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Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase)

 PYRD_HUMAN              Reviewed;         395 AA.
Q02127; A8K8C8; Q6P176;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 3.
23-MAY-2018, entry version 188.
RecName: Full=Dihydroorotate dehydrogenase (quinone), mitochondrial;
Short=DHOdehase;
EC=1.3.5.2;
AltName: Full=Dihydroorotate oxidase;
Flags: Precursor;
Name=DHODH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-7.
PubMed=1446837; DOI=10.1016/0378-1119(92)90150-N;
Minet M., Dufour M.E., Lacroute F.;
"Cloning and sequencing of a human cDNA coding for dihydroorotate
dehydrogenase by complementation of the corresponding yeast mutant.";
Gene 121:393-396(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
PubMed=7487077; DOI=10.1006/abbi.1995.0012;
Copeland R.A., Davis J.P., Dowling R.L., Lombardo D., Murphy K.B.,
Patterson T.A.;
"Recombinant human dihydroorotate dehydrogenase: expression,
purification, and characterization of a catalytically functional
truncated enzyme.";
Arch. Biochem. Biophys. 323:79-86(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-7.
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ENZYME ACTIVITY.
PubMed=8925840; DOI=10.1111/j.1432-1033.1996.0292h.x;
Knecht W., Bergjohann U., Gonski S., Kirschbaum B., Loeffler M.;
"Functional expression of a fragment of human dihydroorotate
dehydrogenase by means of the baculovirus expression vector system,
and kinetic investigation of the purified recombinant enzyme.";
Eur. J. Biochem. 240:292-301(1996).
[6]
SUBCELLULAR LOCATION.
PubMed=10727948; DOI=10.1046/j.1432-1327.2000.01213.x;
Rawls J., Knecht W., Diekert K., Lill R., Loeffler M.;
"Requirements for the mitochondrial import and localization of
dihydroorotate dehydrogenase.";
Eur. J. Biochem. 267:2079-2087(2000).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-395 IN COMPLEX WITH FMN;
DIHYDROOROTATE AND INHIBITORS, AND COFACTOR.
PubMed=10673429; DOI=10.1016/S0969-2126(00)00077-0;
Liu S., Neidhardt E.A., Grossman T.H., Ocain T., Clardy J.;
"Structures of human dihydroorotate dehydrogenase in complex with
antiproliferative agents.";
Structure 8:25-33(2000).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-395 IN COMPLEX WITH FMN
AND INHIBITORS.
PubMed=16480261; DOI=10.1021/jm0506975;
Baumgartner R., Walloschek M., Kralik M., Gotschlich A., Tasler S.,
Mies J., Leban J.;
"Dual binding mode of a novel series of DHODH inhibitors.";
J. Med. Chem. 49:1239-1247(2006).
[12]
VARIANTS POADS GLU-19; CYS-135; ARG-152; CYS-199; ALA-202; ASP-202;
TRP-244; ILE-284; TRP-346 AND GLY-392.
PubMed=19915526; DOI=10.1038/ng.499;
Ng S.B., Buckingham K.J., Lee C., Bigham A.W., Tabor H.K., Dent K.M.,
Huff C.D., Shannon P.T., Jabs E.W., Nickerson D.A., Shendure J.,
Bamshad M.J.;
"Exome sequencing identifies the cause of a Mendelian disorder.";
Nat. Genet. 42:30-35(2010).
-!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
with quinone as electron acceptor.
-!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
quinol. {ECO:0000269|PubMed:8925840}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:10673429};
Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:10673429};
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; orotate from (S)-dihydroorotate (quinone route): step
1/1.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:10727948}; Single-pass membrane protein
{ECO:0000269|PubMed:10727948}.
-!- PTM: The uncleaved transit peptide is required for mitochondrial
targeting and proper membrane integration.
-!- DISEASE: Postaxial acrofacial dysostosis (POADS) [MIM:263750]:
POADS is characterized by severe micrognathia, cleft lip and/or
palate, hypoplasia or aplasia of the posterior elements of the
limbs, coloboma of the eyelids and supernumerary nipples. POADS is
a very rare disorder: only 2 multiplex families, each consisting
of 2 affected siblings born to unaffected, nonconsanguineous
parents, have been described among a total of around 30 reported
cases. {ECO:0000269|PubMed:19915526}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The identification of DHODH defects as the cause of
postaxial acrofacial dysostosis (POADS) was obtained via exome
sequencing (PubMed:19915526), demonstrating that this method is a
powerful tool for identifying genes underlying rare Mendelian
disorders. Exome sequencing consists of targeted resequencing of
all protein-coding subsequences, which requires around 5% as much
sequencing as a whole human genome. {ECO:0000305|PubMed:19915526}.
