Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Coenzyme A disulfide reductase (CoA-disulfide reductase) (CoADR) (EC 1.8.1.14)

 CDR_STAA8               Reviewed;         438 AA.
O52582; Q2FZT2;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 116.
RecName: Full=Coenzyme A disulfide reductase;
Short=CoA-disulfide reductase;
Short=CoADR;
EC=1.8.1.14;
Name=cdr; OrderedLocusNames=SAOUHSC_00908;
Staphylococcus aureus (strain NCTC 8325).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=93061;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15 AND
193-208.
PubMed=9488708; DOI=10.1074/jbc.273.10.5752;
delCardayre S.B., Davies J.E.;
"Staphylococcus aureus coenzyme A disulfide reductase, a new subfamily
of pyridine nucleotide-disulfide oxidoreductase. Sequence, expression,
and analysis of cdr.";
J. Biol. Chem. 273:5752-5757(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 8325;
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
Iandolo J.J.;
"The Staphylococcus aureus NCTC 8325 genome.";
(In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
Washington D.C. (2006).
[3]
CHARACTERIZATION.
PubMed=9488707; DOI=10.1074/jbc.273.10.5744;
delCardayre S.B., Stock K.P., Newton G.L., Fahey R.C., Davies J.E.;
"Coenzyme A disulfide reductase, the primary low molecular weight
disulfide reductase from Staphylococcus aureus. Purification and
characterization of the native enzyme.";
J. Biol. Chem. 273:5744-5751(1998).
[4]
CHARACTERIZATION, ACTIVE SITE, MUTAGENESIS OF CYS-43, AND MASS
SPECTROMETRY.
PubMed=10052943; DOI=10.1021/bi9825899;
Luba J., Charrier V., Claiborne A.;
"Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence
for asymmetric behavior on interaction with pyridine nucleotides.";
Biochemistry 38:2725-2737(1999).
[5]
X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH FAD AND
SUBSTRATE, MUTAGENESIS OF TYR-361 AND TYR-419, AND SUBUNIT.
PubMed=16981688; DOI=10.1021/bi061139a;
Mallett T.C., Wallen J.R., Karplus P.A., Sakai H., Tsukihara T.,
Claiborne A.;
"Structure of coenzyme A-disulfide reductase from Staphylococcus
aureus at 1.54 A resolution.";
Biochemistry 45:11278-11289(2006).
-!- FUNCTION: Catalyzes specifically the NADPH-dependent reduction of
coenzyme A disulfide. Is also active with other disulfide
substrates containing at least one 4'-phosphopantethienyl moiety
such as 4,4'-diphosphopantethine, but is not able to reduce
oxidized glutathione, cystine, pantethine, or H(2)O(2).
-!- CATALYTIC ACTIVITY: 2 CoA + NADP(+) = CoA-disulfide + NADPH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2 uM for NADPH;
KM=11 uM for CoA disulfide;
KM=140 uM for 3'-dephospho-CoA disulfide;
KM=80 uM for 4,4'-diphosphopantethine;
KM=1100 uM for CoA glutathione mixed disulfide;
pH dependence:
Optimum pH is 7.0-8.0.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16981688}.
-!- DOMAIN: Contains 2 FAD binding domains and a single NADPH binding
domain.
-!- MASS SPECTROMETRY: Mass=49153; Method=Electrospray; Range=2-438;
Evidence={ECO:0000269|PubMed:10052943};
-!- MISCELLANEOUS: Reduction of disulfides occurs by a thiol-disulfide
exchange reaction, but involves only a single catalytic cysteine
residue that forms a stable mixed disulfide with CoA during
catalysis.
-!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF041467; AAB97073.1; -; Genomic_DNA.
EMBL; CP000253; ABD30033.1; -; Genomic_DNA.
RefSeq; YP_499461.1; NC_007795.1.
PDB; 1YQZ; X-ray; 1.54 A; A/B=1-438.
PDBsum; 1YQZ; -.
ProteinModelPortal; O52582; -.
SMR; O52582; -.
STRING; 93061.SAOUHSC_00908; -.
PRIDE; O52582; -.
EnsemblBacteria; ABD30033; ABD30033; SAOUHSC_00908.
GeneID; 3920795; -.
KEGG; sao:SAOUHSC_00908; -.
PATRIC; fig|93061.5.peg.829; -.
eggNOG; ENOG4107QMW; Bacteria.
eggNOG; COG0446; LUCA.
HOGENOM; HOG000276710; -.
KO; K08255; -.
BioCyc; SAUR93061:G1G5Y-851-MONOMER; -.
BRENDA; 1.8.1.14; 3352.
SABIO-RK; O52582; -.
EvolutionaryTrace; O52582; -.
Proteomes; UP000008816; Chromosome.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0050451; F:CoA-disulfide reductase activity; IEA:UniProtKB-UniRule.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-UniRule.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
Gene3D; 3.50.50.60; -; 6.
HAMAP; MF_01608; CoA_diS_reduct; 1.
InterPro; IPR017758; CoA_disulphide_reductase.
