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
GTGCTAGAAATTATTCCAACCAATTTATCAGGTGAAGTAAAGATTGTTTCATCTAAATCT
TTATCACACCGATATGTACTTGCAGCAGCTCTTGCACATGGACAATCAAAGATTGATAAC
ATATTAGACTCTGATGATTTAATAGCCACACAAAGCGCTTTAAAAAGTTTAGGTGCAACC
ATTAATCAAGGATTAATTACAGGTGGTAAGGTTCAAAGAGTACATGAAACTATTGATTGT
TTTGAGTCTGGTTCTACATTAAGATTTTTAATTCCGGTCGCAATGCTTCAAGATAAACCT
GTGACATTCACGGGTAAAAATCAACTACCATTTCGTACTCAAGAAATGTATGAAAACCTC
TTTAAAGAAACTTATCAATTTGAGCATCCAAAAGATAAGTGGTTACCACTTACTGTAAGT
GGTCCACTTAAAGGTGGTACATATCACTTAAGAGGTGATGTAAGTAGCCAGTTTATTACA
GGCTTACTTTATGCTTTACCACTTGCACCAAATGATTCTGAAATTATTTTAACCTCGCAC
TTAGAATCTGTTGGTTATGTAGATATGACACTCGATGTATTAGATAAATTTGGTATTAAG
ATTATTAAAACTGTAAATGGTTATAAGATACCTGGAAACCAACACTATAATCCGGGCAAC
TACAGTGTAGAAGGTGATTTTAGTGGGGCAGCATTTTTTGTTGCAGCAGGCTTACTTGCT
GGACCAATTCACTTAACTAATTTAAATCACCATAGTTTACAAGGTGATAAAGAAATTATT
GATCTTGCAGTGAAGATGGGTGGAGATATTACACCCACAAGTGAAGGTTATTTGGTTAAA
CCATCTAAATTAAAAGGTATTTCTATTGATGTCGGACAAATTCCAGATTTAGGTCCGATA
CTTATGGTACTTGGTGCACTTGCAGAAGGTACTACAATTATTCATAACGCATCTAGATTA
CGTATTAAAGAATCTGATAGATTAAATGCTATGGTAACAAACCTTAAAGCACTTGGTGCA
AACATTAAAGAAATAGGGGATACTGTAGAAATTAAAGGTGTTTCTAAACTAAAAGGCGGC
GTTCTAGTTTCAAGTTATAAAGATCATAGAATTGCCATGTCGATGGCGGTTGCCTCCATC
ATGTGCGAACAACCAATTACACTAGATGATGAGACTGTAGTGTCTAAAAGTTATCCAAAT
TTCTTTGAAAGTTTTAAAGCGTTAGGAGGTCAAGTAAAGTGA


>protein sequence
VLEIIPTNLSGEVKIVSSKSLSHRYVLAAALAHGQSKIDNILDSDDLIATQSALKSLGAT
INQGLITGGKVQRVHETIDCFESGSTLRFLIPVAMLQDKPVTFTGKNQLPFRTQEMYENL
FKETYQFEHPKDKWLPLTVSGPLKGGTYHLRGDVSSQFITGLLYALPLAPNDSEIILTSH
LESVGYVDMTLDVLDKFGIKIIKTVNGYKIPGNQHYNPGNYSVEGDFSGAAFFVAAGLLA
GPIHLTNLNHHSLQGDKEIIDLAVKMGGDITPTSEGYLVKPSKLKGISIDVGQIPDLGPI
LMVLGALAEGTTIIHNASRLRIKESDRLNAMVTNLKALGANIKEIGDTVEIKGVSKLKGG
VLVSSYKDHRIAMSMAVASIMCEQPITLDDETVVSKSYPNFFESFKALGGQVKW






















© Fisunov Lab of Proteomics, 2016.