PYRC_USTMA
ID PYRC_USTMA Reviewed; 394 AA.
AC P31301; A0A0D1E3G2; Q4PEE2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=PYR3; ORFNames=UMAG_01521;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=1353740; DOI=10.1016/0378-1119(92)90492-8;
RA Spanos A., Kanuga N., Holden D.W., Banks G.R.;
RT "The Ustilago maydis pyr3 gene: sequence and transcriptional analysis.";
RL Gene 117:73-79(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P05020};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P05020};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC -!- INDUCTION: By N-carbamoyl-L-aspartate.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class II DHOase subfamily. {ECO:0000305}.
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DR EMBL; X63181; CAA44866.1; -; Genomic_DNA.
DR EMBL; CM003142; KIS70351.1; -; Genomic_DNA.
DR PIR; JQ1667; DEUSO.
DR RefSeq; XP_011387556.1; XM_011389254.1.
DR AlphaFoldDB; P31301; -.
DR SMR; P31301; -.
DR STRING; 5270.UM01521P0; -.
DR EnsemblFungi; KIS70351; KIS70351; UMAG_01521.
DR GeneID; 23562504; -.
DR KEGG; uma:UMAG_01521; -.
DR VEuPathDB; FungiDB:UMAG_01521; -.
DR eggNOG; KOG2902; Eukaryota.
DR HOGENOM; CLU_041558_0_0_1; -.
DR InParanoid; P31301; -.
DR OMA; TLHHISM; -.
DR OrthoDB; 719800at2759; -.
DR BRENDA; 3.5.2.3; 6587.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000000561; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd01294; DHOase; 1.
DR HAMAP; MF_00219; PyrC_classII; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004721; DHOdimr.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43137; PTHR43137; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001237; DHOdimr; 1.
DR SUPFAM; SSF51556; SSF51556; 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 Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..394
FT /note="Dihydroorotase"
FT /id="PRO_0000147291"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT MOD_RES 98
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P05020"
FT CONFLICT 12
FT /note="A -> G (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 63..65
FT /note="RAL -> AAV (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..89
FT /note="KA -> EG (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="I -> M (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="A -> D (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="G -> A (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..301
FT /note="CA -> WP (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="S -> C (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="A -> R (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..390
FT /note="GKCLGWE -> VSAG (in Ref. 1; CAA44866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 42837 MW; 400DFA2BE435DFB8 CRC64;
MSVQEITIPA PADFHVHLRQ GKMSELVTPH VAEGGVSLAY VMPNLVPPIT STQQAMEYLE
RLRALAPQTM FVGTLYLSPD LTPAEIAKAA QNGVRGVKSY PRGVTTNSDS GIEDYETYYP
IFEEMQKHDM VLNLHGELPS NADAGICVLN AEEKFLTHLF KIHGEFPKLK IVLEHATTRK
AVEAVKQCGD TVGCTITPHH LELIVDDWAG KPLNFCKPVA KYPDDRQALR DVIRQGHPRF
FLGSDSAPHP LANKYPSAVT HGAPGTKASA SGSDHLEATG VVSCGCAAGV YTSSILVPLC
ATLLEAFGAL DQLANYVSIN GRNFYGYNDD QHAKHGSIKL RKVRSRSSIS PAAATVPAVY
VHPEFREVPD SDASKVQVVP FWAGKCLGWE IVRS
