ASNA_STRS7
ID ASNA_STRS7 Reviewed; 330 AA.
AC C0MD73;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=SZO_14180;
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204884; CAX00020.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MD73; -.
DR SMR; C0MD73; -.
DR EnsemblBacteria; CAX00020; CAX00020; SZO_14180.
DR KEGG; seq:SZO_14180; -.
DR eggNOG; COG2502; Bacteria.
DR HOGENOM; CLU_071543_0_0_9; -.
DR OMA; QSRICMF; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000001368; 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..330
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_1000212015"
SQ SEQUENCE 330 AA; 37459 MW; E3C7C9A005A0BBB9 CRC64;
MKKSFIHQQE EISFVKNTFT QYLIAKLDVV EVQGPILSRV GDGMQDNLSG VENPVSVHVL
NIPNATFEVV HSLAKWKRHT LARFGFNEGE GLVVNMKALR PDEDSLDQTH SVYVDQWDWE
KVIPDGQRNL AYLKETVETI YKVIRLTELA VEARYDIEAV LPKKITFIHT EELVARYPDL
TPKERENAIT KEFGAVFLIG IGGVLPDGKP HDGRAPDYDD WTSESENGYH GLNGDILVWN
EQLGTAFELS SMGIRVDEEA LKRQVDITGD QERLQFDWHK SLLNGLFPLT IGGGIGQSRM
AMFLLRKKHI GEVQTSVWPQ EVRDTYDNIL