ASNA_STRZP
ID ASNA_STRZP Reviewed; 330 AA.
AC C1CMR7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=SPP_1991;
OS Streptococcus pneumoniae (strain P1031).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1031;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000920; ACO21459.1; -; Genomic_DNA.
DR RefSeq; WP_000747993.1; NC_012467.1.
DR AlphaFoldDB; C1CMR7; -.
DR SMR; C1CMR7; -.
DR GeneID; 66807034; -.
DR KEGG; spp:SPP_1991; -.
DR HOGENOM; CLU_071543_0_0_9; -.
DR OMA; QSRICMF; -.
DR UniPathway; UPA00134; UER00194.
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 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_1000146702"
SQ SEQUENCE 330 AA; 37618 MW; 7C01444227B198A8 CRC64;
MKKSFIHQQE EISFVKNTFT QYLKDKLEVV EVQGPILSKV GDGMQDNLSG VENPVSVKVL
QIPDATYEVV HSLAKWKRHT LARFGFGEGE GLFVHMKALR PDEDSLDATH SVYVDQWDWE
KVIPNGKRNI VYLKETVEKI YKAIRLTELA VEARYDIESI LPKQITFIHT EELVERYPDL
TPKERENAIC KEFGAVFLIG IGGELPDGKP HDGRAPDYDD WTSESENGYK GLNGDILVWN
ESLGGAFELS SMGIRVDEET LRRQVEITGD EDRLELEWHK SLLNGLFPLT IGGGIGQSRM
AMFLLRKRHI GEVQTSVWPQ EVRDTYENIL