ID PYRC_ALISL Reviewed; 342 AA.
AC B6ER91;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=VSAL_II0468;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RA Hjerde E., Lorentzen M.S., Holden M.T.G., Seeger K., Paulsen S.,
RA Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A.,
RA Sanders S., Thurston S., Parkhill J., Willassen N.-P., Thomson N.R.;
RT "The complete genome sequence of the fish pathogen Aliivibrio
RT salmonicida strain LFI1238.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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.
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DR EMBL; FM178380; CAQ81222.1; -; Genomic_DNA.
DR RefSeq; YP_002264799.1; NC_011313.1.
DR ProteinModelPortal; B6ER91; -.
DR STRING; 316275.VSAL_II0468; -.
DR EnsemblBacteria; CAQ81222; CAQ81222; VSAL_II0468.
DR GeneID; 6961895; -.
DR KEGG; vsa:VSAL_II0468; -.
DR PATRIC; 20857712; VBIAliSal95923_3818.
DR eggNOG; COG0418; -.
DR HOGENOM; HOG000256259; -.
DR KO; K01465; -.
DR OMA; MTLYLTE; -.
DR ProtClustDB; PRK05451; -.
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 CHAIN 1 342 Dihydroorotase.
FT /FTId=PRO_1000100036.
FT METAL 13 13 Zinc 1 (By similarity).
FT METAL 15 15 Zinc 1 (By similarity).
FT METAL 98 98 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 98 98 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 135 135 Zinc 2 (By similarity).
FT METAL 173 173 Zinc 2 (By similarity).
FT METAL 246 246 Zinc 1 (By similarity).
FT MOD_RES 98 98 N6-carboxylysine (By similarity).
SQ SEQUENCE 342 AA; 37790 MW; DBA053A35DA66AC2 CRC64;
MTTLTITRPD DWHLHLRDGD VLTDTVRDSG RYNGRALIMP NLVPPVITTE QALSYRERIQ
AVNSSNTFAP IMSLYLTEKT TSDEIRKAKA TGYIVAAKLY PAGATTNSDS GVSDVQKVYP
ILKTMQEEGM LLLIHGEVTT HDIDIFDREK TFLDTVLAPI VNDFPELKIV LEHITTKDAA
DFVKNAGPNV AATITAHHLL FNRNHMLVGG IKPHFYCLPI LKRNTHQLAL IEAATSGSPK
FFLGTDSAPH SKEKKEAACG CAGSYTAHAS IELYTEVFEN EGKLDNLEAF ASFNGPDFYN
LPRNTDTITL VKEAWITPET MSFGNDVVVP IRAGEAVEWL VK
//
