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Flavo-diiron protein FprA1 (FDP 1) (Flavoprotein A1) (H(2)O-forming NADH oxidase) (EC 1.6.3.4) (NADH oxidase) (NADH:O(2) oxidoreductase)

 FPRA1_CLOAB             Reviewed;         392 AA.
Q97K92;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 1.
22-NOV-2017, entry version 96.
RecName: Full=Flavo-diiron protein FprA1;
Short=FDP 1;
AltName: Full=Flavoprotein A1;
AltName: Full=H(2)O-forming NADH oxidase;
EC=1.6.3.4 {ECO:0000269|PubMed:19084524};
AltName: Full=NADH oxidase;
AltName: Full=NADH:O(2) oxidoreductase;
Name=fprA1; OrderedLocusNames=CA_C1027;
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG
5710 / VKM B-1787).
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=272562;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
"Genome sequence and comparative analysis of the solvent-producing
bacterium Clostridium acetobutylicum.";
J. Bacteriol. 183:4823-4838(2001).
[2]
IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY O(2).
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=15280011; DOI=10.1016/j.febslet.2004.06.047;
Kawasaki S., Ishikura J., Watamura Y., Niimura Y.;
"Identification of O2-induced peptides in an obligatory anaerobe,
Clostridium acetobutylicum.";
FEBS Lett. 571:21-25(2004).
[3]
REPRESSION BY PERR.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=18430081; DOI=10.1111/j.1365-2958.2008.06192.x;
Hillmann F., Fischer R.J., Saint-Prix F., Girbal L., Bahl H.;
"PerR acts as a switch for oxygen tolerance in the strict anaerobe
Clostridium acetobutylicum.";
Mol. Microbiol. 68:848-860(2008).
[4]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=19084524; DOI=10.1016/j.febslet.2008.12.004;
Hillmann F., Riebe O., Fischer R.J., Mot A., Caranto J.D.,
Kurtz D.M. Jr., Bahl H.;
"Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium
acetobutylicum.";
FEBS Lett. 583:241-245(2009).
[5]
INDUCTION BY O(2), AND REPRESSION BY PERR.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=19648241; DOI=10.1128/JB.00351-09;
Hillmann F., Doring C., Riebe O., Ehrenreich A., Fischer R.J.,
Bahl H.;
"The role of PerR in O2-affected gene expression of Clostridium
acetobutylicum.";
J. Bacteriol. 191:6082-6093(2009).
-!- FUNCTION: Catalyzes the four-electron reduction of molecular
oxygen to water. In fact, functions as the terminal component of
an NADH oxidase (NADH:O(2) oxidoreductase) when using
NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as
electron transport intermediaries between NADH and FDP. Is thus
able to reductively scavenge intracellular dioxygen and is part of
an oxidative stress defense system in C.acetobutylicum, an
obligate anaerobic bacterium. {ECO:0000269|PubMed:19084524}.
-!- CATALYTIC ACTIVITY: 2 NADH + O(2) = 2 NAD(+) + 2 H(2)O.
{ECO:0000269|PubMed:19084524}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:19084524};
Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:19084524};
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:19084524};
Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:19084524};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19084524}.
-!- INDUCTION: Up-regulated upon exposure to O(2) (at mRNA and protein
levels). Repressed by PerR. {ECO:0000269|PubMed:15280011,
ECO:0000269|PubMed:18430081, ECO:0000269|PubMed:19648241}.
-!- DOMAIN: Consists of an N-terminal non-heme diiron domain and a C-
terminal flavodoxin-like domain.
-!- SIMILARITY: In the N-terminal section; belongs to the zinc
metallo-hydrolase group 3 family. {ECO:0000305}.
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EMBL; AE001437; AAK79003.1; -; Genomic_DNA.
PIR; H97026; H97026.
RefSeq; NP_347663.1; NC_003030.1.
RefSeq; WP_010964345.1; NC_003030.1.
ProteinModelPortal; Q97K92; -.
SMR; Q97K92; -.
STRING; 272562.CA_C1027; -.
EnsemblBacteria; AAK79003; AAK79003; CA_C1027.
GeneID; 1117210; -.
KEGG; cac:CA_C1027; -.
PATRIC; fig|272562.8.peg.1235; -.
eggNOG; ENOG4105CNW; Bacteria.
eggNOG; COG0426; LUCA.
HOGENOM; HOG000224528; -.
OMA; AFGLHYC; -.
Proteomes; UP000000814; Chromosome.
GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB.
GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:UniProtKB.
GO; GO:0072592; P:oxygen metabolic process; IDA:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
Gene3D; 3.40.50.360; -; 1.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001226; Flavodoxin_CS.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
InterPro; IPR016440; Rubredoxin-O_OxRdtase.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00753; Lactamase_B; 1.
PIRSF; PIRSF005243; ROO; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF56281; SSF56281; 1.
PROSITE; PS00201; FLAVODOXIN; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
Complete proteome; Detoxification; Electron transport; Flavoprotein;
FMN; Iron; Metal-binding; NAD; Oxidoreductase; Reference proteome;
Stress response; Transport.
CHAIN 1 392 Flavo-diiron protein FprA1.
/FTId=PRO_0000405538.
DOMAIN 251 389 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 257 261 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 337 364 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
REGION 32 177 Zinc metallo-hydrolase.
METAL 79 79 Iron 1. {ECO:0000250}.
METAL 81 81 Iron 1. {ECO:0000250}.
METAL 83 83 Iron 2. {ECO:0000250}.
METAL 145 145 Iron 1. {ECO:0000250}.
METAL 164 164 Iron 1. {ECO:0000250}.
METAL 164 164 Iron 2. {ECO:0000250}.
METAL 222 222 Iron 2. {ECO:0000250}.
SEQUENCE 392 AA; 44491 MW; 20C31962FA9E4332 CRC64;
MSAEKLCENV YWVGVKDQKL RVFDIIMNTK KGSTYNSYLI NDDKVAIIDT VKDGFYDEFL
KSIKSVIGDK KVDYIVVQHT ELDHSGSMYR LIKEYPEAKV VSSKAANMYL KEIVNDEFNS
LDAMEVKELN LGKNTLEFIS APNLHWPDTM FTYNKENNIL FTCDVMGCHY CPDGSIKDEG
GEDYLPEMRY YFDVIMSPFK KFVNMGLDKI KDLKLDMIAP SHGPVHINDI EESVKLYREW
AKEKEPKEKN VQIFYITAYG NTGIMAKHLC EDINKKGVKA EVHEITDMKM EDIVELIADA
NGVLVGSPTI NQDAVRPVWD VLSSVCPIVN RGKAAAAFGS YGWSGEGVPM MMDRLKSLKF
KTPDNGLKFK FVPASKEFSE ADKFVDDFIG LL


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