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NADH-rubredoxin oxidoreductase (NROR) (EC 1.18.1.1) (NADH:rubredoxin oxidoreductase)

 NROR_CLOAB              Reviewed;         379 AA.
Q9AL95;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-MAR-2018, entry version 105.
RecName: Full=NADH-rubredoxin oxidoreductase;
Short=NROR;
EC=1.18.1.1;
AltName: Full=NADH:rubredoxin oxidoreductase;
Name=nroR; OrderedLocusNames=CA_C2448;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION
AS NROR, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, AND
KINETIC PARAMETERS.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=11444870; DOI=10.1006/bbrc.2001.5196;
Guedon E., Petitdemange H.;
"Identification of the gene encoding NADH-rubredoxin oxidoreductase in
Clostridium acetobutylicum.";
Biochem. Biophys. Res. Commun. 285:496-502(2001).
[2]
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).
[3]
PROTEIN SEQUENCE OF 1-20, AND FUNCTION.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=19124587; DOI=10.1128/AEM.01425-08;
Kawasaki S., Sakai Y., Takahashi T., Suzuki I., Niimura Y.;
"O2 and reactive oxygen species detoxification complex, composed of
O2-responsive NADH:rubredoxin oxidoreductase-flavoprotein A2-
desulfoferrodoxin operon enzymes, rubperoxin, and rubredoxin, in
Clostridium acetobutylicum.";
Appl. Environ. Microbiol. 75:1021-1029(2009).
[4]
INDUCTION BY O(2).
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=16332833; DOI=10.1128/AEM.71.12.8442-8450.2005;
Kawasaki S., Watamura Y., Ono M., Watanabe T., Takeda K., Niimura Y.;
"Adaptive responses to oxygen stress in obligatory anaerobes
Clostridium acetobutylicum and Clostridium aminovalericum.";
Appl. Environ. Microbiol. 71:8442-8450(2005).
[5]
FUNCTION.
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).
[6]
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).
[7]
FUNCTION, AND COFACTOR.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=19118342; DOI=10.1099/mic.0.022756-0;
Riebe O., Fischer R.J., Wampler D.A., Kurtz D.M. Jr., Bahl H.;
"Pathway for H2O2 and O2 detoxification in Clostridium
acetobutylicum.";
Microbiology 155:16-24(2009).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-379 IN COMPLEX WITH FAD,
COFACTOR, DISULFIDE BONDS, SUBUNIT, AND DOMAIN.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=20017214; DOI=10.1002/prot.22650;
Nishikawa K., Shomura Y., Kawasaki S., Niimura Y., Higuchi Y.;
"Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium
acetobutylicum: a key component of the dioxygen scavenging system in
obligatory anaerobes.";
Proteins 78:1066-1070(2010).
-!- FUNCTION: Catalyzes the NADH-dependent reduction of rubredoxin
(Rd). NADPH is a very poor electron donor compared to NADH.
Functions as an intermediate component in the electron transfer
chain: NADH->NROR->Rd->FprA1/2. Also functions as an intermediate
component in the electron transfer chains from NADH to revRbr and
Dfx. Therefore, is a key electron carrier in an efficient
multienzyme complex that can scavenge O(2) and reactive oxygen
species (ROS), and thus plays an important role in the oxidative
stress defense system in C.acetobutylicum, an obligate anaerobic
bacterium. {ECO:0000269|PubMed:11444870,
ECO:0000269|PubMed:19084524, ECO:0000269|PubMed:19118342,
ECO:0000269|PubMed:19124587}.
-!- CATALYTIC ACTIVITY: 2 reduced rubredoxin + NAD(+) + H(+) = 2
oxidized rubredoxin + NADH. {ECO:0000269|PubMed:11444870}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:11444870,
ECO:0000269|PubMed:19118342, ECO:0000269|PubMed:20017214};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11444870,
ECO:0000269|PubMed:19118342, ECO:0000269|PubMed:20017214};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.0 uM for rubredoxin {ECO:0000269|PubMed:11444870};
KM=17.4 uM for NADH {ECO:0000269|PubMed:11444870};
KM=2070 uM for NADPH {ECO:0000269|PubMed:11444870};
Vmax=570 umol/min/mg enzyme with rubredoxin and NADH as
substrates {ECO:0000269|PubMed:11444870};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20017214}.
-!- INDUCTION: Up-regulated upon exposure to O(2). Repressed by PerR.
{ECO:0000269|PubMed:16332833, ECO:0000269|PubMed:19648241}.
-!- DOMAIN: Is composed of three domains: an FAD-binding domain
(residues 2-107 and 223-297), an NADH-binding domain (residues
108-222), and a C-terminal domain (residues 298-379).
{ECO:0000269|PubMed:20017214}.
-!- MISCELLANEOUS: The disulfide bonds are not involved in the
electron transfer from NADH to rubredoxin catalyzed by NROR.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY026492; AAK08126.1; -; Genomic_DNA.
EMBL; AE001437; AAK80402.1; -; Genomic_DNA.
PIR; G97201; G97201.
PIR; JC7710; JC7710.
RefSeq; NP_349062.1; NC_003030.1.
RefSeq; WP_010965743.1; NC_003030.1.
PDB; 3KLJ; X-ray; 2.10 A; A=2-379.
PDBsum; 3KLJ; -.
ProteinModelPortal; Q9AL95; -.
SMR; Q9AL95; -.
STRING; 272562.CA_C2448; -.
EnsemblBacteria; AAK80402; AAK80402; CA_C2448.
GeneID; 1118631; -.
KEGG; cac:CA_C2448; -.
PATRIC; fig|272562.8.peg.2644; -.
eggNOG; ENOG4107SJS; Bacteria.
eggNOG; COG1251; LUCA.
