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PYRC_LACPL
ID   PYRC_LACPL              Reviewed;         430 AA.
AC   P77884; F9URI4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 137.
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=lp_2702;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX   PubMed=8982065; DOI=10.1016/s0378-1119(96)00461-1;
RA   Elagoez A., Abdi A., Hubert J.-C., Kammerer B.;
RT   "Structure and organisation of the pyrimidine biosynthesis pathway genes in
RT   Lactobacillus plantarum: a PCR strategy for sequencing without cloning.";
RL   Gene 182:37-43(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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; Z54240; CAA91003.1; -; Genomic_DNA.
DR   EMBL; AL935263; CCC79823.1; -; Genomic_DNA.
DR   RefSeq; WP_003644720.1; NC_004567.2.
DR   RefSeq; YP_004890337.1; NC_004567.2.
DR   AlphaFoldDB; P77884; -.
DR   SMR; P77884; -.
DR   STRING; 220668.lp_2702; -.
DR   MEROPS; M38.972; -.
DR   EnsemblBacteria; CCC79823; CCC79823; lp_2702.
DR   KEGG; lpl:lp_2702; -.
DR   PATRIC; fig|220668.9.peg.2262; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_1_0_9; -.
DR   OMA; QHAQEPR; -.
DR   PhylomeDB; P77884; -.
DR   BioCyc; LPLA220668:G1GW0-2314-MON; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000000432; 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..430
FT                   /note="Dihydroorotase"
FT                   /id="PRO_0000147237"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         63..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
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   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
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   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   CONFLICT        50
FT                   /note="Q -> H (in Ref. 1; CAA91003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="A -> T (in Ref. 1; CAA91003)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   430 AA;  45439 MW;  28AA854FC82946EF CRC64;
     MTTLIKNAQV WQAGQLQTTD ILIAEGRIKA IGHQLHDQFG PADHVICADQ HFVSPGFVDV
     HVHLRDPGQT AKETIATGTL AAAHGGFTTV GAMPNVDPVP DTPERVATMV ARNQQEAHVH
     VAQYASITTG RTSEQLVDFA GIKAAGAFAV SNDGSGVQTA GTMFAAMQGA AKVGLPLAAH
     VEDDSLYHHG VMNAGPVADR LGLPGINNVS EAAQVARDVM LAEASGVHYH VCHVSTAESL
     RVIRNAKAAG INVTCEVSPH HLLLCDEDIT MDNPMLKMNP PLRSAKDRAA LVAGLLDGTI
     DMIATDHAPH TDAEKQGSMK TAAFGITGIE TAFATLYTAL VKTRLLTLGR LIELMSTRPA
     ELFGLNTAGR LVVGAPADLT IIDLDHQYEI EAATMLSKGH NSPFIGWPVY GNVLMTLVDG
     KLAYGKETQA
 
 
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