FPRA_METTM
ID FPRA_METTM Reviewed; 404 AA.
AC Q50497; D9PYL0;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Coenzyme F420H(2) oxidase {ECO:0000305};
DE EC=1.5.3.22 {ECO:0000269|PubMed:15340796, ECO:0000269|PubMed:16218963};
DE AltName: Full=FMN protein FprA;
DE AltName: Full=Flavoprotein A {ECO:0000303|PubMed:7649162};
DE AltName: Full=Type A flavoprotein FprA;
GN Name=fprA {ECO:0000303|PubMed:7730275};
GN Synonyms=fpaA {ECO:0000303|PubMed:7649162}, fprA3;
GN OrderedLocusNames=MTBMA_c17400;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-31, COFACTOR,
RP SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=7730275; DOI=10.1128/jb.177.9.2436-2441.1995;
RA Wasserfallen A., Huber K., Leisinger T.;
RT "Purification and structural characterization of a flavoprotein induced by
RT iron limitation in Methanobacterium thermoautotrophicum Marburg.";
RL J. Bacteriol. 177:2436-2441(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [3]
RP PROTEIN SEQUENCE OF 1-22, COFACTOR, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
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 [4]
RP DISCUSSION OF FUNCTION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=15340796; DOI=10.1007/s00203-004-0675-3;
RA Seedorf H., Dreisbach A., Hedderich R., Shima S., Thauer R.K.;
RT "F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme
RT F420-dependent enzyme involved in O2 detoxification.";
RL Arch. Microbiol. 182:126-137(2004).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=16218963; DOI=10.1111/j.1742-4658.2005.04931.x;
RA Seedorf H., Kahnt J., Pierik A.J., Thauer R.K.;
RT "Si-face stereospecificity at C5 of coenzyme F420 for F420H2 oxidase from
RT methanogenic Archaea as determined by mass spectrometry.";
RL FEBS J. 272:5337-5342(2005).
RN [7] {ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI, ECO:0007744|PDB:2OHJ}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH FMN AND IRON,
RP REACTION MECHANISM, COFACTOR, SUBUNIT, AND DOMAIN.
RX PubMed=17480207; DOI=10.1111/j.1742-4658.2007.05706.x;
RA Seedorf H., Hagemeier C.H., Shima S., Thauer R.K., Warkentin E., Ermler U.;
RT "Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from
RT methanogenic Archaea catalyzing the reduction of O2 to H2O.";
RL FEBS J. 274:1588-1599(2007).
CC -!- FUNCTION: Catalyzes the oxidation of F420H(2) with O(2)
CC (PubMed:15340796, PubMed:16218963). May be involved in O(2)
CC detoxification, reducing the intracellular O(2) concentration to a
CC level allowing growth at the expense of methane formation
CC (PubMed:15340796). {ECO:0000269|PubMed:15340796,
CC ECO:0000269|PubMed:16218963}.
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:0000269|PubMed:15340796, ECO:0000269|PubMed:16218963};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:15340796, ECO:0000269|PubMed:17480207,
CC ECO:0000269|PubMed:7649162, ECO:0000269|PubMed:7730275};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:15340796,
CC ECO:0000269|PubMed:17480207, ECO:0000269|PubMed:7649162,
CC ECO:0000269|PubMed:7730275};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:15340796, ECO:0000269|PubMed:17480207};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:15340796,
CC ECO:0000269|PubMed:17480207};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for F420H(2) (at an O(2) concentration of 40 uM)
CC {ECO:0000269|PubMed:15340796};
CC KM=2 uM for O(2) (at a F420H(2) concentration of 30 uM)
CC {ECO:0000269|PubMed:15340796};
CC Vmax=240 umol/min/mg enzyme toward F420H(2) (at 65 degrees Celsius)
CC {ECO:0000269|PubMed:15340796};
CC Vmax=80 umol/min/mg enzyme toward O(2) {ECO:0000269|PubMed:15340796};
CC pH dependence:
CC Optimum pH is near 7.5. {ECO:0000269|PubMed:15340796};
CC -!- SUBUNIT: Homodimer (PubMed:7649162). Homotetramer (PubMed:7730275,
CC PubMed:17480207). The tetramer is composed of two functional dimers
CC (PubMed:17480207). {ECO:0000269|PubMed:17480207,
CC ECO:0000269|PubMed:7649162, ECO:0000269|PubMed:7730275}.
