CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001439
UniProt Accession
Genbank Protein ID
 D85035 
Genbank Nucleotide ID
Protein Name
 Dihydropyrimidine dehydrogenase [NADP(+)] 
Protein Synonyms/Alias
 DHPDHase; DPD; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase 
Gene Name
 Dpyd 
Gene Synonyms/Alias
 DPD 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
384MELAKEEKCEFLPFLacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine (By similarity). 
Sequence Annotation
 DOMAIN 69 100 4Fe-4S ferredoxin-type 1.
 DOMAIN 944 976 4Fe-4S ferredoxin-type 2.
 DOMAIN 978 1007 4Fe-4S ferredoxin-type 3.
 NP_BIND 194 198 FAD (By similarity).
 NP_BIND 218 226 FAD (By similarity).
 NP_BIND 340 343 NADP (By similarity).
 NP_BIND 364 365 NADP (By similarity).
 NP_BIND 437 439 NADP (By similarity).
 NP_BIND 480 489 FAD (By similarity).
 NP_BIND 481 487 NADP (By similarity).
 NP_BIND 574 575 FMN (By similarity).
 NP_BIND 793 795 FMN (By similarity).
 NP_BIND 816 817 FMN (By similarity).
 REGION 668 670 Substrate binding (By similarity).
 REGION 736 737 Substrate binding (By similarity).
 ACT_SITE 671 671 Proton acceptor (By similarity).
 METAL 79 79 Iron-sulfur 1 (4Fe-4S) (By similarity).
 METAL 82 82 Iron-sulfur 1 (4Fe-4S) (By similarity).
 METAL 87 87 Iron-sulfur 1 (4Fe-4S) (By similarity).
 METAL 91 91 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 130 130 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 136 136 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 140 140 Iron-sulfur 1 (4Fe-4S) (By similarity).
 METAL 156 156 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 953 953 Iron-sulfur 3 (4Fe-4S) (By similarity).
 METAL 956 956 Iron-sulfur 3 (4Fe-4S) (By similarity).
 METAL 959 959 Iron-sulfur 3 (4Fe-4S) (By similarity).
 METAL 963 963 Iron-sulfur 3 (4Fe-4S) (By similarity).
 METAL 986 986 Iron-sulfur 4 (4Fe-4S) (By similarity).
 METAL 989 989 Iron-sulfur 4 (4Fe-4S) (By similarity).
 METAL 992 992 Iron-sulfur 4 (4Fe-4S) (By similarity).
 METAL 996 996 Iron-sulfur 4 (4Fe-4S) (By similarity).
 BINDING 129 129 FAD; via carbonyl oxygen (By similarity).
 BINDING 235 235 FAD (By similarity).
 BINDING 371 371 NADP (By similarity).
 BINDING 550 550 FMN (By similarity).
 BINDING 609 609 Substrate (By similarity).
 BINDING 709 709 FMN (By similarity).
 BINDING 767 767 FMN; via amide nitrogen (By similarity).
 MOD_RES 384 384 N6-acetyllysine (By similarity).  
Keyword
 4Fe-4S; Acetylation; Complete proteome; Cytoplasm; FAD; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1025 AA 
Protein Sequence
MAGVLSRDAP DIESILALNP RIQAHATLRS TMAKKLDKKH WKRNTDKNCF ICEKLENNFD 60
DIKHTTLGER GALREAVRCL KCADAPCQKS CPTSLDIKSF ITSIANKNYY GAAKLIFSDN 120
PLGLTCGMVC PTSDLCVGGC NLHATEEGPI NIGGLQQFAT EVFKAMNIPQ IRSPLLPPPE 180
HMPEAYSAKI ALFGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV 240
VNFEIELMKD LGVKIICGKS ISTDEMTLST LKENGYKAAF IGIGLPEPKK DHIFQGLTQV 300
QGFYTSKDFL PLVAKGSKPG MCACHSPLPS VRGAVIVLGA GDTAFDCATS ALRCGARRVF 360
IVFRKGFANI RAVPEEMELA KEEKCEFLPF LSPRKVIVKD GKIVGMQFVR TEQDETGNWV 420
EDEEQIVRLK ADVVISPFGS VLDDPKVIEA LSPIKFNRWG LPEVNPETMQ TSEPWVFAGG 480
DVVGMANTTV ESVNDGKQAS WYIHEYIQAQ YGALVPSQPT LPLFYTPVDL VDISVEMAGL 540
RFPNPFGLAS ATPATSTPMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPLY 600
GPGQSSFLNI ELISEKTAAY WCHSVTELKA DFPDNILIAS IMCSYNKNDW MELSKMAEAS 660
GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ SVRVPFFAKL TPNVTDIVSI 720
ARAAKEGGAD GVTATNTVSG LMGLKADGSP WPSVGSGKRT TYGGVSGTTI RPIALRAVTA 780
IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL 840
KSIEELSDWD GQSPPTMSHQ KGKPVPHIAE LMGQKLPSFG PYLERRKKIL AASKIRENDQ 900
NRACSPLQRK HFNSQKPIPA IKDVIGKSLQ YLGTFGELNI MEQVVALIDE EMCINCGKCY 960
MTCNDSGYQA IQFDPETHLP TVSDTCTGCT LCLSVCPIMD CIRMVSRATP YEPKRGLPLA 1020
VKPVC 1025 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
 GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050661; F:NADP binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0002058; F:uracil binding; IDA:RGD.
 GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0007623; P:circadian rhythm; IDA:RGD.
 GO:0042493; P:response to drug; IDA:RGD.
 GO:0051384; P:response to glucocorticoid stimulus; IEP:RGD.
 GO:0007584; P:response to nutrient; IDA:RGD.
 GO:0006214; P:thymidine catabolic process; ISS:UniProtKB.
 GO:0006222; P:UMP biosynthetic process; IEA:InterPro.
 GO:0006212; P:uracil catabolic process; ISS:UniProtKB. 
Interpro
 IPR001450; 4Fe4S-bd_dom.
 IPR017896; 4Fe4S_Fe-S-bd.
 IPR017900; 4Fe4S_Fe_S_CS.
 IPR013785; Aldolase_TIM.
 IPR005720; Dihydroorotate_DH.
 IPR012135; Dihydroorotate_DH_1_2.
 IPR012285; Fum_reductase_C.
 IPR009051; Helical_ferredxn. 
Pfam
 PF01180; DHO_dh
 PF12838; Fer4_7 
SMART
  
PROSITE
 PS00198; 4FE4S_FER_1
 PS51379; 4FE4S_FER_2 
PRINTS