Tag | Content |
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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 |
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75 | RLLTYVVKPGETSKS | ubiquitination | [1] | 180 | KWLETLAKREFINGM | ubiquitination | [1] | 258 | VLESIKVKAEVVSSD | ubiquitination | [1] | 305 | CVSIGMVKEAELSRY | ubiquitination | [1] | 326 | TQVARLSKILVAYGL | acetylation | [2] | 340 | LPVSPDEKWFKELTL | acetylation | [2] | 343 | SPDEKWFKELTLHKK | acetylation | [2] | 358 | TPLDILLKKMSIDKK | acetylation | [2] | 425 | VVIPPGSKSISNRAL | ubiquitination | [1] | 454 | LLHSDDTKHMLTAVH | acetylation | [2] | 695 | RFARDVLKPMGCKIT | ubiquitination | [1] | 779 | AMATELAKFGVKTTE | ubiquitination | [1] | 803 | LNSIKDLKVPSDSSG | ubiquitination | [1] | 933 | QHNNQSVKQFVVENG | ubiquitination | [1] | 1058 | ALRRSFSKYIATITG | ubiquitination | [1] | 1127 | KQLSILRKATDSIPI | ubiquitination | [1] | 1337 | EILGLPHKFDKFETE | acetylation | [2] | 1340 | GLPHKFDKFETESAQ | ubiquitination | [1] | 1350 | TESAQLVKEKLLDGN | ubiquitination | [1] | 1402 | PLGNKKFKGDNTDWL | ubiquitination | [1] |
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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, Villén 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. |
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