CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002675
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pentafunctional AROM polypeptide 
Protein Synonyms/Alias
 3-dehydroquinate synthase; DHQS; 3-phosphoshikimate 1-carboxyvinyltransferase; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EPSPS; Shikimate kinase; SK; 3-dehydroquinate dehydratase; 3-dehydroquinase; Shikimate dehydrogenase 
Gene Name
 ARO1 
Gene Synonyms/Alias
 AROM; YDR127W; YD9302.02 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
75RLLTYVVKPGETSKSubiquitination[1]
180KWLETLAKREFINGMubiquitination[1]
258VLESIKVKAEVVSSDubiquitination[1]
305CVSIGMVKEAELSRYubiquitination[1]
326TQVARLSKILVAYGLacetylation[2]
340LPVSPDEKWFKELTLacetylation[2]
343SPDEKWFKELTLHKKacetylation[2]
358TPLDILLKKMSIDKKacetylation[2]
425VVIPPGSKSISNRALubiquitination[1]
454LLHSDDTKHMLTAVHacetylation[2]
695RFARDVLKPMGCKITubiquitination[1]
779AMATELAKFGVKTTEubiquitination[1]
803LNSIKDLKVPSDSSGubiquitination[1]
933QHNNQSVKQFVVENGubiquitination[1]
1058ALRRSFSKYIATITGubiquitination[1]
1127KQLSILRKATDSIPIubiquitination[1]
1337EILGLPHKFDKFETEacetylation[2]
1340GLPHKFDKFETESAQubiquitination[1]
1350TESAQLVKEKLLDGNubiquitination[1]
1402PLGNKKFKGDNTDWLubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. 
Sequence Annotation
 NP_BIND 43 45 NAD (By similarity).
 NP_BIND 78 81 NAD (By similarity).
 NP_BIND 109 111 NAD (By similarity).
 NP_BIND 134 135 NAD (By similarity).
 NP_BIND 174 177 NAD (By similarity).
 NP_BIND 895 902 ATP (By similarity).
 REGION 1 392 3-dehydroquinate synthase.
 REGION 189 192 Substrate binding 2 (By similarity).
 REGION 272 276 Substrate binding 2 (By similarity).
 REGION 405 871 EPSP synthase.
 REGION 890 1080 Shikimate kinase.
 REGION 1081 1293 3-dehydroquinase.
 REGION 1306 1588 Shikimate dehydrogenase.
 ACT_SITE 268 268 Proton acceptor; for 3-dehydroquinate
 ACT_SITE 283 283 Proton acceptor; for 3-dehydroquinate
 ACT_SITE 853 853 For EPSP synthase activity (Potential).
 ACT_SITE 1198 1198 Proton acceptor; for 3-dehydroquinate
 ACT_SITE 1227 1227 Schiff-base intermediate with substrate;
 METAL 189 189 Zinc; catalytic (By similarity).
 METAL 279 279 Zinc; catalytic (By similarity).
 METAL 295 295 Zinc; catalytic (By similarity).
 BINDING 114 114 NAD (By similarity).
 BINDING 125 125 Substrate 1 (By similarity).
 BINDING 141 141 Substrate 2 (By similarity).
 BINDING 147 147 Substrate 2 (By similarity).
 BINDING 156 156 NAD (By similarity).
 BINDING 157 157 Substrate 2 (By similarity).
 BINDING 185 185 NAD (By similarity).
 BINDING 258 258 Substrate 2 (By similarity).
 BINDING 279 279 Substrate 2 (By similarity).
 BINDING 295 295 Substrate 2 (By similarity).
 BINDING 364 364 Substrate 2 (By similarity).  
