ID ASNA_STRP6 Reviewed; 330 AA. AC Q5XAY8; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 16-JUN-2009, entry version 33. DE RecName: Full=Aspartate--ammonia ligase; DE EC=6.3.1.1; DE AltName: Full=Asparagine synthetase A; GN Name=asnA; OrderedLocusNames=M6_Spy1290; OS Streptococcus pyogenes serotype M6. OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=301450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-946 / MGAS10394 / Serotype M6; RX PubMed=15272401; DOI=10.1086/422697; RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.; RT "Progress toward characterization of the group A Streptococcus RT metagenome: complete genome sequence of a macrolide-resistant serotype RT M6 strain."; RL J. Infect. Dis. 190:727-738(2004). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + NH(3) = AMP + diphosphate CC + L-asparagine. CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L- CC asparagine from L-aspartate (ammonia route): step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. AsnA subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000003; AAT87425.1; -; Genomic_DNA. DR RefSeq; YP_060608.1; -. DR GeneID; 2942371; -. DR GenomeReviews; CP000003_GR; M6_Spy1290. DR KEGG; spa:M6_Spy1290; -. DR HOGENOM; Q5XAY8; -. DR OMA; Q5XAY8; LNDNLNG. DR BioCyc; SPYO286636:M6_SPY1290-MON; -. DR BRENDA; 6.3.1.1; 314561. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro. DR GO; GO:0004071; F:aspartate-ammonia ligase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0006529; P:asparagine biosynthetic process; IEA:HAMAP. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro. DR HAMAP; MF_00555; -; 1. DR InterPro; IPR006195; aa-tRNA-synth_II_cons-reg. DR InterPro; IPR004618; AsnA. DR Pfam; PF03590; AsnA; 1. DR PIRSF; PIRSF001555; Asp_ammon_ligase; 1. DR ProDom; PD024629; AsnA; 1. DR TIGRFAMs; TIGR00669; asnA; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding. FT CHAIN 1 330 Aspartate--ammonia ligase. FT /FTId=PRO_0000195895. SQ SEQUENCE 330 AA; 37357 MW; 38EC443DADF39CEA CRC64; MKKSFIHQQE EISFVKNTFT QYLIAKLDVV EVQGPILSRV GDGMQDNLSG TENPVSVNVL KIPNATFEVV HSLAKWKRHT LARFGFNEGE GLVVNMKALR PDEDSLDQTH SVYVDQWDWE KVIPDGKRNL AYLKETVETI YKVIRLTELA VEARYDIEAV LPKKITFIHT EELVAKYPDL TPKERENAIT KEFGAVFLIG IGGGLPDGKP HDGRAPDYDD WTTETENGYH GLNGDLLVWN DQLGSAFELS SMGIRVDEEA LKRQVEMTGD QDRLAFDWHK SLLNGLFPLT IGGGIGQSRM VMFLLRKKHI GEVQTSVWPQ EVRDSYDNIL //