ID   ASNA_MYCGA              Reviewed;         327 AA.
AC   Q7NAM0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 93.
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=MYCGA6160;
GN   ORFNames=MGA_0424;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; AE015450; AAP56966.2; -; Genomic_DNA.
DR   RefSeq; WP_011113875.1; NC_004829.2.
DR   AlphaFoldDB; Q7NAM0; -.
DR   SMR; Q7NAM0; -.
DR   KEGG; mga:MGA_0424; -.
DR   PATRIC; fig|233150.7.peg.693; -.
DR   HOGENOM; CLU_071543_0_0_14; -.
DR   OrthoDB; 487853at2; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000001418; 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; Reference proteome.
FT   CHAIN           1..327
FT                   /note="Aspartate--ammonia ligase"
FT                   /id="PRO_0000195882"
SQ   SEQUENCE   327 AA;  37760 MW;  300C80E0A974789A CRC64;
     MKKLTLLETE LAIKYIKDLF QNALSKELNL LRVSAPLIIA PDSGLNDNLN GWEAPVSFKS
     KTNGVSSQVV QSLAKWKRYS IARYEIPLYQ GLYTDMNAIR MDETLDATHS MYVDQWDWEL
     RISENDRNVE FLKNTVNKIY KVLKEAQLKV NEKYGIFEQK DLLPEHIHFV TTQELLDQYP
     DKNPSEREQL VCEKYKAVFV MQVGKKLSNN QVHDGRSPDY DDWSLNGDIM VYNPRSKKAL
     ELSSMGIRVN KEVLLKQLEE SKQNERLELM FHKKLVNGEL HQTIGGGIGQ SRLCYFLLQK
     DHIGEVQASH WSDEIVVEAK AKGIKLL