ASNA_LACDA
ID ASNA_LACDA Reviewed; 338 AA.
AC P54264; Q1G9Z6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=Ldb1194;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8636057; DOI=10.1128/jb.178.8.2459-2461.1996;
RA Kim S.I., Germond J.-E., Pridmore D., Soell D.;
RT "Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA
RT synthetase: coregulation by transcription antitermination?";
RL J. Bacteriol. 178:2459-2461(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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.
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; X89438; CAA61602.1; -; Genomic_DNA.
DR EMBL; CR954253; CAI97996.1; -; Genomic_DNA.
DR PIR; S71073; S71073.
DR RefSeq; WP_011543942.1; NZ_JQAV01000007.1.
DR AlphaFoldDB; P54264; -.
DR SMR; P54264; -.
DR STRING; 390333.Ldb1194; -.
DR EnsemblBacteria; CAI97996; CAI97996; Ldb1194.
DR KEGG; ldb:Ldb1194; -.
DR PATRIC; fig|390333.7.peg.1064; -.
DR eggNOG; COG2502; Bacteria.
DR HOGENOM; CLU_071543_0_0_9; -.
DR OMA; QSRICMF; -.
DR BioCyc; LDEL390333:LDB_RS05125-MON; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000001259; 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 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; Reference proteome.
FT CHAIN 1..338
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_0000195879"
FT CONFLICT 17..32
FT /note="RETEKAIRYIRETFQT -> AKRKRQSATSGKPSS (in Ref. 1;
FT CAA61602)"
FT /evidence="ECO:0000305"
FT CONFLICT 310..314
FT /note="GKAHI -> QGPH (in Ref. 1; CAA61602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38786 MW; 6718FB1A6A6C6123 CRC64;
MAKLVIPSDY DPKMTIRETE KAIRYIRETF QTEFGTAMNL ERISAPMFVK KSSGLNDNLS
GWEKPVSFTL HDGNEGELQI VHSLAKWKRW ALKHYGFSHG EGLFTNMNAI RKDEEVLDNL
HSVYVDQWDW EKVIDKSERT EATLRQTVQR IFETIKGMEY HVRALYPQAA YHLPEEISFV
TSEELEARWP SLTPSEREDK ICQEKGAVFL EHIGGALPLS KKPHDLRAPD YDDWTLNGDL
LFWYEPLQRA FEVSSMSIRV DEDRLQEQLK LAGAEDRLDL PFHQALLKGD LPYSIGGGIG
QSRLCMLLLG KAHIGEVQAS IWPDEIVEKC QAAKIQLL
