ASNA_SHISS
ID ASNA_SHISS Reviewed; 330 AA.
AC Q3YVP8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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}; OrderedLocusNames=SSON_3875;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ90414.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YVP8; -.
DR SMR; Q3YVP8; -.
DR EnsemblBacteria; AAZ90414; AAZ90414; SSON_3875.
DR KEGG; ssn:SSON_3875; -.
DR HOGENOM; CLU_071543_0_0_6; -.
DR OMA; QSRICMF; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000002529; 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_1000017962"
SQ SEQUENCE 330 AA; 36677 MW; 6E8D3A2ACE43CFC6 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 EDRLQLEWHQ ALLRGEMPQT IGGGIGQSRL
TMLLLQLPHI GQVQCGVWPA AVRENVPSLL
