PYRC_THET8
ID PYRC_THET8 Reviewed; 426 AA.
AC Q5SK67;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
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};
GN OrderedLocusNames=TTHA0781 {ECO:0000312|EMBL:BAD70604.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:2Z00}
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) IN COMPLEX WITH ZINC, AND COFACTOR.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Kanagawa M., Baba S., Kuramitsu S., Yokoyama S., Kawai G., Sampei G.;
RT "Crystal structure of dihydroorotase from Thermus thermophilus.";
RL Submitted (MAY-2007) to the PDB data bank.
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, ECO:0000269|Ref.2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00220,
CC ECO:0000269|Ref.2};
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, ECO:0000305}.
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DR EMBL; AP008226; BAD70604.1; -; Genomic_DNA.
DR RefSeq; WP_011228195.1; NC_006461.1.
DR RefSeq; YP_144047.1; NC_006461.1.
DR PDB; 2Z00; X-ray; 2.42 A; A=1-426.
DR PDBsum; 2Z00; -.
DR AlphaFoldDB; Q5SK67; -.
DR SMR; Q5SK67; -.
DR STRING; 300852.55772163; -.
DR EnsemblBacteria; BAD70604; BAD70604; BAD70604.
DR GeneID; 3170046; -.
DR KEGG; ttj:TTHA0781; -.
DR PATRIC; fig|300852.9.peg.774; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_1_0_0; -.
DR OMA; QHAQEPR; -.
DR PhylomeDB; Q5SK67; -.
DR UniPathway; UPA00070; UER00117.
DR EvolutionaryTrace; Q5SK67; -.
DR Proteomes; UP000000532; 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; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..426
FT /note="Dihydroorotase"
FT /id="PRO_0000440857"
FT ACT_SITE 306
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00"
FT BINDING 57..59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 324..325
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 14..24
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2Z00"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2Z00"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 202..222
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2Z00"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:2Z00"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2Z00"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:2Z00"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:2Z00"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:2Z00"
SQ SEQUENCE 426 AA; 45694 MW; 753EBA4721371781 CRC64;
MILIRNVRLV DARGERGPAD VLIGEGRILS LEGGEAKQVV DGTGCFLAPG FLDLHAHLRE
PGEEVKEDLF SGLLAAVRGG YTDLVSMPNT KPPVDTPEAV RALKEKAKAL GLARLHPAAA
LTEKQEGKTL TPAGLLREAG AVLLTDDGRT NEDAGVLAAG LLMAAPLGLP VAVHAEDAGL
RRNGVMNDGP LADLLGLPGN PPEAEAARIA RDLEVLRYAL RRSPATPRLH VQHLSTKRGL
ELVREAKRAG LPVTAEATPH HLTLTEEALR TFDPLFKVAP PLRGEEDREA LLEGLLDGTL
DAIATDHAPH TLAEKEKDLL RAPFGIPSLE VAFPLLYTEL HLKRGFPLQR LVELFTDGPR
RVLGLPPLHL EEGAEASLVL LSPKERPVDP SAFASKARYS PWAGWVLGGW PVLTLVAGRI
VHEALK
