CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010200
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyrimidine monooxygenase RutA 
Protein Synonyms/Alias
  
Gene Name
 rutA 
Gene Synonyms/Alias
 ycdM; b1012; JW0997 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
296WLTEQSQKDTRSGTDacetylation[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
 Catalyzes the pyrimidine ring opening between N-3 and C- 4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro. 
Sequence Annotation
 REGION 68 69 FMN binding (Potential).
 REGION 159 160 FMN binding (Potential).
 BINDING 134 134 FMN (Potential).
 BINDING 143 143 FMN (Potential).
 BINDING 209 209 FMN (Potential).  
Keyword
 Complete proteome; FMN; Monooxygenase; NADP; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 382 AA 
Protein Sequence
MQDAAPRLTF TLRDEERLMM KIGVFVPIGN NGWLISTHAP QYMPTFELNK AIVQKAEHYH 60
FDFALSMIKL RGFGGKTEFW DHNLESFTLM AGLAAVTSRI QIYATAATLT LPPAIVARMA 120
ATIDSISGGR FGVNLVTGWQ KPEYEQMGIW PGDDYFSRRY DYLTEYVQVL RDLWGTGKSD 180
FKGDFFTMND CRVSPQPSVP MKVICAGQSD AGMAFSARYA DFNFCFGKGV NTPTAFAPTA 240
ARMKQAAEQT GRDVGSYVLF MVIADETDDA ARAKWEHYKA GADEEALSWL TEQSQKDTRS 300
GTDTNVRQMA DPTSAVNINM GTLVGSYASV ARMLDEVASV PGAEGVLLTF DDFLSGIETF 360
GERIQPLMQC RAHLPALTQE VA 382 
Gene Ontology
 GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
 GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
 GO:0052614; F:uracil oxygenase activity; IDA:EcoCyc.
 GO:0019740; P:nitrogen utilization; IDA:UniProtKB.
 GO:0006212; P:uracil catabolic process; IDA:UniProtKB. 
Interpro
 IPR011251; Luciferase-like_dom.
 IPR019914; Pyrimidine_monooxygenase_RutA. 
Pfam
 PF00296; Bac_luciferase 
SMART
  
PROSITE
  
PRINTS