ID   ASNA_BACMK              Reviewed;         327 AA.
AC   A9VPK1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=BcerKBAB4_1672;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY42913.1; -; Genomic_DNA.
DR   RefSeq; WP_002031125.1; NC_010184.1.
DR   AlphaFoldDB; A9VPK1; -.
DR   SMR; A9VPK1; -.
DR   STRING; 315730.BcerKBAB4_1672; -.
DR   EnsemblBacteria; ABY42913; ABY42913; BcerKBAB4_1672.
DR   KEGG; bwe:BcerKBAB4_1672; -.
DR   eggNOG; COG2502; Bacteria.
DR   HOGENOM; CLU_071543_0_0_9; -.
DR   OMA; QSRICMF; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000002154; 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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding.
FT   CHAIN           1..327
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_1000129110"
SQ   SEQUENCE   327 AA;  38084 MW;  C31776804598D180 CRC64;
     MYQSLMTVRE TQIAIKEVKT FFEDQLAKRL ELFRVSAPLF VTKKSGLNDH LNGVERPIEF
     DMLHSGEELE IVHSLAKWKR FALHEYGYEA GEGLYTNMNA IRRDEELDAT HSIYVDQWDW
     EKIVQKEWRT IDYLQKTVQT IYGIFKELEG HLFEKYPFLG KYLPEEIIFI TSQELEDKYP
     ELTPKDREHA IAKEHGAVFI IGIGDALRSG EKHDGRASDY DDWKLNGDIL FWHPVLQASF
     ELSSMGIRVD SKALDEQLTK TGEDFKREYD FHKGILEDVL PLTIGGGIGQ SRMCMYFLRK
     AHIGEVQSSV WPDDLREACK KENIHLF