ID ASNA_LIMRD Reviewed; 336 AA.
AC A5VMP8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 87.
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=Lreu_1885;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ84122.1; -; Genomic_DNA.
DR RefSeq; WP_003669400.1; NZ_AZDD01000009.1.
DR AlphaFoldDB; A5VMP8; -.
DR SMR; A5VMP8; -.
DR STRING; 557436.Lreu_1885; -.
DR KEGG; lre:Lreu_1885; -.
DR PATRIC; fig|557436.17.peg.1961; -.
DR eggNOG; COG2502; Bacteria.
DR HOGENOM; CLU_071543_0_0_9; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000001991; 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:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00645; AsnA; 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..336
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_1000061106"
SQ SEQUENCE 336 AA; 39389 MW; A861C4CA19CF5042 CRC64;
MDLTIPKDYD PRLSIRETEA AIRYIRETFQ DEFGKELNLQ RMSAPMFVEK STGLNDNLNG
VEQPVSFEMK DMPNETVEIV HSLAKWKRLA LKRYGFGMHE GLYTNMNAIR KEEDLDNFHS
IYVDQWDWEK IISKDERTEE TLKDTVRDIF KVIKHMEHEV WYKFPQAVYH LPDEIHFVTT
QELEDRWPDL TPLEREDKIA KELGAVFVMK IGDKLQRSGK PHDGRAPDYD DWSLNGDIIF
WYEPLQRRIE VSSMGIRVSP ESMKYQLEQA DATDREKLPF HKMLLNGELP YTIGGGIGQS
RLCMLLLGKA HIGEVQASIW PEDMIKKCEE NHIQIL
//
