ACL_RS03860
  | Uniprot: A9NGB2
Description: tryptophan synthase subunit beta EC number: 4.2.1.20 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00015899}. Cofactor: COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00166768}; Enzyme regulation: Function [CC]: FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}. Pathway: PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00015996}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): trpB Gene names (synonym): Mass: 42,603 Subunit structure [CC]: SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00216216}. Gene ontology (GO): tryptophan synthase activity [GO:0004834] Gene ontology IDs: GO:0004834 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the TrpB family. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541094}. Protein families: TrpB family Coiled coil: Domain [FT]: DOMAIN 46 372 PALP. {ECO:0000259|Pfam:PF00291}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NGB2 MEROPS: EnsemblBacteria KO: ABX81392 UniPathway: K01696 CDD: Gene3D: HAMAP: InterPro: MF_00133 PANTHER: IPR006653;IPR006654;IPR023026;IPR001926 PIRSF: PTHR10314:SF3 PRINTS: PIRSF001413 PROSITE: Pfam: PS00168 ProDom: PF00291 SMART: SUPFAM: TIGRFAMs: SSF53686 |
813254-814430(-) >nucleotide sequence ACCAGATAAGTTAACAACAATAATCTGATCCTTTGGTAAAGTTTTTGCAAGCGATATTGC ATAGGCTAGAGCATGAGAGGATTCTATTGCAGGTATGATACCTTCTATAAGTGTTAAATA CTCAAATGCTTGTACAGCTTCTTCATCTGTTGCACCAAAGTAAGTAACACGTTTAATTTC ATCTAAATATGCATGTTCTGGACCAACACCAGGGTAGTCAAGTCCGGCAGAAATCGAGTA TACTGGTGAAATTTCACCTTTATCATCCAATAAAACTTTAGTCTTCATTCCATGAATAAC CCCAGTTTGACCAAGTGTCATCGTAGCAGCATGTAAATTTGTATCTAAACCTTTACCTAA CGCTTCAACGCCAATAAGTTTTACAGTAGGATCCGGAATAAAATCAAAGAATGCACCAAT TGCATTAGACCCGCCACCAACACAAGCAATGACATAATCTGGTAGTCTATTTTCTAATTT TAGTATTTGTTCTTTAATCTCAATACCAATAACTTTTTGGAAATCACGAACCATCATCGG ATATGGATGTGGTCCAACTGCTGAACCAATTAAGTAAAACATTGATTCATGTTCAGTACT CCATTTTATTAAAGCACTATCAACAGCTTCTTTAAGTGTTCTTAATCCTTCTTGAACACT AACTACAGTTGCACCTAAAAGTTGCATCTTATAAACATTAAGTGCTTGTTTTTCAACATC TACTGCACCCATATGAATTTCACATTCTAAACCAAGTAGTGCTGCTACAGTTGCAGTGGC TACACCATGTTGTCCAGCACCTGTTTCTGCAATCAACTTCTTTTTACCCATACGTTTAGC AAGTAACGCTTGCCCAATGACATTATTAATTTTGTGAGAACCTGTATGATTTAAGTCTTC ACGTTTTAAATATACTTTTGCACCACCAAGACATTCTGTTAAGCGTTTAGCAAAATACAA ATTAGAAGGTCTACCAGCATATGTATTGAGTAAGTCTTTAAATTCTTCAATAAATGCAGG ATCATCCTTGAATTTATTATATGCATCCTCTACTTCTTTAATTGCGGTAAGTAAGTACGG TGGTAAGTATGCCCCACCAAATTGTCCAAATTCCAT >protein sequence ECLGGAKVYLKREDLNHTGSHKINNVIGQALLAKRMGKKKLIAETGAGQHGVATATVAAL LGLECEIHMGAVDVEKQALNVYKMQLLGATVVSVQEGLRTLKEAVDSALIKWSTEHESMF YLIGSAVGPHPYPMMVRDFQKVIGIEIKEQILKLENRLPDYVIACVGGGSNAIGAFFDFI PDPTVKLIGVEALGKGLDTNLHAATMTLGQTGVIHGMKTKVLLDDKGEISPVYSISAGLD YPGVGPEHAYLDEIKRVTYFGATDEEAVQAFEYLTLIEGIIPAIESSHALAYAISLAKTL PKDQIIVVNLSGRGDKDVKHIARFRGFEIVDW |
© Fisunov Lab of Proteomics, 2016.