PYRC_RUBXD
ID PYRC_RUBXD Reviewed; 436 AA.
AC Q1AVY7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00220};
DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00220};
DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00220};
GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00220}; OrderedLocusNames=Rxyl_1479;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00220};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00220}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00220}.
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DR EMBL; CP000386; ABG04441.1; -; Genomic_DNA.
DR RefSeq; WP_011564458.1; NC_008148.1.
DR AlphaFoldDB; Q1AVY7; -.
DR SMR; Q1AVY7; -.
DR STRING; 266117.Rxyl_1479; -.
DR PRIDE; Q1AVY7; -.
DR EnsemblBacteria; ABG04441; ABG04441; Rxyl_1479.
DR KEGG; rxy:Rxyl_1479; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_1_0_11; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 1319925at2; -.
DR PhylomeDB; Q1AVY7; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000006637; Chromosome.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01317; DHOase_IIa; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_00220_B; PyrC_classI_B; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004722; DHOase.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..436
FT /note="Dihydroorotase"
FT /id="PRO_0000325595"
FT ACT_SITE 309
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 68..70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 327..328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ SEQUENCE 436 AA; 45111 MW; 1278C6F572A4CEC0 CRC64;
MSTRSGSAAE LAIRGAHVVD PSSGLDGVTD VVVRGGRVAA VGRGRPAARE LDASGLFLFP
GFVDLHAHWR TPGREDEEDL ESGSSAAAAG GFTGVVMMPN TDPVLDRPAL VSGLVRRAER
ESRVRAFVAA ALHAGLAGER LTEMRLLKEA GALCVSDDGL GTQSAGVLRN GMLYARSAGL
PVILHCEDRT LATGAVHEGA AAALAGVPGT PASAEDVATA AALVLAAETG ARVHITHVST
ALSAALVGFF RGRAAVTADT TPHHTTLTDE LVFALDGLFR VNPPLRPGSD REGVVGALRD
GILDFVATDH APHAPEEKEL PLEEAAPGFL GHETAFAALY TGLVLEGRLS LGRLVEAMSC
GPGRWVGGLG SLSPGSPADL ALVDLGEEWT VSRRTLASRS SNSPYLGRRL RGRVVGTMVG
GEMVYDRMGA RLGVRT
