GCW_03470
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Uniprot: A0A0F6CLA0
Description: asparagine synthase EC number: 6.3.1.1 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-aspartate + NH(3) = AMP + diphosphate + L-asparagine. {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00511418}. Cofactor: Enzyme regulation: Function [CC]: Pathway: PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00511426}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): asnA Gene names (synonym): Mass: 37,761 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; aminoacyl-tRNA ligase activity [GO:0004812]; aspartate-ammonia ligase activity [GO:0004071]; ATP binding [GO:0005524]; L-asparagine biosynthetic process [GO:0070981]; tRNA aminoacylation for protein translation [GO:0006418] Gene ontology IDs: GO:0004071; GO:0004812; GO:0005524; GO:0005737; GO:0006418; GO:0070981 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily. {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00571261}. Protein families: Class-II aminoacyl-tRNA synthetase family, AsnA subfamily Coiled coil: Domain [FT]: DOMAIN 92 313 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:PS50862}. Motif: Region: EMBL: CP006916 ProteinModelPortal: MEROPS: EnsemblBacteria KO: AHB99872 UniPathway: K01914 CDD: Gene3D: cd00645 HAMAP: InterPro: MF_00555 PANTHER: IPR006195;IPR004618 PIRSF: PRINTS: PIRSF001555 PROSITE: Pfam: PS50862 ProDom: PF03590 SMART: SUPFAM: TIGRFAMs: 838719-839703(+) >nucleotide sequence CAGAACGCTTTATCAAAAGAACTAAATTTACTAAGAGTGAGTGCTCCTTTGATTATCACT CCTAACTCAGGGTTGAATGACAACCTTAATGGTTGAGAAGCTCCAGTTTCATTTAAATCA AAAACTAATGGTGTTAGTTCACAAGTCGTTCAATCTTTAGCAAAATGAAAAAGATATTCA ATTGCTAGATATGAAATTCCTTTATATCAAGGTTTATACACTGACATGAATGCAATCAGA ATGGATGAGACTCTTGATGCTACACACTCAATGTACGTTGATCAATGAGACTGAGAATTA AGAATCAGTGAAAATGATCGTAATGTCGAGTTTTTAAAGAACACTGTTAATAAAATTTAT AAAGTTCTTAAAGAAGCACAACTAAAAGTTAACGAAAAATACGGTATTTTTGAACAAAAA GACTTGTTACCTGAACATATTCACTTCGTAACTACTCAAGAATTACTAGATCAATATCCT GATAAAACTCCATCTGAAAGAGAGCAACTTGTATGTGAGAAATACAAAGCGGTATTTGTA ATGCAAGTAGGTAAAAAATTATCTAACAATCAAGTACATGATGGTAGATCTCCAGACTAT GACGATTGATCATTAAATGGTGATATTATGGTTTACAACCCTAGGTCTAAAAAAGCATTA GAGTTGTCATCAATGGGAATTCGCGTAAATAAAGAAGTTTTACTTAAACAATTAGAAGAA TCTAAACAAAATGAGCGTTTGCAACTAATGTTCCACAAGAAATTAGTTAATGGTGAATTG CACCAAACTATCGGTGGTGGAATTGGTCAATCAAGATTATGTTACTTCTTGTTACAAAAA GACCACATTGGTGAAGTACAAGCTTCGCACTGAAGTGATGAAATTATTGCTGAAGCTAAA GCAAAAGGGATTAAGTTACTTTAA >protein sequence KTNGVSSQVVQSLAKWKRYSIARYEIPLYQGLYTDMNAIRMDETLDATHSMYVDQWDWEL RISENDRNVEFLKNTVNKIYKVLKEAQLKVNEKYGIFEQKDLLPEHIHFVTTQELLDQYP DKTPSEREQLVCEKYKAVFVMQVGKKLSNNQVHDGRSPDYDDWSLNGDIMVYNPRSKKAL ELSSMGIRVNKEVLLKQLEESKQNERLQLMFHKKLVNGELHQTIGGGIGQSRLCYFLLQK DHIGEVQASHWSDEIIAEAKAKGIKLL |
© Fisunov Lab of Proteomics, 2016.