InterPro; IPR023536; CoA_disulphide_reductase_staph.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR03385; CoA_CoA_reduc; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; FAD;
Flavoprotein; NADP; Oxidoreductase; Redox-active center;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9488708}.
CHAIN 2 438 Coenzyme A disulfide reductase.
/FTId=PRO_0000184688.
NP_BIND 8 33 FAD. {ECO:0000269|PubMed:16981688}.
NP_BIND 151 166 NADP. {ECO:0000250}.
NP_BIND 267 277 FAD. {ECO:0000269|PubMed:16981688}.
ACT_SITE 43 43 Nucleophile.
{ECO:0000269|PubMed:10052943}.
ACT_SITE 43 43 Redox-active.
{ECO:0000269|PubMed:10052943}.
BINDING 15 15 Substrate. {ECO:0000269|PubMed:16981688}.
BINDING 19 19 Substrate. {ECO:0000269|PubMed:16981688}.
BINDING 22 22 Substrate. {ECO:0000269|PubMed:16981688}.
BINDING 39 39 Substrate. {ECO:0000269|PubMed:16981688}.
BINDING 42 42 Substrate. {ECO:0000269|PubMed:16981688}.
BINDING 71 71 Substrate. {ECO:0000269|PubMed:16981688}.
BINDING 299 299 Substrate. {ECO:0000269|PubMed:16981688}.
BINDING 419 419 FAD; via carbonyl oxygen.
{ECO:0000269|PubMed:16981688}.
BINDING 427 427 Substrate. {ECO:0000269|PubMed:16981688}.
MUTAGEN 43 43 C->S: Loss of activity.
{ECO:0000269|PubMed:10052943}.
MUTAGEN 361 361 Y->F: Reduces activity by 92%. Loss of
activity; when associated with F-419.
{ECO:0000269|PubMed:16981688}.
MUTAGEN 419 419 Y->F: Reduces activity by 80%. Loss of
activity; when associated with F-361.
{ECO:0000269|PubMed:16981688}.
STRAND 4 7 {ECO:0000244|PDB:1YQZ}.
HELIX 13 23 {ECO:0000244|PDB:1YQZ}.
STRAND 25 27 {ECO:0000244|PDB:1YQZ}.
STRAND 29 36 {ECO:0000244|PDB:1YQZ}.
STRAND 38 40 {ECO:0000244|PDB:1YQZ}.
HELIX 42 44 {ECO:0000244|PDB:1YQZ}.
HELIX 45 49 {ECO:0000244|PDB:1YQZ}.
HELIX 56 59 {ECO:0000244|PDB:1YQZ}.
HELIX 64 71 {ECO:0000244|PDB:1YQZ}.
STRAND 74 77 {ECO:0000244|PDB:1YQZ}.
STRAND 79 85 {ECO:0000244|PDB:1YQZ}.
TURN 86 89 {ECO:0000244|PDB:1YQZ}.
STRAND 90 95 {ECO:0000244|PDB:1YQZ}.
TURN 96 99 {ECO:0000244|PDB:1YQZ}.
STRAND 100 105 {ECO:0000244|PDB:1YQZ}.
STRAND 107 111 {ECO:0000244|PDB:1YQZ}.
STRAND 115 117 {ECO:0000244|PDB:1YQZ}.
HELIX 133 146 {ECO:0000244|PDB:1YQZ}.
STRAND 150 154 {ECO:0000244|PDB:1YQZ}.
HELIX 158 170 {ECO:0000244|PDB:1YQZ}.
STRAND 173 181 {ECO:0000244|PDB:1YQZ}.
HELIX 189 192 {ECO:0000244|PDB:1YQZ}.
HELIX 193 201 {ECO:0000244|PDB:1YQZ}.
STRAND 206 209 {ECO:0000244|PDB:1YQZ}.
STRAND 212 216 {ECO:0000244|PDB:1YQZ}.
STRAND 219 222 {ECO:0000244|PDB:1YQZ}.
STRAND 227 229 {ECO:0000244|PDB:1YQZ}.
STRAND 231 235 {ECO:0000244|PDB:1YQZ}.
STRAND 239 242 {ECO:0000244|PDB:1YQZ}.
HELIX 244 246 {ECO:0000244|PDB:1YQZ}.
STRAND 272 274 {ECO:0000244|PDB:1YQZ}.
HELIX 276 278 {ECO:0000244|PDB:1YQZ}.
STRAND 279 290 {ECO:0000244|PDB:1YQZ}.
HELIX 295 310 {ECO:0000244|PDB:1YQZ}.
STRAND 324 328 {ECO:0000244|PDB:1YQZ}.
STRAND 331 338 {ECO:0000244|PDB:1YQZ}.
HELIX 340 345 {ECO:0000244|PDB:1YQZ}.
STRAND 348 358 {ECO:0000244|PDB:1YQZ}.
STRAND 362 364 {ECO:0000244|PDB:1YQZ}.
STRAND 367 375 {ECO:0000244|PDB:1YQZ}.
TURN 376 378 {ECO:0000244|PDB:1YQZ}.
