ASNA_BACFR
ID ASNA_BACFR Reviewed; 345 AA.
AC Q64PM4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=BF3815;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD50557.1; -; Genomic_DNA.
DR RefSeq; WP_005790904.1; NZ_UYXF01000018.1.
DR RefSeq; YP_101091.1; NC_006347.1.
DR AlphaFoldDB; Q64PM4; -.
DR SMR; Q64PM4; -.
DR STRING; 295405.BF3815; -.
DR EnsemblBacteria; BAD50557; BAD50557; BF3815.
DR GeneID; 66331553; -.
DR KEGG; bfr:BF3815; -.
DR PATRIC; fig|295405.11.peg.3663; -.
DR HOGENOM; CLU_071543_0_0_10; -.
DR OMA; QSRICMF; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000002197; 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.
FT CHAIN 1..345
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_1000017937"
SQ SEQUENCE 345 AA; 39996 MW; 1951B8063797CA3E CRC64;
MSYLIKPQNY KPLLDLKQTE LGIKQIKEFF QLNLSSELRL RRVTAPLFVL KGMGINDDLN
GIERPVSFPI KDLGDAQAEV VHSLAKWKRL TLADYHIEPG YGIYTDMNAI RSDEELGNLH
SLYVDQWDWE RVITAEDRNA DFLKEIVNRI YAAMIRTEYM VYEMYPQIKP CLPQKLHFIH
SEELRQLYPD MEPKCREHAI CKKYGAVFII GIGCKLSDGK KHDGRAPDYD DYTSKGLNDL
PGLNGDLLLW DDVLQRSIEL SSMGIRVDKE ALLRQVKQEN QEQRLELYFH KRLLNDTLPL
SIGGGIGQSR LCMFYLRKAH IGEIQASIWP EEMRRECTAL NIHLI
