ID   ASNA_BACFN              Reviewed;         345 AA.
AC   Q5L9E0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=BF3607;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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; CR626927; CAH09288.1; -; Genomic_DNA.
DR   RefSeq; WP_005790904.1; NZ_UFTH01000001.1.
DR   AlphaFoldDB; Q5L9E0; -.
DR   SMR; Q5L9E0; -.
DR   PaxDb; 272559-BF9343_3507; -.
DR   GeneID; 66331553; -.
DR   KEGG; bfs:BF9343_3507; -.
DR   eggNOG; COG2502; Bacteria.
DR   HOGENOM; CLU_071543_0_0_10; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000006731; 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: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..345
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_1000017936"
SQ   SEQUENCE   345 AA;  39996 MW;  1951B8063797CA3E CRC64;
     MSYLIKPQNY KPLLDLKQTE LGIKQIKEFF QLNLSSELRL RRVTAPLFVL KGMGINDDLN
     GIERPVSFPI KDLGDAQAEV VHSLAKWKRL TLADYHIEPG YGIYTDMNAI RSDEELGNLH
     SLYVDQWDWE RVITAEDRNA DFLKEIVNRI YAAMIRTEYM VYEMYPQIKP CLPQKLHFIH
     SEELRQLYPD MEPKCREHAI CKKYGAVFII GIGCKLSDGK KHDGRAPDYD DYTSKGLNDL
     PGLNGDLLLW DDVLQRSIEL SSMGIRVDKE ALLRQVKQEN QEQRLELYFH KRLLNDTLPL
     SIGGGIGQSR LCMFYLRKAH IGEIQASIWP EEMRRECTAL NIHLI
//