ID   ASNA_ECOUT              Reviewed;         330 AA.
AC   Q1R4I8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-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=UTI89_C4299;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE09726.1; -; Genomic_DNA.
DR   RefSeq; YP_543257.1; -.
DR   SMR; Q1R4I8; 4-330.
DR   GeneID; 3994421; -.
DR   GenomeReviews; CP000243_GR; UTI89_C4299.
DR   KEGG; eci:UTI89_C4299; -.
DR   HOGENOM; Q1R4I8; -.
DR   OMA; Q1R4I8; LNDNLNG.
DR   BioCyc; ECOL364106:UTI89_C4299-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_1000017943.
SQ   SEQUENCE   330 AA;  36723 MW;  26554E290C972D0A CRC64;
     MKTAYIAKQR QISFVKSHFS RQLEERLGLI EVQAPILSRV GDGTQDNLSG CEKAVQVKVK
     ALPDAQFEVV HSLAKWKRQT LGQHDFSAGE GLYTHMKALR PDEDRLSPLH SVYVDQWDWE
     RVMGDGERQF STLKSTVEAI WEGIKATEAA VSEEFGLAPF LPDQIHFVHS QELLSRYPEL
     DAKGRERAIA KDLGAVFLVG IGGKLSDGHR HDVRAPDYDD WSTPSELGHA GLNGDILVWN
     PVLEDAFELS SMGIRVDADT LKHQLALTGD EDRLELEWHQ ALLRGEMPQT IGGGIGQSRL
     TMLLLQLPHI GQVQCGVWPA AVRESVPSLL
//