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UniProtKB/Swiss-Prot entry O04904


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYRC_ARATH
Primary accession number O04904
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 72)
Name and origin of the protein
Protein name Dihydroorotase, mitochondrial [Precursor]
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: PYR4
OrderedLocusNames: At4g22930
ORFNames: F7H19.110
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Zhou L., Lacroute F., Thornburg R.W.;
"Characterization of the Arabidopsis thaliana cDNA encoding dihydroorotase.";
(er) Plant Gene Register PGR97-115.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF000146; AAB71134.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031018; CAA19808.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161558; CAB79248.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05124; T05124.
RefSeq NP_194024.1; -.
UniGene At.2374
3D structure databases
HSSP P05020; 1J79. [HSSP ENTRY / PDB]
ModBase O04904.
Organism-specific databases
TAIR At4g22930; -.
Gene expression databases
ArrayExpress O04904; -.
GermOnline AT4G22930; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from direct assay from TAIR).
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0004151; Molecular function: dihydroorotase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019856; Biological process: pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006680; Amidohydro_1.
IPR004721; DHOdimr.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001237; DHOdimr; 1.
TIGRFAMs TIGR00856; pyrC_dimer; 1.
PROSITE PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
Proteomics databases
PRIDE O04904; -.
Genome annotation databases
GeneID 828392; -.
GenomeReviews CT486007_GR; AT4G22930.
KEGG ath:AT4G22930; -.
NMPDR fig|3702.1.peg.20157; -.
Other
ProtoNet O04904.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Mitochondrion; Pyrimidine biosynthesis; Transit peptide; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   377        Dihydroorotase, mitochondrial. PRO_0000029883
METAL   44    44        Zinc 1 (By similarity). 
METAL   46    46        Zinc 1 (By similarity). 
METAL   130   130        Zinc 1; via carbamate group (By similarity). 
METAL   130   130        Zinc 2; via carbamate group (By similarity). 
METAL   168   168        Zinc 2 (By similarity). 
METAL   206   206        Zinc 2 (By similarity). 
METAL   280   280        Zinc 1 (By similarity). 
MOD_RES   130   130        N6-carboxylysine (By similarity). 
Sequence information
Length: 377 AA [This is the length of the unprocessed precursor] Molecular weight: 41950 Da [This is the MW of the unprocessed precursor] CRC64: 783C22BE5581DEDB [This is a checksum on the sequence]
        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 

O04904 in FASTA format

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