ID ASNA_MALP2 Reviewed; 326 AA.
AC Q8EWQ5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 107.
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=MYPE1480;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC43939.1; -; Genomic_DNA.
DR RefSeq; WP_011076975.1; NC_004432.1.
DR AlphaFoldDB; Q8EWQ5; -.
DR SMR; Q8EWQ5; -.
DR STRING; 272633.gene:10731247; -.
DR KEGG; mpe:MYPE1480; -.
DR eggNOG; COG2502; Bacteria.
DR HOGENOM; CLU_071543_0_0_14; -.
DR InParanoid; Q8EWQ5; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000002522; 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 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..326
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_0000195883"
SQ SEQUENCE 326 AA; 37679 MW; 701C768BB4194B0A CRC64;
MYNLSILETQ KAIKFIKDLF QVNLAHALKL HRVTAPLVLE RNKGINDDLN GSENPVTFTS
DGNGISGEIP QSLAKWKRMM LGKYEIPLHE GIYADMNAIR KDESLSSIHS IYVDQWDWEL
HIKKTERNLE TLKVVVKKIY EIIRLCQKEV NKKYEWFAEN LLPEEITFIS SEDLLQRYPN
KTPKERERLI ASKYKAVFII GIGDNLSDGK PHDLRAPDYD DWKLNGDIIV WNETTKSALE
LSSMGIRVDE VSLVEQLDKS NNNSRKELDF HKKLINKEFP YSIGGGIGQS RLCYFLLHKQ
HIGEVQSSLW PKDILEEAEK NNIKLL
//