-!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
Type 2 subfamily. {ECO:0000305}.
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EMBL; M94065; AAA50163.1; -; mRNA.
EMBL; AK292293; BAF84982.1; -; mRNA.
EMBL; BC065245; AAH65245.1; -; mRNA.
CCDS; CCDS42192.1; -.
PIR; PC1219; PC1219.
RefSeq; NP_001352.2; NM_001361.4.
UniGene; Hs.654427; -.
PDB; 1D3G; X-ray; 1.60 A; A=29-395.
PDB; 1D3H; X-ray; 1.80 A; A=29-395.
PDB; 2B0M; X-ray; 2.00 A; A=29-395.
PDB; 2BXV; X-ray; 2.15 A; A=29-395.
PDB; 2FPT; X-ray; 2.40 A; A=29-395.
PDB; 2FPV; X-ray; 1.80 A; A=29-395.
PDB; 2FPY; X-ray; 2.00 A; A=29-395.
PDB; 2FQI; X-ray; 1.95 A; A=29-395.
PDB; 2PRH; X-ray; 2.40 A; A=29-395.
PDB; 2PRL; X-ray; 2.10 A; A=29-395.
PDB; 2PRM; X-ray; 3.00 A; A=29-395.
PDB; 2WV8; X-ray; 1.90 A; A=31-395.
PDB; 3F1Q; X-ray; 2.00 A; A=29-395.
PDB; 3FJ6; X-ray; 1.80 A; A=29-395.
PDB; 3FJL; X-ray; 1.90 A; A=29-395.
PDB; 3G0U; X-ray; 2.00 A; A=29-395.
PDB; 3G0X; X-ray; 1.80 A; A=29-395.
PDB; 3KVJ; X-ray; 1.94 A; A=29-395.
PDB; 3KVK; X-ray; 2.05 A; A=29-395.
PDB; 3KVL; X-ray; 1.85 A; A=29-395.
PDB; 3KVM; X-ray; 2.00 A; A=29-395.
PDB; 3U2O; X-ray; 2.18 A; A=1-395.
PDB; 3W7R; X-ray; 1.68 A; A=29-395.
PDB; 3ZWS; X-ray; 1.60 A; A=29-395.
PDB; 3ZWT; X-ray; 1.55 A; A=29-395.
PDB; 4IGH; X-ray; 1.30 A; A=32-395.
PDB; 4JGD; X-ray; 2.05 A; A=29-395.
PDB; 4JS3; X-ray; 2.00 A; A=29-395.
PDB; 4JTS; X-ray; 2.21 A; A=29-395.
PDB; 4JTT; X-ray; 2.10 A; A=29-395.
PDB; 4JTU; X-ray; 1.90 A; A=29-395.
PDB; 4LS0; X-ray; 2.07 A; A=29-395.
PDB; 4LS1; X-ray; 2.20 A; A=29-395.
PDB; 4LS2; X-ray; 2.27 A; A=29-395.
PDB; 4OQV; X-ray; 1.23 A; A=32-395.
PDB; 4RK8; X-ray; 2.22 A; A=29-395.
PDB; 4RKA; X-ray; 2.71 A; A=29-395.
PDB; 4RLI; X-ray; 2.50 A; A=29-395.
PDB; 4RR4; X-ray; 2.38 A; A=29-395.
PDB; 4YLW; X-ray; 1.79 A; A=29-395.
PDB; 4ZL1; X-ray; 1.86 A; A=29-395.
PDB; 4ZMG; X-ray; 1.90 A; A=29-395.
PDB; 5H2Z; X-ray; 1.58 A; A=29-395.
PDB; 5H73; X-ray; 1.58 A; A=29-395.
PDB; 5HIN; X-ray; 1.60 A; A=29-395.
PDB; 5HQE; X-ray; 1.62 A; A=29-395.
PDB; 5K9C; X-ray; 1.66 A; A=29-395.
PDB; 5K9D; X-ray; 1.70 A; A=29-395.
PDB; 5MUT; X-ray; 1.75 A; A=31-395.
PDB; 5MVC; X-ray; 1.85 A; A=29-395.
PDB; 5MVD; X-ray; 1.95 A; A=33-395.
