ID   ASNA_ECOLI              Reviewed;         330 AA.
AC   P00963; Q2M862;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   10-JUN-2026, entry version 200.
DE   RecName: Full=Aspartate--ammonia ligase;
DE            EC=6.3.1.1 {ECO:0000269|PubMed:1369484};
DE   AltName: Full=Asparagine synthetase A;
GN   Name=asnA; OrderedLocusNames=b3744, JW3722;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=6117826; DOI=10.1093/nar/9.18.4669;
RA   Nakamura M., Yamada M., Hirota Y., Sugimoto K., Oka A., Takanami M.;
RT   "Nucleotide sequence of the asnA gene coding for asparagine synthetase of
RT   E. coli K-12.";
RL   Nucleic Acids Res. 9:4669-4676(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6357950; DOI=10.1016/0378-1119(83)90087-2;
RA   Buhk H.-J., Messer W.;
RT   "The replication origin region of Escherichia coli: nucleotide sequence and
RT   functional units.";
RL   Gene 24:265-279(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
RX   PubMed=383377; DOI=10.1101/sqb.1979.043.01.019;
RA   Hirota Y., Yasuda S., Yamada M., Nishimura A., Sugimoto K., Sugisaki H.,
RA   Oka A., Takanami M.;
RT   "Structural and functional properties of the Escherichia coli origin of DNA
RT   replication.";
RL   Cold Spring Harb. Symp. Quant. Biol. 43:129-138(1979).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-5, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12;
RX   PubMed=1369484; DOI=10.1271/bbb.56.376;
RA   Sugiyama A., Kato H., Nishioka T., Oda J.;
RT   "Overexpression and purification of asparagine synthetase from Escherichia
RT   coli.";
RL   Biosci. Biotechnol. Biochem. 56:376-379(1992).
RN   [8]
RP   FUNCTION IN PRODUCTION OF EXTRACELLULAR DEATH FACTOR (EDF), AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17962566; DOI=10.1126/science.1147248;
RA   Kolodkin-Gal I., Hazan R., Gaathon A., Carmeli S., Engelberg-Kulka H.;
RT   "A linear pentapeptide is a quorum-sensing factor required for mazEF-
RT   mediated cell death in Escherichia coli.";
RL   Science 318:652-655(2007).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC   STRAIN=K12;
RX   PubMed=9437423; DOI=10.1038/nsb0198-15;
RA   Nakatsu T., Kato H., Oda J.;
RT   "Crystal structure of asparagine synthetase reveals a close evolutionary
RT   relationship to class II aminoacyl-tRNA synthetase.";
RL   Nat. Struct. Biol. 5:15-19(1998).
CC   -!- FUNCTION: May amidate Asp of the extracellular death factor precursor
CC       Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn.
CC       {ECO:0000305|PubMed:17962566}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate + NH4(+) + ATP = L-asparagine + AMP + diphosphate
CC         + H(+); Xref=Rhea:RHEA:11372, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58048, ChEBI:CHEBI:456215; EC=6.3.1.1;
CC         Evidence={ECO:0000269|PubMed:1369484};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11373;
CC         Evidence={ECO:0000305|PubMed:1369484};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (ammonia route): step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P00963; P00963: asnA; NbExp=2; IntAct=EBI-1117481, EBI-1117481;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DISRUPTION PHENOTYPE: Loss of production of extracellular death factor.
CC       {ECO:0000269|PubMed:17962566}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       AsnA subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; V00263; CAA23512.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; K00826; AAA24253.1; -; Genomic_DNA.
DR   EMBL; J01657; AAA24248.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62096.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76767.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77544.1; -; Genomic_DNA.
DR   EMBL; M10679; AAA24249.1; -; Genomic_DNA.
DR   PIR; A01191; AJECNA.
DR   RefSeq; NP_418200.1; NC_000913.3.
DR   RefSeq; WP_000845104.1; NZ_CP009789.1.
DR   PDB; 11AS; X-ray; 2.50 A; A/B=1-330.
DR   PDB; 12AS; X-ray; 2.20 A; A/B=1-330.
DR   AlphaFoldDB; P00963; -.
DR   SMR; P00963; -.
DR   BioGRID; 4263263; 118.
DR   BioGRID; 852560; 2.
DR   DIP; DIP-9176N; -.
DR   FunCoup; P00963; 207.
DR   IntAct; P00963; 6.
DR   STRING; 511145.b3744; -.
DR   jPOST; P00963; -.
DR   PaxDb; 511145-b3744; -.
DR   EnsemblBacteria; AAC76767; AAC76767; b3744.
DR   GeneID; 948258; -.
DR   KEGG; ecj:JW3722; -.
DR   KEGG; eco:b3744; -.
DR   KEGG; ecoc:C3026_20285; -.
DR   PATRIC; fig|1411691.4.peg.2956; -.
DR   EchoBASE; EB0089; -.
DR   eggNOG; COG2502; Bacteria.
DR   HOGENOM; CLU_071543_0_0_6; -.
DR   InParanoid; P00963; -.
DR   OMA; QSRICMF; -.
DR   OrthoDB; 3185462at2; -.
DR   PhylomeDB; P00963; -.
DR   BioCyc; EcoCyc:ASNSYNA-MONOMER; -.
DR   BioCyc; MetaCyc:ASNSYNA-MONOMER; -.
DR   UniPathway; UPA00134; UER00194.
DR   EvolutionaryTrace; P00963; -.
DR   PRO; PR:P00963; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P00963; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004071; F:aspartate-ammonia ligase activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00645; AsnA; 1.
DR   FunFam; 3.30.930.10:FF:000025; Aspartate--ammonia ligase; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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   NCBIfam; TIGR00669; asnA; 1.
DR   PANTHER; PTHR30073; ASPARTATE--AMMONIA LIGASE; 1.
DR   PANTHER; PTHR30073:SF5; ASPARTATE--AMMONIA LIGASE; 1.
DR   Pfam; PF03590; AsnA; 1.
DR   PIRSF; PIRSF001555; Asp_ammon_ligase; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PDBsum; 11AS; -.
DR   PDBsum; 12AS; -.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Asparagine biosynthesis;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..330
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_0000195873"
FT   HELIX           5..27
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   TURN            48..51
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           76..83
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          112..122
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           130..154
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           170..176
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           182..193
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:11AS"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:11AS"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          232..240
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   TURN            241..244
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          245..255
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           258..268
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           277..283
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   STRAND          290..296
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           297..305
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           310..312
FT                   /evidence="ECO:0007829|PDB:12AS"
FT   HELIX           320..325
FT                   /evidence="ECO:0007829|PDB:12AS"
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
//