ID ASNA_CLOTE Reviewed; 341 AA.
AC Q897F7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=CTC_00781;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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; AE015927; AAO35379.1; -; Genomic_DNA.
DR RefSeq; WP_011099045.1; NC_004557.1.
DR AlphaFoldDB; Q897F7; -.
DR SMR; Q897F7; -.
DR STRING; 212717.CTC_00781; -.
DR GeneID; 24253458; -.
DR KEGG; ctc:CTC_00781; -.
DR HOGENOM; CLU_071543_0_0_9; -.
DR OrthoDB; 9766088at2; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000001412; 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:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00645; AsnA; 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 NCBIfam; TIGR00669; asnA; 1.
DR PANTHER; PTHR30073; ASPARTATE--AMMONIA LIGASE; 1.
DR PANTHER; PTHR30073:SF5; ASPARTATE--AMMONIA LIGASE; 1.
DR Pfam; PF03590; AsnA; 1.
DR PIRSF; PIRSF001555; Asp_ammon_ligase; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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..341
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_0000195872"
SQ SEQUENCE 341 AA; 40005 MW; 709CB138963B7438 CRC64;
MEIKCSERLI IPKEYKTELD LKETAIAIKE VKDCFERALA KQLNLIRVSA PLFVRCDKGL
NDNLNGVERP VKFTVKDDNE AAVEIVHSLA KWKRMALYRY NFNADEGLYT DMNAIRRDEE
LDNTHSIYVD QWDWERIIKK EDRNEEYLKD IVRKIFKAFK ETEEHINKLY PFLGEVLPEE
VFFMTTQELE DMFPDLTAKE REDAITKEKK AVFLMKIGKT LESGEKHDGR APDYDDWELN
GDILFWNPVL NKAFELSSMG IRVDEESLLK QLKLANCEER KELQFHKMLL EKKLPYTIGG
GIGQSRMCML FLKKAHIGEV QSSIWPEEMI KFCEEKGMTI L
//
