ID   ASNA_ECOL5              Reviewed;         330 AA.
AC   Q0TAW5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Aspartate--ammonia ligase;
DE            EC=6.3.1.1;
DE   AltName: Full=Asparagine synthetase A;
GN   Name=asnA; OrderedLocusNames=ECP_3943;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; CP000247; ABG71914.1; -; Genomic_DNA.
DR   RefSeq; YP_671815.1; -.
DR   SMR; Q0TAW5; 4-330.
DR   GeneID; 4189322; -.
DR   GenomeReviews; CP000247_GR; ECP_3943.
DR   KEGG; ecp:ECP_3943; -.
DR   HOGENOM; Q0TAW5; -.
DR   OMA; Q0TAW5; LNDNLNG.
DR   BioCyc; ECOL362663:ECP_3943-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_1000017942.
SQ   SEQUENCE   330 AA;  36651 MW;  2A8D2E3ECE523FDD CRC64;
     MKTAYIAKQR QISFVKSHFS RQLEERLGLI EVQAPILSRV GDGTQDNLSG CEKAVQVKVK
     ALPDAQFEVV HSLAKWKRQT LGQHDFSAGE GLYTHMKALR PDEDRLSPLH SVYVDQWDWE
     RVMGDGERQF STLKSTVEAI WAGIKATEAA VSEEFGLAPF LPDQIHFVHS QELLSRYPDL
     DAKGRERAIA KDLGAVFLVG IGGKLSDGHR HDVRAPDYDD WSTPSELGHA GLNGDILVWN
     PVLEDAFELS SMGIRVDADT LKHQLALTGD EDRLELEWHQ ALLRGEMPQT IGGGIGQSRL
     TMLLLQLPHI GQVQCGVWPA AVRESVPSLL
//