(data stored in ACNUC7421 zone)

SWISSPROT: C6AZB5_RHILS

ID   C6AZB5_RHILS            Unreviewed;       348 AA.
AC   C6AZB5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 66.
DE   RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00701465};
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:SAAS00701485};
GN   Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00219};
GN   OrderedLocusNames=Rleg_0130 {ECO:0000313|EMBL:ACS54441.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54441.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54441.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54441.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|SAAS:SAAS00853095}.
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:SAAS00701469}.
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:SAAS00701468}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|SAAS:SAAS00701478}.
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:SAAS00853094}.
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DR   EMBL; CP001622; ACS54441.1; -; Genomic_DNA.
DR   RefSeq; WP_012755863.1; NC_012850.1.
DR   ProteinModelPortal; C6AZB5; -.
DR   EnsemblBacteria; ACS54441; ACS54441; Rleg_0130.
DR   KEGG; rlg:Rleg_0130; -.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OMA; HLRDGAM; -.
DR   OrthoDB; POG091H06EN; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
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:SF1; PTHR43137:SF1; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF001237; DHOdimr; 1.
DR   SFLD; SFLDF00074; dihydroorotase3; 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; C6AZB5.
DR   SWISS-2DPAGE; C6AZB5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00219,
KW   ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00470770,
KW   ECO:0000313|EMBL:ACS54441.1};
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:SAAS00701466};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440,
KW   ECO:0000256|SAAS:SAAS00701487}.
FT   DOMAIN       11    321       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION       15     17       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00219}.
FT   ACT_SITE    247    247       {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        13     13       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        15     15       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        99     99       Zinc 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        99     99       Zinc 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       136    136       Zinc 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       174    174       Zinc 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       247    247       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING      41     41       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     219    219       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     251    251       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     263    263       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   MOD_RES      99     99       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00219}.
SQ   SEQUENCE   348 AA;  38282 MW;  0AF9E3C1C4CC6759 CRC64;
     MQSITIRRPD DWHLHLRDGA MLEGVIADTS RTFARAIIMP NLVPPVVTSA DAKAYRERIL
     KALPDGHRFQ PLMTLYLTEH TSPDDVEEGK NSGLITAVKL YPAGATTNSH GGVRDMEKAM
     PVLERMAKIG LPLCVHGEVT TPEVDIFDRE AVFIETVLDP LRQRLPELKV TMEHVTTSDG
     VDYIKTAKGN LAGSITTHHL IINRNAILVG GIRPHYYCLP VAKRENHRLA LRAAAVSGDA
     RFFLGTDSAP HVDPLKECAC GCAGIYTSVN TMSCLAHVFE QEGALERLEA FVSLNGPAWY
     GLQPNEERIT LARQADPVVF PARIETGAGP VTVFDPMFPL HWQVVQQA
//

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