ID   PYRC_ARATH              Reviewed;         377 AA.
AC   O04904;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=Dihydroorotase, mitochondrial;
DE            Short=DHOase;
DE            EC=3.5.2.3;
DE   Flags: Precursor;
GN   Name=PYR4; OrderedLocusNames=At4g22930; ORFNames=F7H19.110;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Zhou L., Lacroute F., Thornburg R.W.;
RT   "Characterization of the Arabidopsis thaliana cDNA encoding
RT   dihydroorotase.";
RL   (er) Plant Gene Register PGR97-115.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 3/6.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- SIMILARITY: Belongs to the DHOase family.
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DR   EMBL; AF000146; AAB71134.1; -; mRNA.
DR   EMBL; AL031018; CAA19808.1; -; Genomic_DNA.
DR   EMBL; AL161558; CAB79248.1; -; Genomic_DNA.
DR   IPI; IPI00535140; -.
DR   PIR; T05124; T05124.
DR   RefSeq; NP_194024.1; -.
DR   UniGene; At.2374; -.
DR   HSSP; P05020; 1J79.
DR   PRIDE; O04904; -.
DR   GeneID; 828392; -.
DR   GenomeReviews; CT486007_GR; AT4G22930.
DR   KEGG; ath:AT4G22930; -.
DR   NMPDR; fig|3702.1.peg.20157; -.
DR   TAIR; At4g22930; -.
DR   OMA; O04904; IMPNLVP.
DR   BRENDA; 3.5.2.3; 302.
DR   ArrayExpress; O04904; -.
DR   GermOnline; AT4G22930; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019856; P:pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF001237; DHOdimr; 1.
DR   TIGRFAMs; TIGR00856; pyrC_dimer; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Hydrolase; Metal-binding; Mitochondrion;
KW   Pyrimidine biosynthesis; Transit peptide; Zinc.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    377       Dihydroorotase, mitochondrial.
FT                                /FTId=PRO_0000029883.
FT   METAL        44     44       Zinc 1 (By similarity).
FT   METAL        46     46       Zinc 1 (By similarity).
FT   METAL       130    130       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       130    130       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       168    168       Zinc 2 (By similarity).
FT   METAL       206    206       Zinc 2 (By similarity).
FT   METAL       280    280       Zinc 1 (By similarity).
FT   MOD_RES     130    130       N6-carboxylysine (By similarity).
SQ   SEQUENCE   377 AA;  41950 MW;  783C22BE5581DEDB CRC64;
     MIKTLVSPYS GFGSQKLKFD RSSEKVKTRA VRMELTITQP DDWHLHLRDG DLLHAVVPHS
     ASNFKRAIVM PNLKPPVTST AAAIIYRKFI MKALPSESSF DPLMTLYLTD KTLPEEIRLA
     RESGVVYAVK LYPAGATTNS QDGVTDLFGK CLPVLEEMVK QNMPLLVHGE VTDPSIDVFD
     REKIFIETVL QPLIQRLPQL KVVMEHITTM DAVNFVESCK EGSVGATVTP QHLLLNRNAL
     FQGGLQPHNY CLPVLKREIH REAIVKAVTS GSKKFFLGTD SAPHERSRKE SSCGCAGIYS
     APIALSLYAK VFDEAGALDK LEAFTSFNGP DFYGLPRNSS KITLKKSPWK VPDVFNFPFG
     EIVPMFAGET LQWQPLK
//