ID A0A0D3ETY7_9ORYZ Unreviewed; 407 AA.
AC A0A0D3ETY7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=dihydroorotase {ECO:0000256|ARBA:ARBA00012860};
DE EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART01G30690.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART01G30690.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART01G30690.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART01G30690.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004880}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class II DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00005631}.
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DR AlphaFoldDB; A0A0D3ETY7; -.
DR STRING; 65489.A0A0D3ETY7; -.
DR PaxDb; 65489-OBART01G30690-1; -.
DR EnsemblPlants; OBART01G30690.1; OBART01G30690.1; OBART01G30690.
DR Gramene; OBART01G30690.1; OBART01G30690.1; OBART01G30690.
DR eggNOG; KOG2902; Eukaryota.
DR HOGENOM; CLU_041558_1_0_1; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000026960; Chromosome 1.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd01294; DHOase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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 NCBIfam; TIGR00856; pyrC_dimer; 1.
DR PANTHER; PTHR43137; DIHYDROOROTASE; 1.
DR PANTHER; PTHR43137:SF1; DIHYDROOROTASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 68..379
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 407 AA; 44968 MW; BE942CB16998593F CRC64;
MQTAATSTFF ANPHVKHLPG PFLRPSPHYG ALVHLPSFRN KTPISIAMAA SPSPPPPLQE
LTITRPDDWH LHLREGDVLA AVLPHSAMHF GRAIVMPNLK PPVTTTARAL EYREEILRAL
PPGSNFVPLM TLYLTDNTSP EEIKLAKKSG VVFAVKLYPS GATTNSQDGV TDIFGKCLPV
LEEMARQEMP LLVHGEVTDQ HVDTFDREKV FIEKILAPLV QRLPQLKIVM EHITTMDAVN
FVESCKEGHV AATVTPQHLL LNRNALFQGG LQPHNYCLPV LKRETHRQAI VSAVTSGSKQ
YFLGTDSAPH DKRRKECSCG CAGIYSAPVA LSLYAKVFEQ AGALDKLEAF TSFNGPDFYG
LPRNTSKIVL RKSAWKVPDT YSYSSGEIVP MFTGNTLEWL PSDQLEE
//