PDB; 5TCE; NMR; -; A=32-65.
PDB; 6ET4; X-ray; 1.70 A; A=29-395.
PDBsum; 1D3G; -.
PDBsum; 1D3H; -.
PDBsum; 2B0M; -.
PDBsum; 2BXV; -.
PDBsum; 2FPT; -.
PDBsum; 2FPV; -.
PDBsum; 2FPY; -.
PDBsum; 2FQI; -.
PDBsum; 2PRH; -.
PDBsum; 2PRL; -.
PDBsum; 2PRM; -.
PDBsum; 2WV8; -.
PDBsum; 3F1Q; -.
PDBsum; 3FJ6; -.
PDBsum; 3FJL; -.
PDBsum; 3G0U; -.
PDBsum; 3G0X; -.
PDBsum; 3KVJ; -.
PDBsum; 3KVK; -.
PDBsum; 3KVL; -.
PDBsum; 3KVM; -.
PDBsum; 3U2O; -.
PDBsum; 3W7R; -.
PDBsum; 3ZWS; -.
PDBsum; 3ZWT; -.
PDBsum; 4IGH; -.
PDBsum; 4JGD; -.
PDBsum; 4JS3; -.
PDBsum; 4JTS; -.
PDBsum; 4JTT; -.
PDBsum; 4JTU; -.
PDBsum; 4LS0; -.
PDBsum; 4LS1; -.
PDBsum; 4LS2; -.
PDBsum; 4OQV; -.
PDBsum; 4RK8; -.
PDBsum; 4RKA; -.
PDBsum; 4RLI; -.
PDBsum; 4RR4; -.
PDBsum; 4YLW; -.
PDBsum; 4ZL1; -.
PDBsum; 4ZMG; -.
PDBsum; 5H2Z; -.
PDBsum; 5H73; -.
PDBsum; 5HIN; -.
PDBsum; 5HQE; -.
PDBsum; 5K9C; -.
PDBsum; 5K9D; -.
PDBsum; 5MUT; -.
PDBsum; 5MVC; -.
PDBsum; 5MVD; -.
PDBsum; 5TCE; -.
PDBsum; 6ET4; -.
ProteinModelPortal; Q02127; -.
SMR; Q02127; -.
BioGrid; 108068; 16.
IntAct; Q02127; 2.
STRING; 9606.ENSP00000219240; -.
BindingDB; Q02127; -.
ChEMBL; CHEMBL1966; -.
DrugBank; DB07561; (2Z)-2-cyano-N-(3'-ethoxybiphenyl-4-yl)-3-hydroxybut-2-enamide.
DrugBank; DB08172; (2Z)-N-(3-chloro-2'-methoxybiphenyl-4-yl)-2-cyano-3-hydroxybut-2-enamide.
DrugBank; DB08169; (2Z)-N-biphenyl-4-yl-2-cyano-3-cyclopropyl-3-hydroxyprop-2-enamide.
DrugBank; DB07443; (2Z)-N-biphenyl-4-yl-2-cyano-3-hydroxybut-2-enamide.
DrugBank; DB07976; 3-{[(3-FLUORO-3'-METHOXYBIPHENYL-4-YL)AMINO]CARBONYL}THIOPHENE-2-CARBOXYLIC ACID.
DrugBank; DB03805; Antiproliferative Agent A771726.
DrugBank; DB01117; Atovaquone.
DrugBank; DB03480; Brequinar Analog.
DrugBank; DB04147; Lauryl Dimethylamine-N-Oxide.
DrugBank; DB01097; Leflunomide.
DrugBank; DB02262; Orotic Acid.
DrugBank; DB03247; Riboflavin Monophosphate.
DrugBank; DB05125; SC12267.
DrugBank; DB08880; Teriflunomide.
GuidetoPHARMACOLOGY; 2604; -.
iPTMnet; Q02127; -.
PhosphoSitePlus; Q02127; -.
BioMuta; DHODH; -.
DMDM; 56405372; -.
EPD; Q02127; -.
MaxQB; Q02127; -.
PaxDb; Q02127; -.
PeptideAtlas; Q02127; -.
PRIDE; Q02127; -.
TopDownProteomics; Q02127; -.
Ensembl; ENST00000219240; ENSP00000219240; ENSG00000102967.
GeneID; 1723; -.
KEGG; hsa:1723; -.
UCSC; uc002fbp.4; human.
CTD; 1723; -.
DisGeNET; 1723; -.
