741; AAB98741; MJ_0748.
DR GeneID; 1451625; -.
DR KEGG; mja:MJ_0748; -.
DR eggNOG; arCOG00509; Archaea.
DR HOGENOM; CLU_017490_0_0_2; -.
DR InParanoid; Q58158; -.
DR OMA; PEAPIYC; -.
DR OrthoDB; 72715at2157; -.
DR PhylomeDB; Q58158; -.
DR Proteomes; UP000000805; 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; IPR000014; PAS.
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 SMART; SM00091; PAS; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport; Flavoprotein; FMN; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..416
FT /note="Coenzyme F420H(2) oxidase"
FT /id="PRO_0000216809"
FT DOMAIN 266..407
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 272..277
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 324..327
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 359..364
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
SQ SEQUENCE 416 AA; 47380 MW; DA2C17F0647A2255 CRC64;
MKKYESRRSK IADGVYWVGV LDWDIRMYHG YTLKGTTYNA YLVFGDEKVA LIDNTYPGTS
AQMWGRIKDA FEKEGREFKI DVIVQNHVEK DHSGALPEIH KKFPDAPIYC TEVAVEGLKK
HYPSLKDAQF KVVHTGDTVD LGGKTLTFLE APLLHWPDSM FTFYNEGGIL FSNDAFGQHL
CFPAHKRFDK DIPEYVLMDA NQKFYANLIT PLSKLVLKKF EEVIQLGLLE KIKMIAPSHG
QIWTDPMKVI KAYQDFATGK AAKDKAVIVY DTMHYSTQKM AHAFAEGLMS EGIDVVMYFL
HYDERSEIVK DILDAKAVLF GIPTIYDEPY PSIGDIIYYL RGLKFNRTGF KRLAVTFGSM
GGEGGAVAKI AEDLAKCGFE VINQYELYYV PTEDELTNCY NMGKELAKRI KEMKIE
