ASNA_CROS8
ID ASNA_CROS8 Reviewed; 330 AA.
AC A7MMW6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-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}; OrderedLocusNames=ESA_04018;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU79204.1; -; Genomic_DNA.
DR RefSeq; WP_012126198.1; NC_009778.1.
DR AlphaFoldDB; A7MMW6; -.
DR SMR; A7MMW6; -.
DR EnsemblBacteria; ABU79204; ABU79204; ESA_04018.
DR KEGG; esa:ESA_04018; -.
DR PATRIC; fig|290339.8.peg.3566; -.
DR HOGENOM; CLU_071543_0_0_6; -.
DR OMA; QSRICMF; -.
DR OrthoDB; 487853at2; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000000260; 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.
FT CHAIN 1..330
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_1000017944"
SQ SEQUENCE 330 AA; 36770 MW; 25A0D6308ADE4A1D CRC64;
MKTAYITRQR QISFVKAHFS RLLEEKLGLL EVQAPILSRV GDGTQDNLSG CEKAVQVNVK
TLPQAQFEVV HSLAKWKRKT LGQHDFSAGE GLYTHMKALR PDEDRLSPVH SVYVDQWDWE
RVMGDGERHL GTLKQTVESI WSAIKETELA AAERSGLTPF LPDAIHFVHS ETLQRRFPEL
DAKGRERAIA KELGAVFLIG IGGKLADGKR HDVRAPDYDD WTTPTESGFA GLNGDILVWN
PLLEDAFEIS SMGIRVDADT LKRQLALTGD QDRLALEWHQ ALLNGEMPQT IGGGIGQSRL
TMLLLQLPHI GQVQCGVWPE QVQSTVAELL