EuPathDB; HostDB:ENSG00000102967.11; -.
GeneCards; DHODH; -.
HGNC; HGNC:2867; DHODH.
HPA; HPA010123; -.
HPA; HPA011942; -.
MalaCards; DHODH; -.
MIM; 126064; gene.
MIM; 263750; phenotype.
neXtProt; NX_Q02127; -.
OpenTargets; ENSG00000102967; -.
Orphanet; 246; Postaxial acrofacial dysostosis.
PharmGKB; PA27327; -.
eggNOG; KOG1436; Eukaryota.
eggNOG; COG0167; LUCA.
GeneTree; ENSGT00500000044924; -.
HOGENOM; HOG000225103; -.
HOVERGEN; HBG006898; -.
InParanoid; Q02127; -.
KO; K00254; -.
OMA; LQNAMGF; -.
OrthoDB; EOG091G07JK; -.
PhylomeDB; Q02127; -.
TreeFam; TF105973; -.
BRENDA; 1.3.5.2; 2681.
BRENDA; 1.3.98.1; 2681.
Reactome; R-HSA-500753; Pyrimidine biosynthesis.
SABIO-RK; Q02127; -.
UniPathway; UPA00070; UER00946.
ChiTaRS; DHODH; human.
EvolutionaryTrace; Q02127; -.
GenomeRNAi; 1723; -.
PRO; PR:Q02127; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000102967; -.
CleanEx; HS_DHODH; -.
ExpressionAtlas; Q02127; baseline and differential.
Genevisible; Q02127; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0004152; F:dihydroorotate dehydrogenase activity; TAS:Reactome.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0010181; F:FMN binding; IEA:Ensembl.
GO; GO:0048039; F:ubiquinone binding; IEA:Ensembl.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:Ensembl.
GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0046134; P:pyrimidine nucleoside biosynthetic process; TAS:Reactome.
GO; GO:0090140; P:regulation of mitochondrial fission; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:1903576; P:response to L-arginine; IEA:Ensembl.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
CDD; cd04738; DHOD_2_like; 1.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR005720; Dihydroorotate_DH.
InterPro; IPR005719; Dihydroorotate_DH_2.
InterPro; IPR001295; Dihydroorotate_DH_CS.
Pfam; PF01180; DHO_dh; 1.
TIGRFAMs; TIGR01036; pyrD_sub2; 1.
PROSITE; PS00911; DHODEHASE_1; 1.
PROSITE; PS00912; DHODEHASE_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disease mutation; Flavoprotein; FMN;
Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
Polymorphism; Pyrimidine biosynthesis; Reference proteome;
Transit peptide; Transmembrane; Transmembrane helix.
CHAIN 1 395 Dihydroorotate dehydrogenase (quinone),
mitochondrial.
/FTId=PRO_0000029884.
TRANSIT 1 10 Mitochondrion; not cleaved.
{ECO:0000250}.
TOPO_DOM 1 10 Mitochondrial matrix. {ECO:0000250}.
TRANSMEM 11 30 Helical. {ECO:0000250}.
TOPO_DOM 31 395 Mitochondrial intermembrane.
{ECO:0000250}.
NP_BIND 95 99 FMN. {ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
NP_BIND 355 356 FMN. {ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
REGION 144 148 Substrate binding.
REGION 211 216 Substrate binding.
REGION 283 284 Substrate binding.
ACT_SITE 214 214 Nucleophile.
BINDING 99 99 Substrate.
BINDING 119 119 FMN. {ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
BINDING 180 180 FMN. {ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
BINDING 211 211 FMN. {ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
BINDING 254 254 FMN. {ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
BINDING 282 282 FMN; via carbonyl oxygen.
{ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
BINDING 305 305 FMN; via amide nitrogen.
{ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
BINDING 334 334 FMN; via amide nitrogen.
{ECO:0000269|PubMed:10673429,
ECO:0000269|PubMed:16480261}.
VARIANT 7 7 K -> Q (in dbSNP:rs3213422).
{ECO:0000269|PubMed:1446837,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_022094.
VARIANT 19 19 G -> E (in POADS; dbSNP:rs267606765).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062412.
VARIANT 135 135 R -> C (in POADS; dbSNP:rs201230446).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062413.
VARIANT 152 152 G -> R (in POADS; dbSNP:rs267606766).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062414.
VARIANT 199 199 R -> C (in POADS; dbSNP:rs267606769).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062415.