CC -!- INDUCTION: By iron limitation. {ECO:0000269|PubMed:7649162,
CC ECO:0000269|PubMed:7730275}.
CC -!- DOMAIN: Contains an N-terminal beta-lactamase-like domain harboring a
CC di-iron center, and a C-terminal flavodoxin-like domain containing FMN.
CC Two monomers assemble via a head-to-tail arrangement, such that the
CC beta-lactamase and the flavodoxin domains face each other, thereby
CC forming two separated and presumably independent active sites.
CC {ECO:0000269|PubMed:17480207}.
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; U17835; AAB88013.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL59308.1; -; Genomic_DNA.
DR RefSeq; WP_013296518.1; NC_014408.1.
DR PDB; 2OHH; X-ray; 1.70 A; A/B/D/E=1-404.
DR PDB; 2OHI; X-ray; 2.30 A; A/B/D/E/G/H/I/J=1-404.
DR PDB; 2OHJ; X-ray; 2.26 A; A/B/D/E=1-404.
DR PDBsum; 2OHH; -.
DR PDBsum; 2OHI; -.
DR PDBsum; 2OHJ; -.
DR AlphaFoldDB; Q50497; -.
DR SMR; Q50497; -.
DR STRING; 79929.MTBMA_c17400; -.
DR EnsemblBacteria; ADL59308; ADL59308; MTBMA_c17400.
DR GeneID; 9705451; -.
DR KEGG; mmg:MTBMA_c17400; -.
DR PATRIC; fig|79929.8.peg.1677; -.
DR HOGENOM; CLU_017490_0_0_2; -.
DR OMA; PEAPIYC; -.
DR OrthoDB; 72715at2157; -.
DR BioCyc; MetaCyc:MON-18960; -.
DR BRENDA; 1.5.3.22; 7427.
DR EvolutionaryTrace; Q50497; -.
DR Proteomes; UP000000345; 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; IPR001226; Flavodoxin_CS.
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; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Flavoprotein;
KW FMN; Iron; Metal-binding; Oxidoreductase; Transport.
FT CHAIN 1..404
FT /note="Coenzyme F420H(2) oxidase"
FT /id="PRO_0000216808"
FT DOMAIN 259..399
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI,
FT ECO:0007744|PDB:2OHJ"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI,
FT ECO:0007744|PDB:2OHJ"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI,
FT ECO:0007744|PDB:2OHJ"
FT BINDING 265..270
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI,
FT ECO:0007744|PDB:2OHJ"
FT BINDING 317..320
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI,
FT ECO:0007744|PDB:2OHJ"
FT BINDING 351..356
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17480207,
FT ECO:0007744|PDB:2OHH, ECO:0007744|PDB:2OHI,
FT ECO:0007744|PDB:2OHJ"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2OHH"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2OHH"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:2OHH"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:2OHH"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 344..355
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:2OHH"
FT STRAND 371..382
FT /evidence="ECO:0007829|PDB:2OHH"
FT HELIX 385..402
FT /evidence="ECO:0007829|PDB:2OHH"
SQ SEQUENCE 404 AA; 45205 MW; 155AF7D9FE9D75FD CRC64;
MKAAAKRISD GVYWTGVLDW DLRNYHGYTL QGTTYNAYLV CGDEGVALID NSYPGTFDEL
MARVEDALQQ VGMERVDYII QNHVEKDHSG VLVELHRRFP EAPIYCTEVA VKGLLKHYPS
LREAEFMTVK TGDVLDLGGK TLTFLETPLL HWPDSMFTLL DEDGILFSND AFGQHLCCPQ
RLDREIPEYI LMDAARKFYA NLITPLSKLV LKKFDEVKEL GLLERIQMIA PSHGQIWTDP
MKIIEAYTGW ATGMVDERVT VIYDTMHGST RKMAHAIAEG AMSEGVDVRV YCLHEDDRSE
IVKDILESGA IALGAPTIYD EPYPSVGDLL MYLRGLKFNR TLTRKALVFG SMGGNGGATG
TMKELLAEAG FDVACEEEVY YVPTGDELDA CFEAGRKLAA EIRR