Keyword
 Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1588 AA 
Protein Sequence
MVQLAKVPIL GNDIIHVGYN IHDHLVETII KHCPSSTYVI CNDTNLSKVP YYQQLVLEFK 60
ASLPEGSRLL TYVVKPGETS KSRETKAQLE DYLLVEGCTR DTVMVAIGGG VIGDMIGFVA 120
STFMRGVRVV QVPTSLLAMV DSSIGGKTAI DTPLGKNFIG AFWQPKFVLV DIKWLETLAK 180
REFINGMAEV IKTACIWNAD EFTRLESNAS LFLNVVNGAK NVKVTNQLTN EIDEISNTDI 240
EAMLDHTYKL VLESIKVKAE VVSSDERESS LRNLLNFGHS IGHAYEAILT PQALHGECVS 300
IGMVKEAELS RYFGILSPTQ VARLSKILVA YGLPVSPDEK WFKELTLHKK TPLDILLKKM 360
SIDKKNEGSK KKVVILESIG KCYGDSAQFV SDEDLRFILT DETLVYPFKD IPADQQKVVI 420
PPGSKSISNR ALILAALGEG QCKIKNLLHS DDTKHMLTAV HELKGATISW EDNGETVVVE 480
GHGGSTLSAC ADPLYLGNAG TASRFLTSLA ALVNSTSSQK YIVLTGNARM QQRPIAPLVD 540
SLRANGTKIE YLNNEGSLPI KVYTDSVFKG GRIELAATVS SQYVSSILMC APYAEEPVTL 600
ALVGGKPISK LYVDMTIKMM EKFGINVETS TTEPYTYYIP KGHYINPSEY VIESDASSAT 660
YPLAFAAMTG TTVTVPNIGF ESLQGDARFA RDVLKPMGCK ITQTATSTTV SGPPVGTLKP 720
LKHVDMEPMT DAFLTACVVA AISHDSDPNS ANTTTIEGIA NQRVKECNRI LAMATELAKF 780
GVKTTELPDG IQVHGLNSIK DLKVPSDSSG PVGVCTYDDH RVAMSFSLLA GMVNSQNERD 840
EVANPVRILE RHCTGKTWPG WWDVLHSELG AKLDGAEPLE CTSKKNSKKS VVIIGMRAAG 900
KTTISKWCAS ALGYKLVDLD ELFEQQHNNQ SVKQFVVENG WEKFREEETR IFKEVIQNYG 960
DDGYVFSTGG GIVESAESRK ALKDFASSGG YVLHLHRDIE ETIVFLQSDP SRPAYVEEIR 1020
EVWNRREGWY KECSNFSFFA PHCSAEAEFQ ALRRSFSKYI ATITGVREIE IPSGRSAFVC 1080
LTFDDLTEQT ENLTPICYGC EAVEVRVDHL ANYSADFVSK QLSILRKATD SIPIIFTVRT 1140
MKQGGNFPDE EFKTLRELYD IALKNGVEFL DLELTLPTDI QYEVINKRGN TKIIGSHHDF 1200
QGLYSWDDAE WENRFNQALT LDVDVVKFVG TAVNFEDNLR LEHFRDTHKN KPLIAVNMTS 1260
KGSISRVLNN VLTPVTSDLL PNSAAPGQLT VAQINKMYTS MGGIEPKELF VVGKPIGHSR 1320
SPILHNTGYE ILGLPHKFDK FETESAQLVK EKLLDGNKNF GGAAVTIPLK LDIMQYMDEL 1380
TDAAKVIGAV NTVIPLGNKK FKGDNTDWLG IRNALINNGV PEYVGHTAGL VIGAGGTSRA 1440
ALYALHSLGC KKIFIINRTT SKLKPLIESL PSEFNIIGIE STKSIEEIKE HVGVAVSCVP 1500
ADKPLDDELL SKLERFLVKG AHAAFVPTLL EAAYKPSVTP VMTISQDKYQ WHVVPGSQML 1560
VHQGVAQFEK WTGFKGPFKA IFDAVTKE 1588 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0003855; F:3-dehydroquinate dehydratase activity; IDA:SGD.
 GO:0003856; F:3-dehydroquinate synthase activity; IDA:SGD.
 GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:SGD.
 GO:0004765; F:shikimate kinase activity; IDA:SGD.
 GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
 GO:0009423; P:chorismate biosynthetic process; TAS:SGD. 
Interpro
 IPR018508; 3-dehydroquinate_DH_AS.
 IPR013785; Aldolase_TIM.
 IPR016037; DHQ_synth_AroB.
 IPR001381; DHquinase_I.
 IPR001986; Enolpyruvate_Tfrase_dom.
 IPR006264; EPSP_synthase.
 IPR023193; EPSP_synthase_CS.
 IPR016040; NAD(P)-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR008289; Pentafunct_AroM.
 IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
 IPR013708; Shikimate_DH-bd_N.
 IPR010110; Shikimate_DH_AroM-type.
 IPR000623; Shikimate_kinase/TSH1.
 IPR023000; Shikimate_kinase_CS.
 IPR006151; Shikm_DH/Glu-tRNA_Rdtase. 
Pfam
 PF01487; DHquinase_I
 PF00275; EPSP_synthase
 PF01488; Shikimate_DH
 PF08501; Shikimate_dh_N
 PF01202; SKI 
SMART
  
PROSITE
 PS01028; DEHYDROQUINASE_I
 PS00104; EPSP_SYNTHASE_1
 PS00885; EPSP_SYNTHASE_2
 PS01128; SHIKIMATE_KINASE 
PRINTS
 PR01100; SHIKIMTKNASE.