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Protein

Dihydroorotase, mitochondrial

Gene

PYR4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain, chloroplastic (CARB), Carbamoyl-phosphate synthase small chain, chloroplastic (CARA)
  2. Aspartate carbamoyltransferase, chloroplastic (PYRB)
  3. Dihydroorotase, mitochondrial (PYR4)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Zinc 1; via tele nitrogenBy similarity
Metal bindingi46 – 461Zinc 1; via tele nitrogenBy similarity
Metal bindingi130 – 1301Zinc 1; via carbamate groupBy similarity
Metal bindingi130 – 1301Zinc 2; via carbamate groupBy similarity
Metal bindingi168 – 1681Zinc 2; via pros nitrogenBy similarity
Metal bindingi206 – 2061Zinc 2; via tele nitrogenBy similarity
Metal bindingi280 – 2801Zinc 1By similarity

GO - Molecular functioni

  • dihydroorotase activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G22930-MONOMER.
BRENDAi3.5.2.3. 399.
UniPathwayiUPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotase, mitochondrial (EC:3.5.2.3)
Short name:
DHOase
Gene namesi
Name:PYR4
Ordered Locus Names:At4g22930
ORF Names:F7H19.110
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G22930.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 377Dihydroorotase, mitochondrialPRO_0000029883
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301N6-carboxylysineBy similarity
Modified residuei223 – 2231PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO04904.
PRIDEiO04904.

PTM databases

iPTMnetiO04904.

Expressioni

Gene expression databases

GenevisibleiO04904. AT.

Interactioni

Protein-protein interaction databases

BioGridi13681. 1 interaction.
STRINGi3702.AT4G22930.1.

Structurei

3D structure databases

ProteinModelPortaliO04904.
SMRiO04904. Positions 35-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Type 1 subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2902. Eukaryota.
COG0418. LUCA.
HOGENOMiHOG000256259.
InParanoidiO04904.
KOiK01465.
OMAiYAEAFEQ.
PhylomeDBiO04904.

Family and domain databases

HAMAPiMF_00219. PyrC_type1.
InterProiIPR006680. Amidohydro-rel.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001237. DHOdimr. 1 hit.
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O04904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKTLVSPYS GFGSQKLKFD RSSEKVKTRA VRMELTITQP DDWHLHLRDG
60 70 80 90 100
DLLHAVVPHS ASNFKRAIVM PNLKPPVTST AAAIIYRKFI MKALPSESSF
110 120 130 140 150
DPLMTLYLTD KTLPEEIRLA RESGVVYAVK LYPAGATTNS QDGVTDLFGK
160 170 180 190 200
CLPVLEEMVK QNMPLLVHGE VTDPSIDVFD REKIFIETVL QPLIQRLPQL
210 220 230 240 250
KVVMEHITTM DAVNFVESCK EGSVGATVTP QHLLLNRNAL FQGGLQPHNY
260 270 280 290 300
CLPVLKREIH REAIVKAVTS GSKKFFLGTD SAPHERSRKE SSCGCAGIYS
310 320 330 340 350
APIALSLYAK VFDEAGALDK LEAFTSFNGP DFYGLPRNSS KITLKKSPWK
360 370
VPDVFNFPFG EIVPMFAGET LQWQPLK
Length:377
Mass (Da):41,950
Last modified:July 1, 1997 - v1
Checksum:i783C22BE5581DEDB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791F → L in BAF00239 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000146 mRNA. Translation: AAB71134.1.
AL031018 Genomic DNA. Translation: CAA19808.1.
AL161558 Genomic DNA. Translation: CAB79248.1.
CP002687 Genomic DNA. Translation: AEE84682.1.
AK228295 mRNA. Translation: BAF00239.1.
PIRiT05124.
RefSeqiNP_194024.1. NM_118422.3.
UniGeneiAt.2374.

Genome annotation databases

EnsemblPlantsiAT4G22930.1; AT4G22930.1; AT4G22930.
GeneIDi828392.
GrameneiAT4G22930.1; AT4G22930.1; AT4G22930.
KEGGiath:AT4G22930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000146 mRNA. Translation: AAB71134.1.
AL031018 Genomic DNA. Translation: CAA19808.1.
AL161558 Genomic DNA. Translation: CAB79248.1.
CP002687 Genomic DNA. Translation: AEE84682.1.
AK228295 mRNA. Translation: BAF00239.1.
PIRiT05124.
RefSeqiNP_194024.1. NM_118422.3.
UniGeneiAt.2374.

3D structure databases

ProteinModelPortaliO04904.
SMRiO04904. Positions 35-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13681. 1 interaction.
STRINGi3702.AT4G22930.1.

PTM databases

iPTMnetiO04904.

Proteomic databases

PaxDbiO04904.
PRIDEiO04904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G22930.1; AT4G22930.1; AT4G22930.
GeneIDi828392.
GrameneiAT4G22930.1; AT4G22930.1; AT4G22930.
KEGGiath:AT4G22930.

Organism-specific databases

TAIRiAT4G22930.

Phylogenomic databases

eggNOGiKOG2902. Eukaryota.
COG0418. LUCA.
HOGENOMiHOG000256259.
InParanoidiO04904.
KOiK01465.
OMAiYAEAFEQ.
PhylomeDBiO04904.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.
BioCyciARA:AT4G22930-MONOMER.
BRENDAi3.5.2.3. 399.

Miscellaneous databases

PROiO04904.

Gene expression databases

GenevisibleiO04904. AT.

Family and domain databases

HAMAPiMF_00219. PyrC_type1.
InterProiIPR006680. Amidohydro-rel.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001237. DHOdimr. 1 hit.
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-377.
    Strain: cv. Columbia.
  5. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
    Aryal U.K., Krochko J.E., Ross A.R.
    J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYRC_ARATH
AccessioniPrimary (citable) accession number: O04904
Secondary accession number(s): Q0WRL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.