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PYRC_ANOFW
ID   PYRC_ANOFW              Reviewed;         428 AA.
AC   B7GFA5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Aflv_1805;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ34166.1; -; Genomic_DNA.
DR   RefSeq; WP_012575365.1; NC_011567.1.
DR   AlphaFoldDB; B7GFA5; -.
DR   SMR; B7GFA5; -.
DR   STRING; 491915.Aflv_1805; -.
DR   EnsemblBacteria; ACJ34166; ACJ34166; Aflv_1805.
DR   KEGG; afl:Aflv_1805; -.
DR   PATRIC; fig|491915.6.peg.1856; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_1_0_9; -.
DR   OMA; QHAQEPR; -.
DR   OrthoDB; 1319925at2; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000000742; 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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Zinc.
FT   CHAIN           1..428
FT                   /note="Dihydroorotase"
FT                   /id="PRO_1000193087"
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"
FT   BINDING         323..324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ   SEQUENCE   428 AA;  46807 MW;  3AC41A200F42B912 CRC64;
     MATIFKRVRL LNEQGELIQT DIKVAGGRIV QIAHDLHAEA DDEVIDVDGQ FVAPGFVDVH
     VHLREPGGEH KETIATGTLA AAKGGFTTIA AMPNTKPVPD TKQHMEWLVN RIRETAHVRV
     LPYASITVRQ AGKQLVDFVA LKEAGAFAFT DDGVGVQSAR IMYEAMQQAA ALDMPIVAHC
     EDETLTYKGC VHDGSFAKRY GLSGIPSVCE SVHIARDVLL AEATGCHYHV CHISTKQSVR
     IVREAKQAGI RVTAEVTPHH LLLCDEDIPT LDANFKMNPP LRTKEDQQAL IEGLLDGTID
     FIATDHAPHT KEEKSEGMVL APFGIVGLET AFPLLYTHFV EKGICTLKQL VDWLSKKPAE
     TFRIDGGELK VGAKADFVVI DLHTEQAIDP NTFVSKGKNT PFAGWTCKGW PTMTIVAGKI
     VWQKGRGE
 
 
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