Aminodeoxychorismate lyase (Q03266)

Identification
NameAminodeoxychorismate lyase
Synonyms
  • 4-amino-4-deoxychorismate lyase
  • ADC lyase
  • ADCL
Gene NameABZ2
Enzyme Class
Biological Properties
General FunctionInvolved in catalytic activity
Specific FunctionConverts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate
Cellular LocationCytoplasm
SMPDB Pathways
tetrahydrofolate biosynthesisPW002417 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Folate biosynthesisec00790 Map00790
SMPDB Reactions
4-amino-4-deoxychorismate → 4-Aminobenzoic acid + hydron + Pyruvic acid
KEGG Reactions
4-amino-4-deoxychorismic acid → Pyruvic acid + hydron + 4-Aminobenzoic acid
Metabolites
YMDB IDNameView
YMDB00175Pyruvic acidShow
YMDB003144-amino-4-deoxychorismic acidShow
YMDB004934-Aminobenzoic acidShow
YMDB00862hydronShow
YMDB162534-amino-4-deoxychorismateShow
GO Classification
Component
Not Available
Function
catalytic activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYMR289W
Gene Sequence>YMR289W ABZ2 SGDID:S000004902, Chr XIII from 848685-849809, Verified ORF, "Aminodeoxychorismate lyase (4-amino-4-deoxychorismate lyase), catalyzes the third step in para-aminobenzoic acid biosynthesis; involved in folic acid biosynthesis" ATGTCACTAATGGACAATTGGAAGACTGATATGGAAAGTTACGATGAAGGAGGCCTAGTT GCTAATCCGAACTTCGAGGTTCTGGCCACTTTCAGGTACGACCCTGGTTTTGCACGCCAG TCAGCGTCAAAGAAAGAGATCTTTGAAACTCCAGACCCTCGATTAGGTTTGAGAGACGAA GATATTAGGCAGCAGATAATTAATGAGGATTACTCAAGTTATTTACGAGTAAGGGAGGTT AATTCCGGCGGTGACCTTCTCGAAAATATTCAGCATCCTGATGCTTGGAAGCATGATTGC AAGACCATTGTGTGCCAGCGTGTAGAAGATATGCTACAAGTCATTTATGAACGATTTTTT TTATTAGATGAACAATACCAAAGAATAAGAATAGCATTATCATACTTTAAAATTGACTTC AGCACGTCTCTGAATGATTTATTGAAGTTATTGGTTGAAAACTTGATTAATTGTAAAGAA GGAAATTCAGAGTATCACGAAAAAATTCAAAAAATGATCAACGAAAGGCAATGCTATAAA ATGCGGGTACTTGTCTCTAAGACAGGAGATATACGAATTGAGGCAATTCCAATGCCTATG GAGCCTATCCTAAAATTAACAACCGATTATGACAGTGTTTCCACATACTTCATCAAAACG ATGCTCAATGGATTTTTAATTGATAGCACAATAAATTGGGATGTTGTTGTTTCATCTGAA CCATTGAACGCATCAGCTTTCACCAGTTTTAAAACCACTTCAAGAGATCATTACGCTAGG GCGAGAGTTCGCATGCAAACTGCTATAAATAACTTAAGAGGTTCAGAACCTACTTCTTCT GTCTCGCAATGCGAAATTTTATTTTCCAACAAATCTGGCCTGCTGATGGAAGGTTCAATA ACAAACGTGGCTGTAATTCAAAAAGATCCTAACGGTTCTAAAAAGTATGTGACACCAAGA TTAGCAACTGGATGTTTGTGCGGAACAATGCGTCATTATTTATTGCGGCTCGGCCTTATT GAAGAGGGAGATATAGATATAGGAAGCCTTACCGTTGGCAACGAAGTTTTGCTTTTCAAT GGCGTCATGGGATGCATAAAGGGAACAGTGAAGACAAAATATTGA
Protein Properties
Pfam Domain Function
Protein Residues374
Protein Molecular Weight42639.39844
Protein Theoretical pI5.53
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Aminodeoxychorismate lyase MSLMDNWKTDMESYDEGGLVANPNFEVLATFRYDPGFARQSASKKEIFETPDPRLGLRDE DIRQQIINEDYSSYLRVREVNSGGDLLENIQHPDAWKHDCKTIVCQRVEDMLQVIYERFF LLDEQYQRIRIALSYFKIDFSTSLNDLLKLLVENLINCKEGNSEYHEKIQKMINERQCYK MRVLVSKTGDIRIEAIPMPMEPILKLTTDYDSVSTYFIKTMLNGFLIDSTINWDVVVSSE PLNASAFTSFKTTSRDHYARARVRMQTAINNLRGSEPTSSVSQCEILFSNKSGLLMEGSI TNVAVIQKDPNGSKKYVTPRLATGCLCGTMRHYLLRLGLIEEGDIDIGSLTVGNEVLLFN GVMGCIKGTVKTKY
References
External Links
ResourceLink
Saccharomyces Genome Database ABZ2
Uniprot IDQ03266
Uniprot NamePABC_YEAST
General Reference
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106