GCW_03470







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
ATGAAAAAATTAACATTGCTAGAAACAGAATTAGCCATTAAATATATTAAGGATCTGTTT
CAGAACGCTTTATCAAAAGAACTAAATTTACTAAGAGTGAGTGCTCCTTTGATTATCACT
CCTAACTCAGGGTTGAATGACAACCTTAATGGTTGAGAAGCTCCAGTTTCATTTAAATCA
AAAACTAATGGTGTTAGTTCACAAGTCGTTCAATCTTTAGCAAAATGAAAAAGATATTCA
ATTGCTAGATATGAAATTCCTTTATATCAAGGTTTATACACTGACATGAATGCAATCAGA
ATGGATGAGACTCTTGATGCTACACACTCAATGTACGTTGATCAATGAGACTGAGAATTA
AGAATCAGTGAAAATGATCGTAATGTCGAGTTTTTAAAGAACACTGTTAATAAAATTTAT
AAAGTTCTTAAAGAAGCACAACTAAAAGTTAACGAAAAATACGGTATTTTTGAACAAAAA
GACTTGTTACCTGAACATATTCACTTCGTAACTACTCAAGAATTACTAGATCAATATCCT
GATAAAACTCCATCTGAAAGAGAGCAACTTGTATGTGAGAAATACAAAGCGGTATTTGTA
ATGCAAGTAGGTAAAAAATTATCTAACAATCAAGTACATGATGGTAGATCTCCAGACTAT
GACGATTGATCATTAAATGGTGATATTATGGTTTACAACCCTAGGTCTAAAAAAGCATTA
GAGTTGTCATCAATGGGAATTCGCGTAAATAAAGAAGTTTTACTTAAACAATTAGAAGAA
TCTAAACAAAATGAGCGTTTGCAACTAATGTTCCACAAGAAATTAGTTAATGGTGAATTG
CACCAAACTATCGGTGGTGGAATTGGTCAATCAAGATTATGTTACTTCTTGTTACAAAAA
GACCACATTGGTGAAGTACAAGCTTCGCACTGAAGTGATGAAATTATTGCTGAAGCTAAA
GCAAAAGGGATTAAGTTACTTTAA


>protein sequence
MKKLTLLETELAIKYIKDLFQNALSKELNLLRVSAPLIITPNSGLNDNLNGWEAPVSFKS
KTNGVSSQVVQSLAKWKRYSIARYEIPLYQGLYTDMNAIRMDETLDATHSMYVDQWDWEL
RISENDRNVEFLKNTVNKIYKVLKEAQLKVNEKYGIFEQKDLLPEHIHFVTTQELLDQYP
DKTPSEREQLVCEKYKAVFVMQVGKKLSNNQVHDGRSPDYDDWSLNGDIMVYNPRSKKAL
ELSSMGIRVNKEVLLKQLEESKQNERLQLMFHKKLVNGELHQTIGGGIGQSRLCYFLLQK
DHIGEVQASHWSDEIIAEAKAKGIKLL






















© Fisunov Lab of Proteomics, 2016.