ID PYRD_BOVIN Reviewed; 395 AA.
AC Q5E9W3; Q0P590;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-APR-2013, entry version 63.
DE RecName: Full=Dihydroorotate dehydrogenase (quinone), mitochondrial;
DE Short=DHOdehase;
DE EC=1.3.5.2;
DE AltName: Full=Dihydroorotate oxidase;
DE Flags: Precursor;
GN Name=DHODH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=3733756;
RA Hines V., Keys L.D. III, Johnston M.;
RT "Purification and properties of the bovine liver mitochondrial
RT dihydroorotate dehydrogenase.";
RL J. Biol. Chem. 261:11386-11392(1986).
RN [4]
RP ERRATUM.
RA Hines V., Keys L.D. III, Johnston M.;
RL J. Biol. Chem. 262:15322-15322(1987).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME KINETICS.
RX PubMed=2540819; DOI=10.1021/bi00429a040;
RA Hines V., Johnston M.;
RT "Analysis of the kinetic mechanism of the bovine liver mitochondrial
RT dihydroorotate dehydrogenase.";
RL Biochemistry 28:1222-1226(1989).
CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC with quinone as electron acceptor.
CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
CC quinol.
CC -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.2 uM for (S)-dihydroorotate;
CC KM=13.6 uM for benzyl-(S)-dihydroorotate;
CC KM=19.4 uM for methyl-(S)-dihydroorotate;
CC KM=10.8 uM for quinone Q(6);
CC KM=13.2 uM for quinone Q(7);
CC Vmax=72 umol/min/mg enzyme toward (S)-dihydroorotate;
CC Vmax=80 umol/min/mg enzyme toward benzyl-(S)-dihydroorotate;
CC Vmax=63 umol/min/mg enzyme toward methyl-(S)-dihydroorotate;
CC Vmax=82 umol/min/mg enzyme toward quinone Q(6);
CC Vmax=88 umol/min/mg enzyme toward quinone Q(7);
CC pH dependence:
CC Optimum pH is 8.0;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; orotate from (S)-dihydroorotate (quinone route): step
CC 1/1.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC membrane protein (By similarity).
CC -!- PTM: The uncleaved transit peptide is required for mitochondrial
CC targeting and proper membrane integration (By similarity).
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC Type 2 subfamily.
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DR EMBL; BT020807; AAX08824.1; -; mRNA.
DR EMBL; BC120337; AAI20338.1; -; mRNA.
DR IPI; IPI00712226; -.
DR RefSeq; NP_001015650.1; NM_001015650.1.
DR UniGene; Bt.7483; -.
DR ProteinModelPortal; Q5E9W3; -.
DR SMR; Q5E9W3; 30-395.
DR PRIDE; Q5E9W3; -.
DR GeneID; 533873; -.
DR KEGG; bta:533873; -.
DR CTD; 1723; -.
DR eggNOG; COG0167; -.
DR HOGENOM; HOG000225103; -.
DR HOVERGEN; HBG006898; -.
DR InParanoid; Q5E9W3; -.
DR KO; K00254; -.
DR OrthoDB; EOG47WNNW; -.
DR SABIO-RK; Q5E9W3; -.
DR UniPathway; UPA00070; UER00946.
DR NextBio; 20876177; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR InterPro; IPR005719; Dihydroorotate_DH_2.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
DR Pfam; PF01180; DHO_dh; 1.
DR PIRSF; PIRSF000164; DHO_oxidase; 1.
DR TIGRFAMs; TIGR01036; pyrD_sub2; 1.
DR PROSITE; PS00911; DHODEHASE_1; 1.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Flavoprotein; FMN; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Pyrimidine biosynthesis;
KW Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 395 Dihydroorotate dehydrogenase (quinone),
FT mitochondrial.
FT /FTId=PRO_0000233397.
FT TRANSIT 1 10 Mitochondrion; not cleaved (By
FT similarity).
FT TOPO_DOM 1 10 Mitochondrial matrix (By similarity).
FT TRANSMEM 11 30 Helical; (By similarity).
FT TOPO_DOM 31 395 Mitochondrial intermembrane (By
FT similarity).
FT NP_BIND 95 99 FMN (By similarity).
FT NP_BIND 355 356 FMN (By similarity).
FT REGION 144 148 Substrate binding (By similarity).
FT REGION 211 216 Substrate binding (By similarity).
FT REGION 283 284 Substrate binding (By similarity).
FT ACT_SITE 214 214 Nucleophile (By similarity).
FT BINDING 99 99 Substrate (By similarity).
FT BINDING 119 119 FMN (By similarity).
FT BINDING 180 180 FMN (By similarity).
FT BINDING 211 211 FMN (By similarity).
FT BINDING 254 254 FMN (By similarity).
FT BINDING 282 282 FMN; via carbonyl oxygen (By similarity).
FT BINDING 305 305 FMN; via amide nitrogen (By similarity).
FT BINDING 334 334 FMN; via amide nitrogen (By similarity).
SQ SEQUENCE 395 AA; 42776 MW; 9D093C1641A44BD0 CRC64;
MAWRQLKKRA QDAMVILGGG GLLFASYLTA TGDEHFYAEL LMPSLQRLLD PETAHRLAVR
FTSLGLLPRT TFQDSDMLEV RVLGHKFRNP VGIAAGFDKH GEAVDGLYKM GFGFVEIGSV
TPEPQEGNPR PRVFRLPEDQ AIINRYGFNS HGLSVVEHRL RARQQTQARL TEDGLPLGIN
LGKNKTSVDA ASDYAEGVRV LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER
DALKVAHKPA VLVKIAPDLT AQDKEDIASV VRELGIDGLI VTNSTVSRPA SLQGALRSEP
GGLSGKPLRD LSTQTIREMY ALTQGRVPIV GVGGVSSGQD ALEKIRAGAS LVQLYTALTY
RGPPVVGGVK RELEALLKEQ GFARVTDAIG ADHRR
//
