CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005468
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NAD-dependent dihydropyrimidine dehydrogenase subunit PreA 
Protein Synonyms/Alias
 DPD; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase 
Gene Name
 preA 
Gene Synonyms/Alias
 yeiA; b2147; JW2134 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
377TPHCNTEKCVGCLLCacetylation[1]
Reference
 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111
Functional Description
 Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6- dihydrothymine (DHT). 
Sequence Annotation
 DOMAIN 335 367 4Fe-4S ferredoxin-type 1.
 DOMAIN 369 398 4Fe-4S ferredoxin-type 2.
 REGION 134 136 Substrate binding (By similarity).
 REGION 201 202 Substrate binding (By similarity).
 ACT_SITE 137 137 Proton acceptor (By similarity).
 METAL 344 344 Iron-sulfur 1 (4Fe-4S) (Potential).
 METAL 347 347 Iron-sulfur 1 (4Fe-4S) (Potential).
 METAL 350 350 Iron-sulfur 1 (4Fe-4S) (Potential).
 METAL 354 354 Iron-sulfur 2 (4Fe-4S) (Potential).
 METAL 378 378 Iron-sulfur 2 (4Fe-4S) (Potential).
 METAL 381 381 Iron-sulfur 2 (4Fe-4S) (Potential).
 METAL 384 384 Iron-sulfur 2 (4Fe-4S) (Potential).
 METAL 388 388 Iron-sulfur 1 (4Fe-4S) (Potential).
 BINDING 76 76 Substrate (By similarity).  
Keyword
 4Fe-4S; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 411 AA 
Protein Sequence
MLTKDLSITF CGVKFPNPFC LSSSPVGNCY EMCAKAYDTG WGGVVFKTIG FFIANEVSPR 60
FDHLVKEDTG FIGFKNMEQI AEHPLEENLA ALRRLKEDYP DKVLIASIMG ENEQQWEELA 120
RLVQEAGADM IECNFSCPQM TSHAMGSDVG QSPELVEKYC RAVKRGSTLP MLAKMTPNIG 180
DMCEVALAAK RGGADGIAAI NTVKSITNID LNQKIGMPIV NGKSSISGYS GKAVKPIALR 240
FIQQMRTHPE LRDFPISGIG GIETWEDAAE FLLLGAATLQ VTTGIMQYGY RIVEDMASGL 300
SHYLADQGFD SLQEMVGLAN NNIVPAEDLD RSYIVYPRIN LDKCVGCGRC YISCYDGGHQ 360
AMEWSEKTRT PHCNTEKCVG CLLCGHVCPV GCIELGEVKF KKGEKEHPVT L 411 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
 GO:0004159; F:dihydrouracil dehydrogenase (NAD+) activity; IEA:EC.
 GO:0051536; F:iron-sulfur cluster binding; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003954; F:NADH dehydrogenase activity; IDA:UniProtKB.
 GO:0006928; P:cellular component movement; IMP:EcoCyc.
 GO:0006208; P:pyrimidine nucleobase catabolic process; IDA:UniProtKB.
 GO:0006222; P:UMP biosynthetic process; IEA:InterPro. 
Interpro
 IPR017896; 4Fe4S_Fe-S-bd.
 IPR017900; 4Fe4S_Fe_S_CS.
 IPR013785; Aldolase_TIM.
 IPR005720; Dihydroorotate_DH.
 IPR012135; Dihydroorotate_DH_1_2. 
Pfam
 PF01180; DHO_dh 
SMART
  
PROSITE
 PS00198; 4FE4S_FER_1
 PS51379; 4FE4S_FER_2 
PRINTS