RUBY1_CLOAB
ID RUBY1_CLOAB Reviewed; 195 AA.
AC Q97FZ9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Rubrerythrin-1;
DE Short=Rr 1;
DE AltName: Full=NADH peroxidase;
DE Short=NPXase;
DE Short=Npx;
DE EC=1.11.1.1;
GN Name=rbr1; Synonyms=rubY; OrderedLocusNames=CA_C2575;
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 GENE NAME, AND NO INDUCTION BY AIR OR H(2)O(2).
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=15336429; DOI=10.1111/j.1574-6968.2004.tb09763.x;
RA May A., Hillmann F., Riebe O., Fischer R.J., Bahl H.;
RT "A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum
RT is encoded by a duplicated gene and identical to the heat shock protein
RT Hsp21.";
RL FEMS Microbiol. Lett. 238:249-254(2004).
RN [3]
RP NO INDUCTION BY VARIOUS ENVIRONMENTAL STRESS CONDITIONS.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=16463182; DOI=10.1007/s00203-006-0091-y;
RA Hillmann F., Fischer R.J., Bahl H.;
RT "The rubrerythrin-like protein Hsp21 of Clostridium acetobutylicum is a
RT general stress protein.";
RL Arch. Microbiol. 185:270-276(2006).
RN [4]
RP NO 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 [5]
RP NO INDUCTION BY O(2), AND NO 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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19118342; DOI=10.1099/mic.0.022756-0;
RA Riebe O., Fischer R.J., Wampler D.A., Kurtz D.M. Jr., Bahl H.;
RT "Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum.";
RL Microbiology 155:16-24(2009).
CC -!- FUNCTION: Functions as the terminal component of an NADH peroxidase
CC (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin
CC oxidoreductase (NROR) as the electron transport intermediary from NADH
CC to RubY. {ECO:0000269|PubMed:19118342}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + NADH = 2 H2O + NAD(+); Xref=Rhea:RHEA:18509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.1;
CC Evidence={ECO:0000269|PubMed:19118342};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC Note=Binds 3 Fe(3+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Rubredoxin (Rd) increases the NADH consumption
CC rate by serving as an intermediary electron-transfer shuttle between
CC NROR and RubY. {ECO:0000269|PubMed:19118342}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19118342}.
CC -!- INDUCTION: Various environmental stress conditions, e.g. oxidative
CC stress (exposure to air or H(2)O(2)) and other stress factors such as
CC salt, increased pH, high concentration of solvents or cold shock, do
CC not lead to increased transcript levels of this gene. Is not repressed
CC by PerR.
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DR EMBL; AE001437; AAK80524.1; -; Genomic_DNA.
DR PIR; A97217; A97217.
DR RefSeq; NP_349184.1; NC_003030.1.
DR RefSeq; WP_010965865.1; NC_003030.1.
DR AlphaFoldDB; Q97FZ9; -.
DR SMR; Q97FZ9; -.
DR STRING; 272562.CA_C2575; -.
DR EnsemblBacteria; AAK80524; AAK80524; CA_C2575.
DR GeneID; 44999044; -.
DR KEGG; cac:CA_C2575; -.
DR PATRIC; fig|272562.8.peg.2764; -.
DR eggNOG; COG1592; Bacteria.
DR HOGENOM; CLU_095256_0_1_9; -.
DR OMA; PQAYFEV; -.
DR OrthoDB; 1681849at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016692; F:NADH peroxidase activity; IDA:UniProtKB.
DR CDD; cd01041; Rubrerythrin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR003251; Rubrerythrin.
DR Pfam; PF02915; Rubrerythrin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Electron transport; Iron; Metal-binding; NAD; Oxidoreductase; Peroxidase;
KW Reference proteome; Transport.
FT CHAIN 1..195
FT /note="Rubrerythrin-1"
FT /id="PRO_0000405532"
FT DOMAIN 3..150
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT DOMAIN 157..191
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 20
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 53
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 53
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 98
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 101
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 132
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 132
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 135
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 162
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 165
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 178
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 181
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
SQ SEQUENCE 195 AA; 22158 MW; A6872207D790F37F CRC64;
MKSLKGTKTA ENLMKAFAGE SQARNRYTFY SNTAKKEGYV QISNIFLETA ENERMHAKRF
FKFLSEGLDD EAVEINGASY PTTLGDTKKN LIAAAKGENE EWTDLYPSFA KTAEDEGFKG
VAAAFRLIAA VEKEHEKRYN ALLKNIEENK VFEKDEVKFW KCIKCGYIFE GKTAPKVCPA
CLHPQAYFEI LSENY
