FPRA_METAZ
ID FPRA_METAZ Reviewed; 410 AA.
AC B1A7S3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Coenzyme F420H(2) oxidase {ECO:0000305};
DE EC=1.5.3.22 {ECO:0000269|PubMed:15340796};
DE AltName: Full=FMN protein FprA {ECO:0000305};
DE AltName: Full=Flavoprotein A {ECO:0000305};
DE AltName: Full=Type A flavoprotein FprA {ECO:0000305};
GN Name=fprA {ECO:0000303|PubMed:15340796};
OS Methanobrevibacter arboriphilus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=39441;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 744 / OCM 137 / AZ;
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).
CC -!- FUNCTION: Catalyzes the oxidation of F420H(2) with O(2). May be
CC involved in O(2) detoxification, reducing the intracellular O(2)
CC concentration to a level allowing growth at the expense of methane
CC formation. Cannot use NADH or NADPH as electron donor or H(2)O(2) as
CC electron acceptor. {ECO:0000269|PubMed:15340796}.
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};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:15340796};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:15340796};
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 -!- 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 37 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. 30% of maximal activity at pH 6.5 and 8.5.
CC {ECO:0000269|PubMed:15340796};
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; EU429441; ACA13278.1; -; Genomic_DNA.
DR KEGG; ag:ACA13278; -.
DR BRENDA; 1.5.3.22; 3259.
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 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; Transport.
FT CHAIN 1..410
FT /note="Coenzyme F420H(2) oxidase"
FT /id="PRO_0000454939"
FT DOMAIN 263..410
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 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 269..274
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 321..324
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
FT BINDING 356..361
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q50497"
SQ SEQUENCE 410 AA; 46060 MW; D38EEB7036518961 CRC64;
MKAQAKKIGN GVYWIGVLDW DLRTYHGYTL DGTSYNAYLI FGDDKVALID NAYPGKTEEL
MARVDDAFAQ EGKTGEECKV DVIIQNHVEK DHSGVLVDIH KRYPKAPIYC TEIAVKGLKR
HYPNIKEAEF ITVGTGDTLE LGGKTLAFLD AFLLHWPDSM FTLLVEEGIL FPNDAFGQHL
CYSKRFDHEI PEHVLMDATK KFYGNLIVPL SKLVLKKFEE VTELGLLEKI KMIAPSHGQI
WTDPMKVIGA YSEWATGKCK DKVTIVYDTM HYSTQKMAHE IAEGIMAEGY DVEMFFLHED
ERSEIVKSIL DSKAIAIGAP TINDEPYPSI GDLMYYLKGL RFERTGIKRK AVTFGSMGGK
GGTPASLGKD LGEYGFDVVD TCEVYYVPDE EENKACFKLG QKLVEEAKKI
