ID   ASNA_LACDB              Reviewed;         338 AA.
AC   Q04A69;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Aspartate--ammonia ligase;
DE            EC=6.3.1.1;
DE   AltName: Full=Asparagine synthetase A;
GN   Name=asnA; OrderedLocusNames=LBUL_1110;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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.
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DR   EMBL; CP000412; ABJ58653.1; -; Genomic_DNA.
DR   RefSeq; YP_813091.1; -.
DR   GeneID; 4435440; -.
DR   GenomeReviews; CP000412_GR; LBUL_1110.
DR   KEGG; lbu:LBUL_1110; -.
DR   OMA; Q04A69; 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    338       Aspartate--ammonia ligase.
FT                                /FTId=PRO_1000017952.
SQ   SEQUENCE   338 AA;  38770 MW;  E94B91D9173F8D61 CRC64;
     MAKLIIPSDY DPKMTIRETE KAIRYIRETF QTEFGTAMNL ERISAPMFVK KSSGLNDNLS
     GWEKPVSFTL HDGNEGELQI VHSLAKWKRW ALKHYGFSHG EGLFTNMNAI RKDEEVLDNL
     HSVYVDQWDW EKVIDKSERT EATLRQTVQR IFETIKGMEY HVRALYPQAA YHLPEEISFV
     TSEELEARWP SLTPSEREDK ICQEKGAVFL EHIGGALPLS KKPHDLRAPD YDDWTLNGDL
     LFWYEPLQRA FEVSSMGIRV DEDRLQEQLK LAGAEDRLDL PFHQALLKGD LPYSIGGGIG
     QSRLCMLLLG KAHIGEVQAS IWPDEIVEKC QAAKIQLL
//