PYRC_ECOLC
ID PYRC_ECOLC Reviewed; 348 AA.
AC B1IV40;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00219};
DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00219};
DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00219};
GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00219}; OrderedLocusNames=EcolC_2538;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:3MJM}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-348 IN COMPLEX WITH
RP DIHYDROOROTIC ACID AND ZINC, AND COFACTOR.
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Ernberg K.E., Lee M., Christopherson R.I., Maher M.J., Guss J.M.;
RT "His257Ala mutant of dihydroorotase from E. coli.";
RL Submitted (APR-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.
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_00219};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|Ref.2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00219,
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_00219}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class II DHOase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00219, ECO:0000305}.
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DR EMBL; CP000946; ACA78169.1; -; Genomic_DNA.
DR RefSeq; WP_000126543.1; NZ_CP022959.1.
DR PDB; 3MJM; X-ray; 1.87 A; A/B=2-348.
DR PDBsum; 3MJM; -.
DR AlphaFoldDB; B1IV40; -.
DR SMR; B1IV40; -.
DR MEROPS; M38.A02; -.
DR KEGG; ecl:EcolC_2538; -.
DR HOGENOM; CLU_041558_1_0_6; -.
DR OMA; TLHHISM; -.
DR UniPathway; UPA00070; UER00117.
DR EvolutionaryTrace; B1IV40; -.
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 GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT CHAIN 1..348
FT /note="Dihydroorotase"
FT /id="PRO_1000078096"
FT ACT_SITE 251
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM"
FT BINDING 19..21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|Ref.2"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|Ref.2"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|Ref.2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|Ref.2"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|Ref.2"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|Ref.2"
FT MOD_RES 103
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3MJM"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3MJM"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:3MJM"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:3MJM"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:3MJM"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:3MJM"
SQ SEQUENCE 348 AA; 38813 MW; 2EFEA36B232519A0 CRC64;
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR
QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSV
DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT
TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA
SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
