ID ASNA_STRP2 Reviewed; 330 AA. AC Q04IJ8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=Aspartate--ammonia ligase; DE EC=6.3.1.1; DE AltName: Full=Asparagine synthetase A; GN Name=asnA; OrderedLocusNames=SPD_1768; OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=373153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17041037; DOI=10.1128/JB.01148-06; RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., RA Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.; RT "Genome sequence of Avery's virulent serotype 2 strain D39 of RT Streptococcus pneumoniae and comparison with that of unencapsulated RT laboratory strain R6."; RL J. Bacteriol. 189:38-51(2007). 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; CP000410; ABJ54080.1; -; Genomic_DNA. DR RefSeq; YP_817190.1; -. DR GeneID; 4441684; -. DR GenomeReviews; CP000410_GR; SPD_1768. DR KEGG; spd:SPD_1768; -. DR OMA; Q04IJ8; LNDNLNG. 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_1000017964. SQ SEQUENCE 330 AA; 37608 MW; BF01477215EC39C5 CRC64; MKKSFIHQQE EISFVKNTFT QYLKDKLEVV EVQGPILSKV GDGMQDNLSG VENPVSVKVL QIPDATYEVV HSLAKWKRHT LARFGFGEGE GLFVHMKALR PDEDSLDATH SVYVDQWDWE KVIPNGKRNI VYLKETVEKI YKAIRLTELA VEARYDIESI LPKQITFIHT EELVERYPDL TSKERENAIC KEFGAVFLIG IGGELPDGKP HDGRAPDYDD WTSESENGYK GLNGDILVWN ESLGGAFELS SMGIRVDEET LRRQVEITGD EDRLELEWHK SLLNGLFPLT IGGGIGQSRM AMFLLRKRHI GEVQTSVWPQ EVRDTYENIL //