ID   ASNA_LACS1              Reviewed;         336 AA.
AC   Q1WTD6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Aspartate--ammonia ligase;
DE            EC=6.3.1.1;
DE   AltName: Full=Asparagine synthetase A;
GN   Name=asnA; OrderedLocusNames=LSL_1033;
OS   Lactobacillus salivarius subsp. salivarius (strain UCC118).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C.,
RA   Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F.,
RA   van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99841.1; -; Genomic_DNA.
DR   RefSeq; YP_535924.1; -.
DR   GeneID; 3977019; -.
DR   GenomeReviews; CP000233_GR; LSL_1033.
DR   KEGG; lsl:LSL_1033; -.
DR   HOGENOM; Q1WTD6; -.
DR   OMA; Q1WTD6; LNDNLNG.
DR   BioCyc; LSAL362948:LSL_1033-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    336       Aspartate--ammonia ligase.
FT                                /FTId=PRO_1000017953.
SQ   SEQUENCE   336 AA;  39133 MW;  C296A67F4BF5C4CF CRC64;
     MDLIIPKDYD PKLSIRETQE AIRYIRETFQ DEFGKEMGLN RVSAPMYVEK SSGINDNLNG
     YEKPVSFTMK DMPGETIEVV HSLAKWKRMA LKKYGFGLHE GLYTNMNAIR KDEDLDNFHS
     SYVDQWDWEK VISKDERNEK TLKETVELIF KVVKHMEHEV WYKFPNAVYH LPDKIHFITS
     QELEDKYPEL EDAKDRENAI CKELGCVFVM QIGDVLKSGK RHDGRAPDYD DWKLNGDILF
     WYEPLQCALE LSSMGIRVDE DSMVEQLKKT GDEDRLKLQY HKMILNKELP YTIGGGIGQS
     RLCMLLLGKA HVGEVQASIW PDEMLKKCEE NGIHIL
//