ID A4G1S1_HERAR Unreviewed; 352 AA.
AC A4G1S1;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 01-MAY-2013, entry version 50.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=HEAR0229;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
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:e53-e53(2007).
CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC aspartate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CU207211; CAL60458.1; -; Genomic_DNA.
DR RefSeq; YP_001098587.1; NC_009138.1.
DR ProteinModelPortal; A4G1S1; -.
DR SMR; A4G1S1; 11-351.
DR STRING; 204773.HEAR0229; -.
DR EnsemblBacteria; CAL60458; CAL60458; HEAR0229.
DR GeneID; 4929847; -.
DR KEGG; har:HEAR0229; -.
DR PATRIC; 22110668; VBIHerArs17568_0227.
DR eggNOG; COG0418; -.
DR HOGENOM; HOG000256259; -.
DR KO; K01465; -.
DR OMA; MTLYLTE; -.
DR ProtClustDB; PRK05451; -.
DR BioCyc; HARS204773:GJCA-224-MONOMER; -.
DR UniPathway; UPA00070; UER00117.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA: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 HAMAP; MF_00219; PyrC_type1; 1; -.
DR InterPro; IPR006680; Amidohydro_1.
DR InterPro; IPR004721; DHOdimr.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001237; DHOdimr; 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; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW Zinc.
FT METAL 22 22 Zinc 1 (By similarity).
FT METAL 24 24 Zinc 1 (By similarity).
FT METAL 108 108 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 108 108 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 145 145 Zinc 2 (By similarity).
FT METAL 183 183 Zinc 2 (By similarity).
FT METAL 256 256 Zinc 1 (By similarity).
FT MOD_RES 108 108 N6-carboxylysine (By similarity).
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
//
