FPRA1_CLOAB
ID FPRA1_CLOAB Reviewed; 392 AA.
AC Q97K92;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Flavo-diiron protein FprA1;
DE Short=FDP 1;
DE AltName: Full=Flavoprotein A1;
DE AltName: Full=H(2)O-forming NADH oxidase;
DE EC=1.6.3.4 {ECO:0000269|PubMed:19084524};
DE AltName: Full=NADH oxidase;
DE AltName: Full=NADH:O(2) oxidoreductase;
GN Name=fprA1; OrderedLocusNames=CA_C1027;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY O(2).
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=15280011; DOI=10.1016/j.febslet.2004.06.047;
RA Kawasaki S., Ishikura J., Watamura Y., Niimura Y.;
RT "Identification of O2-induced peptides in an obligatory anaerobe,
RT Clostridium acetobutylicum.";
RL FEBS Lett. 571:21-25(2004).
RN [3]
RP REPRESSION BY PERR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=18430081; DOI=10.1111/j.1365-2958.2008.06192.x;
RA Hillmann F., Fischer R.J., Saint-Prix F., Girbal L., Bahl H.;
RT "PerR acts as a switch for oxygen tolerance in the strict anaerobe
RT Clostridium acetobutylicum.";
RL Mol. Microbiol. 68:848-860(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, 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.
CC {ECO:0000269|PubMed:19084524}.
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};
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19084524}.
CC -!- INDUCTION: Up-regulated upon exposure to O(2) (at mRNA and protein
CC levels). Repressed by PerR. {ECO:0000269|PubMed:15280011,
CC ECO:0000269|PubMed:18430081, 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; AAK79003.1; -; Genomic_DNA.
DR PIR; H97026; H97026.
DR RefSeq; NP_347663.1; NC_003030.1.
DR RefSeq; WP_010964345.1; NC_003030.1.
DR AlphaFoldDB; Q97K92; -.
DR SMR; Q97K92; -.
DR STRING; 272562.CA_C1027; -.
DR EnsemblBacteria; AAK79003; AAK79003; CA_C1027.
DR GeneID; 44997541; -.
DR KEGG; cac:CA_C1027; -.
DR PATRIC; fig|272562.8.peg.1235; -.
DR eggNOG; COG0426; Bacteria.
DR HOGENOM; CLU_017490_2_1_9; -.
DR OMA; AFGLHYC; -.
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:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:UniProtKB.
DR GO; GO:0072592; P:oxygen 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; Electron transport; Flavoprotein; FMN; Iron; Metal-binding;
KW NAD; Oxidoreductase; Reference proteome; Stress response; Transport.
FT CHAIN 1..392
FT /note="Flavo-diiron protein FprA1"
FT /id="PRO_0000405538"
FT DOMAIN 251..389
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 32..177
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 145
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 257..261
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 337..364
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
SQ 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
