ID   ASNA_HAEIN              Reviewed;         330 AA.
AC   P44338;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=HI_0564;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22222.1; -; Genomic_DNA.
DR   PIR; H64077; H64077.
DR   RefSeq; NP_438721.1; NC_000907.1.
DR   RefSeq; WP_005654693.1; NC_000907.1.
DR   AlphaFoldDB; P44338; -.
DR   SMR; P44338; -.
DR   STRING; 71421.HI_0564; -.
DR   EnsemblBacteria; AAC22222; AAC22222; HI_0564.
DR   KEGG; hin:HI_0564; -.
DR   PATRIC; fig|71421.8.peg.584; -.
DR   eggNOG; COG2502; Bacteria.
DR   HOGENOM; CLU_071543_0_0_6; -.
DR   OMA; QSRICMF; -.
DR   PhylomeDB; P44338; -.
DR   BioCyc; HINF71421:G1GJ1-576-MON; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004071; F:aspartate-ammonia ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IBA:GO_Central.
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_0000195878"
SQ   SEQUENCE   330 AA;  37432 MW;  3C8D32400A77FF41 CRC64;
     MKKTFILQQQ EISFVKNTFT QNLIEQLGII EVQGPILSQV GNGMQDNLSG IEKAVQVNVK
     CIPNAVFEVV HSLAKWKRHT LARFNFKEDE GLFVHMKALR PDEDSLDPTH SVYVDQWDWE
     KVIPEGRRNF AYLKETVNSI YRAIRLTELA VEARFDIPSI LPKQITFVHS EDLVKRYPDL
     SSKERENAIC KEYGAVFLIG IGGKLSDGKP HDGRAPDYDD WTTESENGYK GLNGDILVWN
     DQLGKAFELS SMGIRVDESA LRLQVGLTGD EDHLKMDWHQ DLLNGKLPLT IGGGIGQSRL
     AMLLLRKKHI GEVQSSVWPK EMLEEFSNIL