VARIANT 202 202 G -> A (in POADS; dbSNP:rs267606767).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062416.
VARIANT 202 202 G -> D (in POADS; dbSNP:rs267606767).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062417.
VARIANT 244 244 R -> W (in POADS; dbSNP:rs267606768).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062418.
VARIANT 284 284 T -> I (in POADS).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062419.
VARIANT 346 346 R -> W (in POADS; dbSNP:rs201947120).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062420.
VARIANT 392 392 D -> G (in POADS; dbSNP:rs779076692).
{ECO:0000269|PubMed:19915526}.
/FTId=VAR_062421.
CONFLICT 1 2 MA -> KLP (in Ref. 1; AAA50163).
{ECO:0000305}.
HELIX 34 39 {ECO:0000244|PDB:4OQV}.
HELIX 41 48 {ECO:0000244|PDB:4OQV}.
HELIX 51 63 {ECO:0000244|PDB:4OQV}.
HELIX 76 78 {ECO:0000244|PDB:4OQV}.
STRAND 80 82 {ECO:0000244|PDB:4OQV}.
STRAND 85 93 {ECO:0000244|PDB:4OQV}.
TURN 95 100 {ECO:0000244|PDB:5K9D}.
STRAND 101 103 {ECO:0000244|PDB:3ZWT}.
HELIX 104 109 {ECO:0000244|PDB:4OQV}.
STRAND 113 120 {ECO:0000244|PDB:4OQV}.
STRAND 133 136 {ECO:0000244|PDB:4OQV}.
HELIX 137 139 {ECO:0000244|PDB:4OQV}.
STRAND 141 144 {ECO:0000244|PDB:4OQV}.
HELIX 153 161 {ECO:0000244|PDB:4OQV}.
HELIX 164 172 {ECO:0000244|PDB:4OQV}.
STRAND 177 181 {ECO:0000244|PDB:4OQV}.
HELIX 190 201 {ECO:0000244|PDB:4OQV}.
HELIX 202 204 {ECO:0000244|PDB:4OQV}.
STRAND 206 212 {ECO:0000244|PDB:4OQV}.
HELIX 220 224 {ECO:0000244|PDB:3ZWT}.
HELIX 226 241 {ECO:0000244|PDB:4OQV}.
HELIX 245 247 {ECO:0000244|PDB:4OQV}.
STRAND 250 255 {ECO:0000244|PDB:4OQV}.
HELIX 261 274 {ECO:0000244|PDB:4OQV}.
STRAND 278 281 {ECO:0000244|PDB:4OQV}.
STRAND 285 287 {ECO:0000244|PDB:5K9C}.
TURN 295 298 {ECO:0000244|PDB:4OQV}.
STRAND 299 305 {ECO:0000244|PDB:4OQV}.
HELIX 306 308 {ECO:0000244|PDB:4OQV}.
HELIX 309 322 {ECO:0000244|PDB:4OQV}.
TURN 323 325 {ECO:0000244|PDB:4OQV}.
STRAND 329 334 {ECO:0000244|PDB:4OQV}.
HELIX 338 347 {ECO:0000244|PDB:4OQV}.
STRAND 349 355 {ECO:0000244|PDB:4OQV}.
HELIX 356 361 {ECO:0000244|PDB:4OQV}.
HELIX 364 379 {ECO:0000244|PDB:4OQV}.
HELIX 385 388 {ECO:0000244|PDB:4OQV}.
HELIX 391 393 {ECO:0000244|PDB:4OQV}.
SEQUENCE 395 AA; 42867 MW; 072C3169E78C6440 CRC64;
MAWRHLKKRA QDAVIILGGG GLLFASYLMA TGDERFYAEH LMPTLQGLLD PESAHRLAVR
FTSLGLLPRA RFQDSDMLEV RVLGHKFRNP VGIAAGFDKH GEAVDGLYKM GFGFVEIGSV
TPKPQEGNPR PRVFRLPEDQ AVINRYGFNS HGLSVVEHRL RARQQKQAKL TEDGLPLGVN
LGKNKTSVDA AEDYAEGVRV LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER
DGLRRVHRPA VLVKIAPDLT SQDKEDIASV VKELGIDGLI VTNTTVSRPA GLQGALRSET
GGLSGKPLRD LSTQTIREMY ALTQGRVPII GVGGVSSGQD ALEKIRAGAS LVQLYTALTF
WGPPVVGKVK RELEALLKEQ GFGGVTDAIG ADHRR


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