CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002203
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydroorotase 
Protein Synonyms/Alias
 DHOase 
Gene Name
 pyrC 
Gene Synonyms/Alias
 b1062; JW1049 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
9TAPSQVLKIRRPDDWacetylation[1]
27LRDGDMLKTVVPYTSacetylation[1]
103EGVFTAAKLYPANATacetylation[1]
132PVLERMEKIGMPLLVacetylation[1]
182VFEHITTKDAADYVRacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
  
Sequence Annotation
 METAL 17 17 Zinc 1.
 METAL 19 19 Zinc 1.
 METAL 103 103 Zinc 1; via carbamate group.
 METAL 103 103 Zinc 2; via carbamate group.
 METAL 140 140 Zinc 2.
 METAL 178 178 Zinc 2.
 METAL 251 251 Zinc 1.
 MOD_RES 103 103 N6-carboxylysine.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 348 AA 
Protein Sequence
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 60
QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSI 120
DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT 180
TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA 240
SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 300
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ 348 
Gene Ontology
 GO:0004151; F:dihydroorotase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:EcoCyc.
 GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006680; Amidohydro_1.
 IPR004721; DHOdimr.
 IPR002195; Dihydroorotase_CS. 
Pfam
 PF01979; Amidohydro_1 
SMART
  
PROSITE
 PS00482; DIHYDROOROTASE_1
 PS00483; DIHYDROOROTASE_2 
PRINTS