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Database: UniProt
Entry: Q5E9W3
LinkDB: Q5E9W3
Original site: Q5E9W3 
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   19-FEB-2014, entry version 68.
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   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   SABIO-RK; Q5E9W3; -.
DR   UniPathway; UPA00070; UER00946.
DR   NextBio; 20876177; -.
DR   GO; GO:0016021; C:integral component of 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   HAMAP; MF_00225; DHO_dh_type2; 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
//
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