(data stored in ACNUC7421 zone)

SWISSPROT: PYRC_SHIF8

ID   PYRC_SHIF8              Reviewed;         348 AA.
AC   Q0T5X0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 80.
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=SFV_1084;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00219};
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}.
DR   EMBL; CP000266; ABF03295.1; -; Genomic_DNA.
DR   RefSeq; WP_000126531.1; NC_008258.1.
DR   SMR; Q0T5X0; -.
DR   EnsemblBacteria; ABF03295; ABF03295; SFV_1084.
DR   KEGG; sfv:SFV_1084; -.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OMA; TLHHISM; -.
DR   BioCyc; SFLE373384:SFV_RS06010-MONOMER; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000000659; 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   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   3: Inferred from homology;
DR   PRODOM; Q0T5X0.
DR   SWISS-2DPAGE; Q0T5X0.
KW   Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT   CHAIN           1..348
FT                   /note="Dihydroorotase"
FT                   /id="PRO_1000024061"
FT   REGION          19..21
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   METAL           17
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   METAL           19
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   METAL           103
FT                   /note="Zinc 1; via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   METAL           103
FT                   /note="Zinc 2; via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   METAL           140
FT                   /note="Zinc 2; via pros nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   METAL           178
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   METAL           251
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   BINDING         45
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   BINDING         140
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   BINDING         223
FT                   /note="Substrate; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   BINDING         255
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   BINDING         267
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT   MOD_RES         103
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
SQ   SEQUENCE   348 AA;  38871 MW;  F99B2F997D15A112 CRC64;
     MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR
     QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEAVFT AAKLYPANAT TNSSHGVTSI
     DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT
     TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVT
     SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG
     PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
//

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