ID   ASNA_SERP5              Reviewed;         330 AA.
AC   A8GLK7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   10-JUN-2026, entry version 90.
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=Spro_4905;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(2009).
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 {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; CP000826; ABV43997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GLK7; -.
DR   SMR; A8GLK7; -.
DR   STRING; 399741.Spro_4905; -.
DR   PaxDb; 399741-Spro_4905; -.
DR   KEGG; spe:Spro_4905; -.
DR   eggNOG; COG2502; Bacteria.
DR   HOGENOM; CLU_071543_0_0_6; -.
DR   OrthoDB; 3185462at2; -.
DR   UniPathway; UPA00134; UER00194.
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:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniRule.
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.
FT   CHAIN           1..330
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_1000061107"
SQ   SEQUENCE   330 AA;  36733 MW;  8CB0B9EC20D2919E CRC64;
     MKKQFIQKQQ QISLVKSFFS RQLEQQLGLI EVQAPILSRL GDGTQDNLSG SEKAVQVKVK
     TLPDATFEVV HSLAKWKRKT LGSYDFGAGE GLYTHMKALR PDEDRLSAIH SVYVDQWDWE
     RVMGDGERSQ DYLESTVRSI YAAIKATEGE VSREYGLTPF LPEQIHFVHS ETLLQRYPEL
     DAKGRERAIA KELGAVFLIG IGGKLSHGKS HDVRAPDYDD WTTPAAEGLA GLNGDILVWN
     PVLQDAFELS SMGIRVDASA LKRQLAQTGD EDRLALEWHQ SLLRGEMPQT IGGGIGQSRL
     VMLLLQLSHI GQVQCGVWSP QVREAVEGLL
//