ID ASNA_STRPM Reviewed; 330 AA. AC Q48SJ3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Aspartate--ammonia ligase; DE EC=6.3.1.1; DE AltName: Full=Asparagine synthetase A; GN Name=asnA; OrderedLocusNames=M28_Spy1207; OS Streptococcus pyogenes serotype M28. OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=319700; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGAS6180 / Serotype M28; RX PubMed=16088825; DOI=10.1086/430618; RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., RA Beres S.B., Lefebvre R.B., Musser J.M.; RT "Genome sequence of a serotype M28 strain of group A Streptococcus: RT potential new insights into puerperal sepsis and bacterial disease RT specificity."; RL J. Infect. Dis. 192:760-770(2005). 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; CP000056; AAX72317.1; -; Genomic_DNA. DR RefSeq; YP_280672.1; -. DR GeneID; 3573915; -. DR GenomeReviews; CP000056_GR; M28_Spy1207. DR KEGG; spb:M28_Spy1207; -. DR HOGENOM; Q48SJ3; -. DR OMA; Q48SJ3; LNDNLNG. DR BioCyc; SPYO319701:M28_SPY1207-MON; -. 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_1000017970. SQ SEQUENCE 330 AA; 37399 MW; 255B344AB733920F CRC64; MKKSFIHQQE EISFVKNTFT QYLIAKLDVV EVQGPILSRV GDGMQDNLSG TENPVSVNVL KIPNATFEVV HSLAKWKRHT LARFGFNEGE GLVVNMKALR PDEDSLDQTH SVYVDQWDWE KVIPDGKRNL AYLKETVETI YKVIRLTELA VEARYDIEAV LPKKITFIHT EELVAKYPDL TPKERENAIT KEFGAVFLIG IGGVLPDGKP HDGRAPDYDD WTTETENGYH GLNGDILVWN DQLGSAFELS SMGIRVDEEA LKRQVEMTGD QDRLAFDWHK SLLNGLFPLT IGGGIGQSRM VMFLLRKKHI GEVQTSVWPQ EVRDSYDNIL //