ID   ASNA_LACDA              Reviewed;         338 AA.
AC   P54264; Q1G9Z6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   10-JUN-2026, entry version 137.
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=Ldb1194;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8636057; DOI=10.1128/jb.178.8.2459-2461.1996;
RA   Kim S.I., Germond J.-E., Pridmore D., Soell D.;
RT   "Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA
RT   synthetase: coregulation by transcription antitermination?";
RL   J. Bacteriol. 178:2459-2461(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC   NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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: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.
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; X89438; CAA61602.1; -; Genomic_DNA.
DR   EMBL; CR954253; CAI97996.1; -; Genomic_DNA.
DR   PIR; S71073; S71073.
DR   RefSeq; WP_011543942.1; NC_008054.1.
DR   AlphaFoldDB; P54264; -.
DR   SMR; P54264; -.
DR   STRING; 390333.Ldb1194; -.
DR   PaxDb; 390333-Ldb1194; -.
DR   KEGG; ldb:Ldb1194; -.
DR   PATRIC; fig|390333.7.peg.1064; -.
DR   eggNOG; COG2502; Bacteria.
DR   HOGENOM; CLU_071543_0_0_9; -.
DR   BioCyc; LDEL390333:LDB_RS05125-MONOMER; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000001259; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0140096; F:catalytic activity, acting on a protein; IEA:UniProtKB-ARBA.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00645; AsnA; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..338
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_0000195879"
FT   CONFLICT        17..32
FT                   /note="RETEKAIRYIRETFQT -> AKRKRQSATSGKPSS (in Ref. 1;
FT                   CAA61602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310..314
FT                   /note="GKAHI -> QGPH (in Ref. 1; CAA61602)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   338 AA;  38786 MW;  6718FB1A6A6C6123 CRC64;
     MAKLVIPSDY DPKMTIRETE KAIRYIRETF QTEFGTAMNL ERISAPMFVK KSSGLNDNLS
     GWEKPVSFTL HDGNEGELQI VHSLAKWKRW ALKHYGFSHG EGLFTNMNAI RKDEEVLDNL
     HSVYVDQWDW EKVIDKSERT EATLRQTVQR IFETIKGMEY HVRALYPQAA YHLPEEISFV
     TSEELEARWP SLTPSEREDK ICQEKGAVFL EHIGGALPLS KKPHDLRAPD YDDWTLNGDL
     LFWYEPLQRA FEVSSMSIRV DEDRLQEQLK LAGAEDRLDL PFHQALLKGD LPYSIGGGIG
     QSRLCMLLLG KAHIGEVQAS IWPDEIVEKC QAAKIQLL
//