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PYRC_RUMCH
ID   PYRC_RUMCH              Reviewed;         428 AA.
AC   B8I770;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Ccel_0613;
OS   Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10) (Clostridium cellulolyticum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) 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; CP001348; ACL74994.1; -; Genomic_DNA.
DR   RefSeq; WP_015924163.1; NC_011898.1.
DR   AlphaFoldDB; B8I770; -.
DR   SMR; B8I770; -.
DR   STRING; 394503.Ccel_0613; -.
DR   EnsemblBacteria; ACL74994; ACL74994; Ccel_0613.
DR   KEGG; cce:Ccel_0613; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_1_0_9; -.
DR   OMA; QHAQEPR; -.
DR   OrthoDB; 1319925at2; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000001349; 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..428
FT                   /note="Dihydroorotase"
FT                   /id="PRO_1000193097"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ   SEQUENCE   428 AA;  46465 MW;  831831A2B1653704 CRC64;
     MKLLIKNGHV LDVKTGLDRV TDILAVDGII HEVGSKIDEA GCEVIDATGL YVTPGLVDAH
     CHLRDPGYEY KEDIESGTRS AAKGGFTSVA CMPNTNPVLD NEAMVKYVIN KAKTDGFLNV
     FPIGALSKGL KGEELSEIGE LKFAGAVALS DDGRPVGNSS LMKKAMQYAS MFDITIISHC
     EDLDLVDEGL MNEGYQSSIL GLKGNPAPAE EVMIARDLIL AEYTKATIHI AHVSTELGVD
     LIRNAKRRGV KVTAETCPHY FTLTDNACEG FNTNAKVNPP LRTQKDVDAI IQGLKDGTID
     IISTDHAPHH IDEKNVEFKI AANGMVGFET AFPLAVTYLV KPGHLSLKEL VYKMSFNPSQ
     MLGLNKGTIE VGKLADLIIF DLNEEYKVNI TEFESKSKNS PFNGLLLYGQ PQYTIVGGTP
     VVRKKVLL
 
 
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