STRAND 380 391 {ECO:0000244|PDB:1YQZ}.
HELIX 392 404 {ECO:0000244|PDB:1YQZ}.
HELIX 410 414 {ECO:0000244|PDB:1YQZ}.
TURN 421 423 {ECO:0000244|PDB:1YQZ}.
HELIX 429 435 {ECO:0000244|PDB:1YQZ}.
SEQUENCE 438 AA; 49241 MW; 3A9B643BD8D44402 CRC64;
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRRYAL
AYTPEKFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE QFEESYDKLI LSPGASANSL
GFESDITFTL RNLEDTDAID QFIKANQVDK VLVVGAGYVS LEVLENLNER GLHPTLIHRS
DKINKLMDAD MNQPILDELD KREIPYRLNE EINAINGNEI TFKSGKVEHY DMIIEGVGTH
PNSKFIESSN IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR
AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN
YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS MAMMNQLTVD ELTEFEVAYA
PPYSHPKDLI NMIGYKAK


Related products :

Catalog number Product name Quantity
EIAAB10691 Carbonyl reductase II,DCXR,Dicarbonyl_L-xylulose reductase,Homo sapiens,Human,kiDCR,Kidney dicarbonyl reductase,L-xylulose reductase,Sperm surface protein P34H,XR
EIAAB11124 7-dehydrocholesterol reductase,7-DHC reductase,D7SR,DHCR7,Homo sapiens,Human,Putative sterol reductase SR-2,Sterol Delta(7)-reductase
EIAAB11127 7-dehydrocholesterol reductase,7-DHC reductase,Dhcr7,Rat,Rattus norvegicus,Sterol Delta(7)-reductase
EIAAB11126 7-dehydrocholesterol reductase,7-DHC reductase,Bos taurus,Bovine,DHCR7,Sterol Delta(7)-reductase
EIAAB11125 7-dehydrocholesterol reductase,7-DHC reductase,Dhcr7,Mouse,Mus musculus,Sterol Delta(7)-reductase
26-852 GSR belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. It maintains high levels of reduced glutathione in the cytosol. Both glutathione and glutathione reductase are inducible 0.05 mg
E2220h AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human
U2220h CLIA AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
E2220h ELISA kit AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
E2220h ELISA AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
U2220h CLIA kit AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
EIAAB13217 ANG1,Another new gene 1 protein,C-14 sterol reductase,Delta(14)-sterol reductase,Delta-14-SR,Homo sapiens,Human,Putative sterol reductase SR-1,Sterol C14-reductase,TM7SF2,Transmembrane 7 superfamily m
EIAAB05628 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Quinone reductase CBR4,Rat,Rattus norvegicus
EIAAB05625 3-oxoacyl-[acyl-carrier-protein] reductase,Bos taurus,Bovine,Carbonyl reductase family member 4,CBR4,Quinone reductase CBR4
EIAAB05627 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Mouse,Mus musculus,Quinone reductase CBR4
orb41407 TXNDC1 antibody Polyclonal Rabbit polyclonal to TXNDC1. TXNDC1 is a thioredoxin (TXN; see MIM 187700)-related protein with disulfide reductase activity (Matsuo et al., 2001 [PubMed 11152479]).[supplie 100
EIAAB05626 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,CBR4,Homo sapiens,Human,Quinone reductase CBR4
EIAAB11121 24-dehydrocholesterol reductase,3-beta-hydroxysterol delta-24-reductase,Delta(24)-sterol reductase,Dhcr24,Kiaa0018,Mouse,Mus musculus
EIAAB11123 24-dehydrocholesterol reductase,3-beta-hydroxysterol delta-24-reductase,Delta(24)-sterol reductase,DHCR24,Diminuto_dwarf1 homolog,Homo sapiens,Human,KIAA0018,Seladin-1
EIAAB11122 24-dehydrocholesterol reductase,3-beta-hydroxysterol delta-24-reductase,Delta(24)-sterol reductase,Dhcr24,Rat,Rattus norvegicus
EIAAB25528 Homo sapiens,Human,Mitochondrial peptide methionine sulfoxide reductase,MSRA,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase
EIAAB27759 Azoreductase,DTD,DT-diaphorase,Menadione reductase,NAD(P)H dehydrogenase [quinone] 1,NAD(P)H quinone oxidoreductase 1,Nmor1,Nqo1,Phylloquinone reductase,QR1,Quinone reductase 1,Rat,Rattus norvegicus
EIAAB27760 Azoreductase,DIA4,DTD,DT-diaphorase,Homo sapiens,Human,Menadione reductase,NAD(P)H dehydrogenase [quinone] 1,NAD(P)H quinone oxidoreductase 1,NMOR1,NQO1,Phylloquinone reductase,QR1,Quinone reductase 1
EIAAB25529 Mitochondrial peptide methionine sulfoxide reductase,Msra,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase,Rat,Rattus norvegicus
EIAAB25530 Mitochondrial peptide methionine sulfoxide reductase,Mouse,Msra,Mus musculus,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur