UniProt Accession

 PYRD_YEAST; P28272; D6VWY7; Q2XN75; Q70DC7 

Genbank Protein ID

 M83295; X59371; AJ585637; AJ585638; AJ585639; AJ585640; AJ585641; AJ585642; AJ585643; AJ585644; AJ585645; AJ585646; AJ585647; AJ585648; AJ585649; AJ585650; AJ585651; X75951; Z28216; BK006944 

Genbank Nucleotide ID

 AAA34566.1; CAA42014.1; CAE52157.1; CAE52158.1; CAE52159.1; CAE52160.1; CAE52161.1; CAE52162.1; CAE52163.1; CAE52164.1; CAE52165.1; CAE52166.1; CAE52167.1; CAE52168.1; CAE52169.1; CAE52170.1; CAE52171.1; CAA53557.1; CAA82061.1; DAA08953.1 

Protein Name

 Dihydroorotate dehydrogenase (fumarate) 

Protein Synonyms/Alias

 DHOD; DHODase; DHOdehase; Dihydroorotate oxidase 

Gene Name

 URA1 

Gene Synonyms/Alias

 YKL216W 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
46	KAGAFITKSATTLER	acetylation	[1]
46	KAGAFITKSATTLER	ubiquitination	[2, 3]
155	LTKETLEKVFAFFKK	acetylation	[1]
161	EKVFAFFKKPLGVKL	acetylation	[1]
216	ESVVVKPKNGFGGIG	acetylation	[1]
247	TRLRPEIKVIGTGGI	acetylation	[1]
283	ELQKEGVKIFERIEK	acetylation	[1]
293	ERIEKELKDIMEAKG	acetylation	[1]
293	ERIEKELKDIMEAKG	ubiquitination	[3]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 

Functional Description

 Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. Does not use oxaloacetate or NAD or NADP as electron acceptors. 

Sequence Annotation

 NP_BIND 46 47 FMN (By similarity).
 NP_BIND 252 253 FMN (By similarity).
 NP_BIND 274 275 FMN (By similarity).
 REGION 70 74 Substrate binding (By similarity).
 REGION 196 197 Substrate binding (By similarity).
 ACT_SITE 132 132 Nucleophile (By similarity).
 BINDING 46 46 Substrate (By similarity).
 BINDING 130 130 FMN (By similarity).
 BINDING 130 130 Substrate (By similarity).
 BINDING 167 167 FMN (By similarity).
 BINDING 195 195 FMN; via carbonyl oxygen (By similarity).
 BINDING 224 224 FMN; via amide nitrogen (By similarity).  

Keyword

 Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 314 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0019898; C:extrinsic to membrane; IDA:SGD.
 GO:0004152; F:dihydroorotate dehydrogenase activity; IDA:SGD.
 GO:0052888; F:dihydroorotate oxidase (fumarate) activity; IEA:EC.
 GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
 GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:SGD.
 GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. 

Interpro

 IPR013785; Aldolase_TIM.
 IPR005720; Dihydroorotate_DH.
 IPR024920; Dihydroorotate_DH_1.
 IPR012135; Dihydroorotate_DH_1_2.
 IPR001295; Dihydroorotate_DH_CS. 

Pfam

 PF01180; DHO_dh 

SMART

  

PROSITE

 PS00911; DHODEHASE_1
 PS00912; DHODEHASE_2 

PRINTS