ASNA_ACTSZ
ID ASNA_ACTSZ Reviewed; 330 AA.
AC A6VLN1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Asuc_0503;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(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}.
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DR EMBL; CP000746; ABR73878.1; -; Genomic_DNA.
DR RefSeq; WP_012072258.1; NC_009655.1.
DR AlphaFoldDB; A6VLN1; -.
DR SMR; A6VLN1; -.
DR STRING; 339671.Asuc_0503; -.
DR EnsemblBacteria; ABR73878; ABR73878; Asuc_0503.
DR KEGG; asu:Asuc_0503; -.
DR eggNOG; COG2502; Bacteria.
DR HOGENOM; CLU_071543_0_0_6; -.
DR OMA; QSRICMF; -.
DR OrthoDB; 487853at2; -.
DR UniPathway; UPA00134; UER00194.
DR Proteomes; UP000001114; 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 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..330
FT /note="Aspartate--ammonia ligase"
FT /id="PRO_1000072559"
SQ SEQUENCE 330 AA; 37540 MW; 2C1A482D2B9E58BE CRC64;
MKKSFILQQQ EISFAKNTFT TKLAEHLGLV EVQGPILSQV GNGIQDNLSG KEKPVQVNVK
MIEDATFEVV HSLAKWKRHT LARFGFAEGE GLFVHMKALR PDEDSLDQTH SVYVDQWDWE
KVIPAGRRNL NYLKETVRSI YAAIVETQEA VEQKFGLKAF LPKEITFIHS EDLARDYPHM
TDKERENEIC KKYGAVFLIG IGGDLPDGKP HDMRAPDYDD WTTSSEGEYK GLNGDILVWN
PVLNRAFELS SMGIRVDETA LRRQLALTHD EERLNFAWHQ DLINGRMPLS IGGGIGQSRL
AMLLLQKHHI GEVQSSVWPK TVMEQFENIL
