FPRA2_CLOAB
ID FPRA2_CLOAB Reviewed; 400 AA.
AC Q97GC0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Flavo-diiron protein FprA2;
DE Short=FDP 2;
DE AltName: Full=Flavoprotein A2;
DE AltName: Full=H(2)O-forming NADH oxidase;
DE EC=1.6.3.4 {ECO:0000269|PubMed:19084524, ECO:0000269|PubMed:19124587};
DE AltName: Full=NADH oxidase;
DE AltName: Full=NADH:O(2) oxidoreductase;
GN Name=fprA2; OrderedLocusNames=CA_C2449;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, FMN COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19124587; DOI=10.1128/aem.01425-08;
RA Kawasaki S., Sakai Y., Takahashi T., Suzuki I., Niimura Y.;
RT "O2 and reactive oxygen species detoxification complex, composed of O2-
RT responsive NADH:rubredoxin oxidoreductase-flavoprotein A2-desulfoferrodoxin
RT operon enzymes, rubperoxin, and rubredoxin, in Clostridium
RT acetobutylicum.";
RL Appl. Environ. Microbiol. 75:1021-1029(2009).
RN [3]
RP INDUCTION BY O(2).
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=16332833; DOI=10.1128/aem.71.12.8442-8450.2005;
RA Kawasaki S., Watamura Y., Ono M., Watanabe T., Takeda K., Niimura Y.;
RT "Adaptive responses to oxygen stress in obligatory anaerobes Clostridium
RT acetobutylicum and Clostridium aminovalericum.";
RL Appl. Environ. Microbiol. 71:8442-8450(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, KINETIC PARAMETERS, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19084524; DOI=10.1016/j.febslet.2008.12.004;
RA Hillmann F., Riebe O., Fischer R.J., Mot A., Caranto J.D., Kurtz D.M. Jr.,
RA Bahl H.;
RT "Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium
RT acetobutylicum.";
RL FEBS Lett. 583:241-245(2009).
RN [5]
RP INDUCTION BY O(2), AND REPRESSION BY PERR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19648241; DOI=10.1128/jb.00351-09;
RA Hillmann F., Doring C., Riebe O., Ehrenreich A., Fischer R.J., Bahl H.;
RT "The role of PerR in O2-affected gene expression of Clostridium
RT acetobutylicum.";
RL J. Bacteriol. 191:6082-6093(2009).
CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to
CC water. In fact, functions as the terminal component of an NADH oxidase
CC (NADH:O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase
CC (NROR) and rubredoxin (Rd) as electron transport intermediaries between
CC NADH and FDP. Is thus able to reductively scavenge intracellular
CC dioxygen and is part of an oxidative stress defense system in
CC C.acetobutylicum, an obligate anaerobic bacterium. Can also serve as
CC the terminal component of an NADH:nitric oxide oxidoreductase (NOR)
CC with a catalytic efficiency comparable to that of its NADH oxidase
CC activity, and therefore might have an in vivo role in scavenging nitric
CC oxide. {ECO:0000269|PubMed:19084524, ECO:0000269|PubMed:19124587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+); Xref=Rhea:RHEA:37799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.4;
CC Evidence={ECO:0000269|PubMed:19084524, ECO:0000269|PubMed:19124587};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:19084524};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:19084524};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:19084524};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:19084524};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for O(2) {ECO:0000269|PubMed:19084524};
CC KM=40 uM for NO {ECO:0000269|PubMed:19084524};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19084524,
CC ECO:0000269|PubMed:19124587}.
CC -!- INDUCTION: Up-regulated upon exposure to O(2). Repressed by PerR.
CC {ECO:0000269|PubMed:16332833, ECO:0000269|PubMed:19648241}.
CC -!- DOMAIN: Consists of an N-terminal non-heme diiron domain and a C-
CC terminal flavodoxin-like domain.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
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DR EMBL; AE001437; AAK80403.1; -; Genomic_DNA.
DR PIR; H97201; H97201.
DR RefSeq; NP_349063.1; NC_003030.1.
DR RefSeq; WP_010965744.1; NC_003030.1.
DR AlphaFoldDB; Q97GC0; -.
DR SMR; Q97GC0; -.
DR STRING; 272562.CA_C2449; -.
DR EnsemblBacteria; AAK80403; AAK80403; CA_C2449.
DR GeneID; 44998927; -.
DR KEGG; cac:CA_C2449; -.
DR PATRIC; fig|272562.8.peg.2645; -.
DR eggNOG; COG0426; Bacteria.
DR HOGENOM; CLU_017490_2_1_9; -.
DR OMA; YIIVSHT; -.
DR OrthoDB; 1149616at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016966; F:nitric oxide reductase activity; IDA:UniProtKB.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; 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 Detoxification; Direct protein sequencing; Electron transport;
KW Flavoprotein; FMN; Iron; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Stress response; Transport.
FT CHAIN 1..400
FT /note="Flavo-diiron protein FprA2"
FT /id="PRO_0000405539"
FT DOMAIN 257..397
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 32..216
FT /note="Zinc metallo-hydrolase"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 263..267
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 345..372
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
SQ SEQUENCE 400 AA; 45044 MW; 1322C2C4E4274174 CRC64;
MPAIKIKDNI FSVGVLNPSL RIFDIIMKTE YGTSYNAYLI KGKKNVLIDT VHGRFFDEYL
ENIKSVIDPS SIDYVIMNHC EPDHSGSLAR LYEVAPQIKV IASNAGKIYL KNITNKETLD
VKAVKTNDTL DIGNGKVLKF AIAPFLHWPD SMFTILEEDK IAFTCDFLGC HFCEPRMFDT
KITYMPKYEK SFKEYYDAIF SPFKPYVVKG LDILDALDLD FIATSHGPIL TREGLLAASK
QKYRDLSSEI QSTTKYIPIF YCSAYGNTEI LANEIASGIK SVLNDANIEM LDIINYDYSD
LKEKINICDA FMLGTPTINK DALFPIWELI GGIDAVNCKN KPASAFGSFG WSGEAIPFVI
SRLKELKLKV FQDGFTCLFV PSEDDIKKAF KFGEDFAKSI
