ID   ASNA_SHIB3              Reviewed;         330 AA.
AC   B2TUN1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Aspartate--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_00555};
DE            EC=6.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00555};
DE   AltName: Full=Asparagine synthetase A {ECO:0000255|HAMAP-Rule:MF_00555};
GN   Name=asnA {ECO:0000255|HAMAP-Rule:MF_00555};
GN   OrderedLocusNames=SbBS512_E4177;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-
CC         asparagine; Xref=Rhea:RHEA:11372, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:456215; EC=6.3.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00555};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (ammonia route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00555}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00555}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       AsnA subfamily. {ECO:0000255|HAMAP-Rule:MF_00555}.
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DR   EMBL; CP001063; ACD07035.1; -; Genomic_DNA.
DR   RefSeq; WP_000845087.1; NC_010658.1.
DR   AlphaFoldDB; B2TUN1; -.
DR   SMR; B2TUN1; -.
DR   STRING; 344609.SbBS512_E4177; -.
DR   EnsemblBacteria; ACD07035; ACD07035; SbBS512_E4177.
DR   KEGG; sbc:SbBS512_E4177; -.
DR   HOGENOM; CLU_071543_0_0_6; -.
DR   OMA; QSRICMF; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000001030; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004071; F:aspartate-ammonia ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00645; AsnA; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00555; AsnA; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004618; AsnA.
DR   PANTHER; PTHR30073; PTHR30073; 1.
DR   Pfam; PF03590; AsnA; 1.
DR   PIRSF; PIRSF001555; Asp_ammon_ligase; 1.
DR   SUPFAM; SSF55681; SSF55681; 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; Cytoplasm;
KW   Ligase; Nucleotide-binding.
FT   CHAIN           1..330
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_1000129130"
SQ   SEQUENCE   330 AA;  36597 MW;  323CE79B1858527C CRC64;
     MKTAYIAKQR QISFVKSHFS RQLEECLGLI EVQAPILSRV GDGTQDNLSG CEKAVQVKVK
     ALPDAQFEVV HSLAKWKRQT LGQHDFSAGE GLYTHMKALR PDEDRLSPLH SVYVDQWDWE
     RVMGDGERQF STLKSTVEAI WAGIKATEAA VSEEFGLAPF LPDQIHFVHS QELLSRYPDL
     DAKGRERAIA KDLGAVFLVG IGGKLSDGHR HDVRAPDYDD WSTPSELGHA GLNGDILVWN
     PVLEDAFELS SMGIRVDADT LKHQLALTGD EDRLQLEWHQ ALLRGEMPQT IGGGIGQSRL
     TMLLLQLPHI GQVQCGVWPA AVRESVPSLL