(data stored in ACNUC9543 zone)

SWISSPROT: ASNA_YERPA

ID   ASNA_YERPA              Reviewed;         330 AA.
AC   Q1CC50;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, 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};
GN   OrderedLocusNames=YPA_0003;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) +
CC         L-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;
CC         EC=6.3.1.1; 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
CC       family. AsnA subfamily. {ECO:0000255|HAMAP-Rule:MF_00555}.
DR   EMBL; CP000308; ABG11972.1; -; Genomic_DNA.
DR   RefSeq; WP_002212256.1; NZ_CP009906.1.
DR   SMR; Q1CC50; -.
DR   EnsemblBacteria; ABG11972; ABG11972; YPA_0003.
DR   KEGG; ypa:YPA_0003; -.
DR   HOGENOM; HOG000284502; -.
DR   KO; K01914; -.
DR   OMA; QSRICMF; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000001971; 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   HAMAP; MF_00555; AsnA; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004618; AsnA.
DR   PANTHER; PTHR30073; PTHR30073; 1.
DR   Pfam; PF03590; AsnA; 1.
DR   PIRSF; PIRSF001555; Asp_ammon_ligase; 1.
DR   TIGRFAMs; TIGR00669; asnA; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q1CC50.
DR   SWISS-2DPAGE; Q1CC50.
KW   Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    330       Aspartate--ammonia ligase.
FT                                /FTId=PRO_1000017975.
SQ   SEQUENCE   330 AA;  36828 MW;  7B11F8E203509300 CRC64;
     MKKQFIQKQQ QISFVKSFFS RQLEQQLGLI EVQAPILSRV GDGTQDNLSG SEKAVQVKVK
     SLPDSTFEVV HSLAKWKRKT LGRFDFGADQ GVYTHMKALR PDEDRLSAIH SVYVDQWDWE
     RVMGDGERNL AYLKSTVNKI YAAIKETEAA ISAEFGVKPF LPDHIQFIHS ESLRARFPDL
     DAKGRERAIA KELGAVFLIG IGGKLADGQS HDVRAPDYDD WTSPSAEGFS GLNGDIIVWN
     PILEDAFEIS SMGIRVDAEA LKRQLALTGD EDRLELEWHQ SLLRGEMPQT IGGGIGQSRL
     VMLLLQKQHI GQVQCGVWGP EISEKVDGLL
//

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