ID   ASNA_HAEDU              Reviewed;         330 AA.
AC   Q7VKJ0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=HD_1913;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP96637.1; -; Genomic_DNA.
DR   RefSeq; WP_010945665.1; NC_002940.2.
DR   AlphaFoldDB; Q7VKJ0; -.
DR   SMR; Q7VKJ0; -.
DR   STRING; 233412.HD_1913; -.
DR   EnsemblBacteria; AAP96637; AAP96637; HD_1913.
DR   KEGG; hdu:HD_1913; -.
DR   eggNOG; COG2502; Bacteria.
DR   HOGENOM; CLU_071543_0_0_6; -.
DR   OMA; QSRICMF; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000001022; 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   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; Reference proteome.
FT   CHAIN           1..330
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_0000195877"
SQ   SEQUENCE   330 AA;  37325 MW;  92AB16CE1AA98EE1 CRC64;
     MKKSFILQQQ EISFVKNTFT QYLIDQLDII EVQGPILSQV GNGMQDNLSG IEKAVQVNVK
     CIPGAVFEVV HSLAKWKRHT LARFGFKQGE GLFVHMKALR PDEDSLDPTH SIYVDQWDWE
     KVIPEGQRNF AYLKQTVNQI YKAIRLTELA VEARFDIPSS LPKQITFIHS EELAQRYPNM
     SSKERENAIC KEHGAIFLIG IGGKLSDGKA HDGRAPDYDD WTTESENGYK GLNGDILVWN
     EELGSAFELS SMGIRVDQQA LRLQVSLTGD EDRLTMDWHQ DLLAGRLPLS IGGGIGQSRL
     VMFLLHKKHI GEVQSSVWPT EMLTQFENIL