Reviewed, UniProtKB/Swiss-Prot O04904 (PYRC_ARATH)

Names and origin

Protein names

Recommended name:
    Dihydroorotase, mitochondrial
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	PYR4
Ordered Locus Names:	At4g22930
ORF Names:	F7H19.110

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6.
Subcellular location	Mitochondrion Potential.
Sequence similarities	Belongs to the DHOase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydroorotase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 377		Dihydroorotase, mitochondrial		PRO_0000029883
Sites
	Metal binding	44	1	Zinc 1 By similarity
	Metal binding	46	1	Zinc 1 By similarity
	Metal binding	130	1	Zinc 1; via carbamate group By similarity
	Metal binding	130	1	Zinc 2; via carbamate group By similarity
	Metal binding	168	1	Zinc 2 By similarity
	Metal binding	206	1	Zinc 2 By similarity
	Metal binding	280	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	130	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O04904-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 783C22BE5581DEDB	FASTA	377	41,950
	10 20 30 40 50 60 MIKTLVSPYS GFGSQKLKFD RSSEKVKTRA VRMELTITQP DDWHLHLRDG DLLHAVVPHS 70 80 90 100 110 120 ASNFKRAIVM PNLKPPVTST AAAIIYRKFI MKALPSESSF DPLMTLYLTD KTLPEEIRLA 130 140 150 160 170 180 RESGVVYAVK LYPAGATTNS QDGVTDLFGK CLPVLEEMVK QNMPLLVHGE VTDPSIDVFD 190 200 210 220 230 240 REKIFIETVL QPLIQRLPQL KVVMEHITTM DAVNFVESCK EGSVGATVTP QHLLLNRNAL 250 260 270 280 290 300 FQGGLQPHNY CLPVLKREIH REAIVKAVTS GSKKFFLGTD SAPHERSRKE SSCGCAGIYS 310 320 330 340 350 360 APIALSLYAK VFDEAGALDK LEAFTSFNGP DFYGLPRNSS KITLKKSPWK VPDVFNFPFG 370 EIVPMFAGET LQWQPLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the Arabidopsis thaliana cDNA encoding dihydroorotase." Zhou L., Lacroute F., Thornburg R.W. Plant Gene Register PGR97-115 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF000146 mRNA. Translation: AAB71134.1. AL031018 Genomic DNA. Translation: CAA19808.1. AL161558 Genomic DNA. Translation: CAB79248.1.
IPI	IPI00535140.
PIR	T05124.
RefSeq	NP_194024.1.
UniGene	At.2374
3D structure databases
HSSP	HSSP built from PDB template 1J79 based on UniProtKB P05020.
ModBase	Search...
Proteomic databases
PRIDE	O04904.
Genome annotation databases
GeneID	828392.
GenomeReviews	Gene locus AT4G22930 in contig CT486007_GR.
KEGG	ath:AT4G22930.
NMPDR	fig|3702.1.peg.20157.
Organism-specific databases
TAIR	At4g22930.
Phylogenomic databases
OMA	O04904. IMPNLVP.
Enzyme and pathway databases
BRENDA	3.5.2.3. 302.
Gene expression databases
ArrayExpress	O04904.
GermOnline	AT4G22930. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR004721. DHOdimr. IPR002195. Dihydroorotase_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
PIRSF	PIRSF001237. DHOdimr. 1 hit.
TIGRFAMs	TIGR00856. pyrC_dimer. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_ARATH

Accession

Primary (citable) accession number: O04904

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)