ID   ASNA_CLOPS              Reviewed;         336 AA.
AC   Q0SRK2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Aspartate--ammonia ligase;
DE            EC=6.3.1.1;
DE   AltName: Full=Asparagine synthetase A;
GN   Name=asnA; OrderedLocusNames=CPR_1945;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + NH(3) = AMP + diphosphate
CC       + L-asparagine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (ammonia route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. AsnA subfamily.
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DR   EMBL; CP000312; ABG87095.1; -; Genomic_DNA.
DR   RefSeq; YP_699255.1; -.
DR   GeneID; 4205151; -.
DR   GenomeReviews; CP000312_GR; CPR_1945.
DR   KEGG; cpr:CPR_1945; -.
DR   TIGR; CPR_1945; -.
DR   HOGENOM; Q0SRK2; -.
DR   OMA; Q0SRK2; LNDNLNG.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0004071; F:aspartate-ammonia ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   HAMAP; MF_00555; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004618; AsnA.
DR   Pfam; PF03590; AsnA; 1.
DR   PIRSF; PIRSF001555; Asp_ammon_ligase; 1.
DR   ProDom; PD024629; AsnA; 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;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    336       Aspartate--ammonia ligase.
FT                                /FTId=PRO_1000017940.
SQ   SEQUENCE   336 AA;  39068 MW;  CA67B4E4D9F7D0BE CRC64;
     MEKLFIPKDY KPLLSLRETE VAIKELKDFF EDSLAKNLNL TRVSAPLFVN KGSGLNDDLN
     GIERPVSFDM KAIPEFNIQI VHSLAKWKRL ALHRYEFKHG EGLYTDMNAI RRDEDLDNIH
     SIYVDQWDWE KIIDKEERNL ETLKETVRSI YSTFKATEDF IVSKYPHIEK ILPEDITFIT
     SQELEDRYPD LTSKERETAI CKEFGAVFII GIGGKLASGE KHDDRSPDYD DWTLNGDLLF
     YYPLFDEAVE LSSMGIRVDE ESLLKQLKIA ECEERKELPF HQMLLEGKLP YTIGGGIGQS
     RICMFFLRKA HIGEVQASMW DEDMIRTCEE NNIHLL
//