ASNA_ECOLI
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 03-AUG-2022, entry version 185.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=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: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}.
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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_SSZK01000036.1.
DR RefSeq; YP_006952153.1; NC_019049.1.
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 PDBsum; 11AS; -.
DR PDBsum; 12AS; -.
DR AlphaFoldDB; P00963; -.
DR SMR; P00963; -.
DR BioGRID; 4263263; 112.
DR BioGRID; 852560; 2.
DR DIP; DIP-9176N; -.
DR IntAct; P00963; 6.
DR STRING; 511145.b3744; -.
DR SWISS-2DPAGE; P00963; -.
DR jPOST; P00963; -.
DR PaxDb; P00963; -.
DR PRIDE; P00963; -.
DR EnsemblBacteria; AAC76767; AAC76767; b3744.
DR EnsemblBacteria; BAE77544; BAE77544; BAE77544.
DR GeneID; 948258; -.
DR KEGG; ecj:JW3722; -.
DR KEGG; eco:b3744; -.
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 PhylomeDB; P00963; -.
DR BioCyc; EcoCyc:ASNSYNA-MON; -.
DR BioCyc; MetaCyc:ASNSYNA-MON; -.
DR UniPathway; UPA00134; UER00194.
DR EvolutionaryTrace; P00963; -.
DR PRO; PR:P00963; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0006529; P:asparagine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
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 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 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 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