HOGENOM; HOG000276711; -.
OMA; ALMYVYM; -.
BRENDA; 1.18.1.1; 1452.
EvolutionaryTrace; Q9AL95; -.
Proteomes; UP000000814; Chromosome.
GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0015044; F:rubredoxin-NAD+ reductase activity; IDA:UniProtKB.
GO; GO:0072592; P:oxygen metabolic process; IDA:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Pfam; PF07992; Pyr_redox_2; 1.
PRINTS; PR00469; PNDRDTASEII.
SUPFAM; SSF51905; SSF51905; 3.
1: Evidence at protein level;
3D-structure; Complete proteome; Detoxification;
Direct protein sequencing; Disulfide bond; Electron transport; FAD;
Flavoprotein; NAD; Oxidoreductase; Reference proteome;
Stress response; Transport.
CHAIN 1 379 NADH-rubredoxin oxidoreductase.
/FTId=PRO_0000405536.
NP_BIND 33 35 FAD. {ECO:0000269|PubMed:20017214}.
BINDING 42 42 FAD. {ECO:0000269|PubMed:20017214}.
BINDING 79 79 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:20017214}.
BINDING 125 125 FAD. {ECO:0000269|PubMed:20017214}.
BINDING 259 259 FAD. {ECO:0000269|PubMed:20017214}.
DISULFID 26 286 {ECO:0000269|PubMed:20017214}.
DISULFID 137 216 {ECO:0000269|PubMed:20017214}.
STRAND 5 9 {ECO:0000244|PDB:3KLJ}.
HELIX 13 22 {ECO:0000244|PDB:3KLJ}.
TURN 23 25 {ECO:0000244|PDB:3KLJ}.
STRAND 29 32 {ECO:0000244|PDB:3KLJ}.
STRAND 34 37 {ECO:0000244|PDB:3KLJ}.
HELIX 42 44 {ECO:0000244|PDB:3KLJ}.
HELIX 45 50 {ECO:0000244|PDB:3KLJ}.
HELIX 55 57 {ECO:0000244|PDB:3KLJ}.
STRAND 59 61 {ECO:0000244|PDB:3KLJ}.
HELIX 63 68 {ECO:0000244|PDB:3KLJ}.
STRAND 72 74 {ECO:0000244|PDB:3KLJ}.
STRAND 79 83 {ECO:0000244|PDB:3KLJ}.
TURN 84 87 {ECO:0000244|PDB:3KLJ}.
STRAND 88 91 {ECO:0000244|PDB:3KLJ}.
STRAND 96 98 {ECO:0000244|PDB:3KLJ}.
STRAND 100 104 {ECO:0000244|PDB:3KLJ}.
STRAND 108 110 {ECO:0000244|PDB:3KLJ}.
HELIX 127 140 {ECO:0000244|PDB:3KLJ}.
STRAND 143 146 {ECO:0000244|PDB:3KLJ}.
HELIX 150 162 {ECO:0000244|PDB:3KLJ}.
STRAND 166 169 {ECO:0000244|PDB:3KLJ}.
STRAND 171 175 {ECO:0000244|PDB:3KLJ}.
TURN 177 179 {ECO:0000244|PDB:3KLJ}.
HELIX 182 193 {ECO:0000244|PDB:3KLJ}.
TURN 194 196 {ECO:0000244|PDB:3KLJ}.
STRAND 198 200 {ECO:0000244|PDB:3KLJ}.
HELIX 205 207 {ECO:0000244|PDB:3KLJ}.
HELIX 209 214 {ECO:0000244|PDB:3KLJ}.
STRAND 215 219 {ECO:0000244|PDB:3KLJ}.
STRAND 223 225 {ECO:0000244|PDB:3KLJ}.
HELIX 228 230 {ECO:0000244|PDB:3KLJ}.
STRAND 237 243 {ECO:0000244|PDB:3KLJ}.
STRAND 254 256 {ECO:0000244|PDB:3KLJ}.
HELIX 258 260 {ECO:0000244|PDB:3KLJ}.
STRAND 261 263 {ECO:0000244|PDB:3KLJ}.
HELIX 271 285 {ECO:0000244|PDB:3KLJ}.
STRAND 300 303 {ECO:0000244|PDB:3KLJ}.
STRAND 306 312 {ECO:0000244|PDB:3KLJ}.
STRAND 320 326 {ECO:0000244|PDB:3KLJ}.
STRAND 331 337 {ECO:0000244|PDB:3KLJ}.
STRAND 340 348 {ECO:0000244|PDB:3KLJ}.
HELIX 350 361 {ECO:0000244|PDB:3KLJ}.
HELIX 372 376 {ECO:0000244|PDB:3KLJ}.
SEQUENCE 379 AA; 41286 MW; 08C83695DB7FE3E9 CRC64;
MKSTKILILG AGPAGFSAAK AALGKCDDIT MINSEKYLPY YRPRLNEIIA KNKSIDDILI
KKNDWYEKNN IKVITSEFAT SIDPNNKLVT LKSGEKIKYE KLIIASGSIA NKIKVPHADE
IFSLYSYDDA LKIKDECKNK GKAFIIGGGI LGIELAQAII DSGTPASIGI ILEYPLERQL
DRDGGLFLKD KLDRLGIKIY TNSNFEEMGD LIRSSCVITA VGVKPNLDFI KDTEIASKRG
ILVNDHMETS IKDIYACGDV AEFYGKNPGL INIANKQGEV AGLNACGEDA SYSEIIPSPI
LKVSGISIIS CGDIENNKPS KVFRSTQEDK YIVCMLKENK IDAAAVIGDV SLGTKLKKAI
DSSKSFDNIS SLDAILNNL


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