ID ASNA_HAEI8 Reviewed; 330 AA. AC Q4QMY5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Aspartate--ammonia ligase; DE EC=6.3.1.1; DE AltName: Full=Asparagine synthetase A; GN Name=asnA; OrderedLocusNames=NTHI0692; OS Haemophilus influenzae (strain 86-028NP). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=281310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005; RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., RA Munson R.S. Jr.; RT "Genomic sequence of an otitis media isolate of nontypeable RT Haemophilus influenzae: comparative study with H. influenzae serotype RT d, strain KW20."; RL J. Bacteriol. 187:4627-4636(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; CP000057; AAX87612.1; -; Genomic_DNA. DR RefSeq; YP_248272.1; -. DR GeneID; 3430000; -. DR GenomeReviews; CP000057_GR; NTHI0692. DR KEGG; hit:NTHI0692; -. DR HOGENOM; Q4QMY5; -. DR OMA; Q4QMY5; LNDNLNG. DR BioCyc; HINF281310:NTHI0692-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_1000017946. SQ SEQUENCE 330 AA; 37465 MW; 3AC5C7401EA22F41 CRC64; MKKTFILQQQ EISFVKNTFT QNLIEQLGII EVQGPILSQV GNGMQDNLSG IEKAVQVNVK CIPNAIFEVV HSLAKWKRHT LARFNFKEDE GLFVHMKALR PDEDSLDPTH SVYVDQWDWE KVIPEGRRNF AYLKETVNSI YRAIRLTELA VEARFDIPSI LPKQITFVHS EDLVKRYPDL SSKERENAIC KEYGAVFLIG IGGKLSDGKP HDGRAPDYDD WTTESENGYK GLNGDILVWN DQLGKAFELS SMGIRVDESA LRLQVGLTGD EDRLKMDWHQ DLLNGKLPLT IGGGIGQSRL AMLLLRKKHI GEVQSSVWPK EMLEEFSNIL //