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Database: UniProt/TrEMBL
Entry: A4G1S1_HERAR
LinkDB: A4G1S1_HERAR
Original site: A4G1S1_HERAR 
ID   A4G1S1_HERAR            Unreviewed;       352 AA.
AC   A4G1S1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   25-OCT-2017, entry version 86.
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   ECO:0000313|EMBL:CAL60458.1};
GN   OrderedLocusNames=HEAR0229 {ECO:0000313|EMBL:CAL60458.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60458.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL60458.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M.,
RA   Leize E., Lieutaud A., Lievremont D., Makita Y., Mangenot S.,
RA   Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier N.,
RA   Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D.,
RA   Van Dorsselaer A., Weiss S., Weissenbach J., Lett M.C., Danchin A.,
RA   Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-
RT   rich environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL60458.1; -; Genomic_DNA.
DR   ProteinModelPortal; A4G1S1; -.
DR   STRING; 204773.HEAR0229; -.
DR   EnsemblBacteria; CAL60458; CAL60458; HEAR0229.
DR   KEGG; har:HEAR0229; -.
DR   eggNOG; ENOG4105EKE; Bacteria.
DR   eggNOG; COG0418; LUCA.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OMA; HLRDGAM; -.
DR   OrthoDB; POG091H06EN; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000006697; 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_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:UP000006697};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00219,
KW   ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS00470770,
KW   ECO:0000313|EMBL:CAL60458.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440,
KW   ECO:0000256|SAAS:SAAS00919161}.
FT   DOMAIN       20    319       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION       24     26       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00219}.
FT   ACT_SITE    256    256       {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        22     22       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL        24     24       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       108    108       Zinc 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       108    108       Zinc 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       145    145       Zinc 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       183    183       Zinc 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   METAL       256    256       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING      50     50       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     145    145       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     228    228       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     260    260       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00219}.
FT   BINDING     272    272       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00219}.
FT   MOD_RES     108    108       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00219}.
SQ   SEQUENCE   352 AA;  38971 MW;  AFEE4644BF43AFD8 CRC64;
     MIMNSASTRP SSITITRPDD WHLHLRDGAT IASVLPDTAR QFARAIVMPN LKPPVTTTAQ
     AVAYRERILA ALPAGMQFEP LMTLYLTNNT PPEEIQRARD SGVVHAVKLY PAGATTNSDA
     GVSDLSKCYK TLEAMQKIGM PFLVHGEVTD PNVDIFDREA VFIDRVMQPL RRDMPELKVV
     FEHITTKDAA QYVAEADRHV AATITAHHLL YNRNEIFKGG IRPHYYCLPV LKRELHRQAL
     VAAATSGSNK FFLGTDSAPH PKGLKEHACG CAGCYTALHA MELYTQAFDQ ADALDKLEQF
     ASFNGPDFYS LPRNTGTITL RREEWQVPGE LPLGETTLVP LNGGETIGWK FV
//
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