ACL_RS01075
  | Uniprot: A9NER4
Description: 3-phosphoshikimate 1-carboxyvinyltransferase EC number: 2.5.1.19 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00215600}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00527849}. Pathway: PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_00210}. Active site: ACT_SITE 301 301 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_00210}.; ACT_SITE 329 329 Proton donor. {ECO:0000256|HAMAP-Rule:MF_00210}. Binding site: BINDING 29 29 Shikimate-3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00210}.; BINDING 117 117 Phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00210}.; BINDING 188 188 Shikimate-3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00210}.; BINDING 328 328 Shikimate-3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00210}.; BINDING 332 332 Phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00210}.; BINDING 375 375 Phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00210}.; BINDING 401 401 Phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00210}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): aroA Gene names (synonym): Mass: 45,339 Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00527867}. Gene ontology (GO): cytoplasm [GO:0005737]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] Gene ontology IDs: GO:0003866; GO:0005737; GO:0009073; GO:0009423 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00567303}. Protein families: EPSP synthase family Coiled coil: Domain [FT]: DOMAIN 11 409 EPSP_synthase. {ECO:0000259|Pfam:PF00275}. Motif: Region: REGION 24 25 Shikimate-3-phosphate binding. {ECO:0000256|HAMAP-Rule:MF_00210}.; REGION 87 90 Phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00210}.; REGION 160 162 Shikimate-3-phosphate binding. {ECO:0000256|HAMAP-Rule:MF_00210}. EMBL: CP000896 ProteinModelPortal: A9NER4 MEROPS: EnsemblBacteria KO: ABX80844 UniPathway: K00800 CDD: Gene3D: HAMAP: 3.65.10.10 InterPro: MF_00210 PANTHER: IPR001986;IPR006264;IPR023193;IPR013792 PIRSF: PRINTS: PIRSF000505 PROSITE: Pfam: PS00885 ProDom: PF00275 SMART: SUPFAM: TIGRFAMs: SSF55205 |
210219-211461(+) >nucleotide sequence TTATCACACCGATATGTACTTGCAGCAGCTCTTGCACATGGACAATCAAAGATTGATAAC ATATTAGACTCTGATGATTTAATAGCCACACAAAGCGCTTTAAAAAGTTTAGGTGCAACC ATTAATCAAGGATTAATTACAGGTGGTAAGGTTCAAAGAGTACATGAAACTATTGATTGT TTTGAGTCTGGTTCTACATTAAGATTTTTAATTCCGGTCGCAATGCTTCAAGATAAACCT GTGACATTCACGGGTAAAAATCAACTACCATTTCGTACTCAAGAAATGTATGAAAACCTC TTTAAAGAAACTTATCAATTTGAGCATCCAAAAGATAAGTGGTTACCACTTACTGTAAGT GGTCCACTTAAAGGTGGTACATATCACTTAAGAGGTGATGTAAGTAGCCAGTTTATTACA GGCTTACTTTATGCTTTACCACTTGCACCAAATGATTCTGAAATTATTTTAACCTCGCAC TTAGAATCTGTTGGTTATGTAGATATGACACTCGATGTATTAGATAAATTTGGTATTAAG ATTATTAAAACTGTAAATGGTTATAAGATACCTGGAAACCAACACTATAATCCGGGCAAC TACAGTGTAGAAGGTGATTTTAGTGGGGCAGCATTTTTTGTTGCAGCAGGCTTACTTGCT GGACCAATTCACTTAACTAATTTAAATCACCATAGTTTACAAGGTGATAAAGAAATTATT GATCTTGCAGTGAAGATGGGTGGAGATATTACACCCACAAGTGAAGGTTATTTGGTTAAA CCATCTAAATTAAAAGGTATTTCTATTGATGTCGGACAAATTCCAGATTTAGGTCCGATA CTTATGGTACTTGGTGCACTTGCAGAAGGTACTACAATTATTCATAACGCATCTAGATTA CGTATTAAAGAATCTGATAGATTAAATGCTATGGTAACAAACCTTAAAGCACTTGGTGCA AACATTAAAGAAATAGGGGATACTGTAGAAATTAAAGGTGTTTCTAAACTAAAAGGCGGC GTTCTAGTTTCAAGTTATAAAGATCATAGAATTGCCATGTCGATGGCGGTTGCCTCCATC ATGTGCGAACAACCAATTACACTAGATGATGAGACTGTAGTGTCTAAAAGTTATCCAAAT TTCTTTGAAAGTTTTAAAGCGTTAGGAGGTCAAGTAAAGTGA >protein sequence INQGLITGGKVQRVHETIDCFESGSTLRFLIPVAMLQDKPVTFTGKNQLPFRTQEMYENL FKETYQFEHPKDKWLPLTVSGPLKGGTYHLRGDVSSQFITGLLYALPLAPNDSEIILTSH LESVGYVDMTLDVLDKFGIKIIKTVNGYKIPGNQHYNPGNYSVEGDFSGAAFFVAAGLLA GPIHLTNLNHHSLQGDKEIIDLAVKMGGDITPTSEGYLVKPSKLKGISIDVGQIPDLGPI LMVLGALAEGTTIIHNASRLRIKESDRLNAMVTNLKALGANIKEIGDTVEIKGVSKLKGG VLVSSYKDHRIAMSMAVASIMCEQPITLDDETVVSKSYPNFFESFKALGGQVKW |
© Fisunov Lab of Proteomics, 2016.