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Database: UniProt/TrEMBL
Entry: B1YTC8_BURA4
LinkDB: B1YTC8_BURA4
Original site: B1YTC8_BURA4 
ID   B1YTC8_BURA4            Unreviewed;       364 AA.
AC   B1YTC8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   25-OCT-2017, entry version 78.
DE   RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00919138};
DE            Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00219};
DE            EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00919151};
GN   Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00219};
GN   OrderedLocusNames=BamMC406_0596 {ECO:0000313|EMBL:ACB63093.1};
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB63093.1, ECO:0000313|Proteomes:UP000001680};
RN   [1] {ECO:0000313|Proteomes:UP000001680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Ramette A., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|SAAS:SAAS00919147}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate. {ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00919159}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00219, ECO:0000256|RuleBase:RU003440};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00219, ECO:0000256|RuleBase:RU003440};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440,
CC       ECO:0000256|SAAS:SAAS00919160}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|SAAS:SAAS00919143}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class II DHOase subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440,
CC       ECO:0000256|SAAS:SAAS00919139}.
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DR   EMBL; CP001025; ACB63093.1; -; Genomic_DNA.
DR   ProteinModelPortal; B1YTC8; -.
DR   EnsemblBacteria; ACB63093; ACB63093; BamMC406_0596.
DR   KEGG; bac:BamMC406_0596; -.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OMA; HLRDGAM; -.
DR   OrthoDB; POG091H06EN; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000001680; Chromosome 1.
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_type1; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001680};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00219,
KW   ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00470770,
KW   ECO:0000313|EMBL:ACB63093.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00219,
KW   ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00470804};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00219,
KW   ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00919137};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440,
KW   ECO:0000256|SAAS:SAAS00919161}.
FT   DOMAIN       29    331       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION       33     35       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00219}.
FT   ACT_SITE    268    268       {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        31     31       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        33     33       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       117    117       Zinc 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       117    117       Zinc 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       154    154       Zinc 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       192    192       Zinc 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       268    268       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING      59     59       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     154    154       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     240    240       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     272    272       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     284    284       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   MOD_RES     117    117       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00219}.
SQ   SEQUENCE   364 AA;  39685 MW;  EC4610ECCD74A4FA CRC64;
     MASPFLTTPP MTASNASSPA TLTLARPDDL HLHLRDGDML AAVLPHTARQ FARAIVMPNL
     KPPVTTTAHA QAYRERILAA LPAGMTFEPL MTLYLTDNTA PDEIRRARDS GFVHGVKLYP
     AGATTNSDHG VSDLAKCAKT LEVMQETGMP LLVHGEVTDP SVDMFDREKV FIDRVMTPLR
     RDFPGLKVVF EHITTKDAAD YVRDADAAPG LLGATITPQH MLYSRNALFV GGIRPHYYCL
     PVLKRETHRV ALVEAATSGN PRFFLGTDSA PHARGAKETA CGCAGCYTAL HALELYAEAF
     DQAGALDKLE NFASRFGADF YGLPHSTETV TLRRETWELP REVFAGDTPV VPLRAGEAIG
     WKFA
//
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