NROR_CLOAB
ID NROR_CLOAB Reviewed; 379 AA.
AC Q9AL95;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=NADH-rubredoxin oxidoreductase;
DE Short=NROR;
DE EC=1.18.1.1;
DE AltName: Full=NADH:rubredoxin oxidoreductase;
GN Name=nroR; OrderedLocusNames=CA_C2448;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION AS
RP NROR, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, AND KINETIC
RP PARAMETERS.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11444870; DOI=10.1006/bbrc.2001.5196;
RA Guedon E., Petitdemange H.;
RT "Identification of the gene encoding NADH-rubredoxin oxidoreductase in
RT Clostridium acetobutylicum.";
RL Biochem. Biophys. Res. Commun. 285:496-502(2001).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-20, AND FUNCTION.
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 [4]
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 [5]
RP FUNCTION.
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 [6]
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).
RN [7]
RP FUNCTION, AND COFACTOR.
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-379 IN COMPLEX WITH FAD,
RP COFACTOR, DISULFIDE BONDS, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=20017214; DOI=10.1002/prot.22650;
RA Nishikawa K., Shomura Y., Kawasaki S., Niimura Y., Higuchi Y.;
RT "Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium
RT acetobutylicum: a key component of the dioxygen scavenging system in
RT obligatory anaerobes.";
RL Proteins 78:1066-1070(2010).
CC -!- FUNCTION: Catalyzes the NADH-dependent reduction of rubredoxin (Rd).
CC NADPH is a very poor electron donor compared to NADH. Functions as an
CC intermediate component in the electron transfer chain:
CC NADH->NROR->Rd->FprA1/2. Also functions as an intermediate component in
CC the electron transfer chains from NADH to revRbr and Dfx. Therefore, is
CC a key electron carrier in an efficient multienzyme complex that can
CC scavenge O(2) and reactive oxygen species (ROS), and thus plays an
CC important role in the oxidative stress defense system in
CC C.acetobutylicum, an obligate anaerobic bacterium.
CC {ECO:0000269|PubMed:11444870, ECO:0000269|PubMed:19084524,
CC ECO:0000269|PubMed:19118342, ECO:0000269|PubMed:19124587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [rubredoxin] = NADH + 2 oxidized
CC [rubredoxin]; Xref=Rhea:RHEA:18597, Rhea:RHEA-COMP:10302, Rhea:RHEA-
CC COMP:10303, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.18.1.1;
CC Evidence={ECO:0000269|PubMed:11444870};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11444870, ECO:0000269|PubMed:19118342,
CC ECO:0000269|PubMed:20017214};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11444870,
CC ECO:0000269|PubMed:19118342, ECO:0000269|PubMed:20017214};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for rubredoxin {ECO:0000269|PubMed:11444870};
CC KM=17.4 uM for NADH {ECO:0000269|PubMed:11444870};
CC KM=2070 uM for NADPH {ECO:0000269|PubMed:11444870};
CC Vmax=570 umol/min/mg enzyme with rubredoxin and NADH as substrates
CC {ECO:0000269|PubMed:11444870};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20017214}.
CC -!- INDUCTION: Up-regulated upon exposure to O(2). Repressed by PerR.
CC {ECO:0000269|PubMed:16332833, ECO:0000269|PubMed:19648241}.
CC -!- DOMAIN: Is composed of three domains: an FAD-binding domain (residues
CC 2-107 and 223-297), an NADH-binding domain (residues 108-222), and a C-
CC terminal domain (residues 298-379). {ECO:0000269|PubMed:20017214}.
CC -!- MISCELLANEOUS: The disulfide bonds are not involved in the electron
CC transfer from NADH to rubredoxin catalyzed by NROR.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AY026492; AAK08126.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK80402.1; -; Genomic_DNA.
DR PIR; G97201; G97201.
DR PIR; JC7710; JC7710.
DR RefSeq; NP_349062.1; NC_003030.1.
DR RefSeq; WP_010965743.1; NC_003030.1.
DR PDB; 3KLJ; X-ray; 2.10 A; A=2-379.
DR PDBsum; 3KLJ; -.
DR AlphaFoldDB; Q9AL95; -.
DR SMR; Q9AL95; -.
DR STRING; 272562.CA_C2448; -.
DR EnsemblBacteria; AAK80402; AAK80402; CA_C2448.
DR GeneID; 44998926; -.
DR KEGG; cac:CA_C2448; -.
DR PATRIC; fig|272562.8.peg.2644; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_4_4_9; -.
DR OMA; YGLVEPA; -.
DR OrthoDB; 1149616at2; -.
DR BRENDA; 1.18.1.1; 1452.
DR SABIO-RK; Q9AL95; -.
DR EvolutionaryTrace; Q9AL95; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0015044; F:rubredoxin-NAD+ reductase activity; 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; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR041575; Rubredoxin_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; Direct protein sequencing; Disulfide bond;
KW Electron transport; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Reference proteome; Stress response; Transport.
FT CHAIN 1..379
FT /note="NADH-rubredoxin oxidoreductase"
FT /id="PRO_0000405536"
FT BINDING 33..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20017214"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20017214"
FT BINDING 79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20017214"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20017214"
FT BINDING 259
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20017214"
FT DISULFID 26..286
FT /evidence="ECO:0000269|PubMed:20017214"
FT DISULFID 137..216
FT /evidence="ECO:0000269|PubMed:20017214"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:3KLJ"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:3KLJ"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3KLJ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:3KLJ"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:3KLJ"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:3KLJ"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:3KLJ"
SQ 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
