(data stored in ACNUC1104 zone)

SWISSPROT: D3VG40_XENNA

ID   D3VG40_XENNA            Unreviewed;       330 AA.
AC   D3VG40;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 55.
DE   RecName: Full=Aspartate--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00964848};
DE            EC=6.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00964843};
DE   AltName: Full=Asparagine synthetase A {ECO:0000256|HAMAP-Rule:MF_00555};
GN   Name=asnA {ECO:0000256|HAMAP-Rule:MF_00555,
GN   ECO:0000313|EMBL:CBJ88130.1};
GN   OrderedLocusNames=XNC1_0037 {ECO:0000313|EMBL:CBJ88130.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88130.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88130.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) +
CC         L-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;
CC         EC=6.3.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00555,
CC         ECO:0000256|SAAS:SAAS01124561};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (ammonia route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00964853}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00555,
CC       ECO:0000256|SAAS:SAAS00964846}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. AsnA subfamily. {ECO:0000256|HAMAP-Rule:MF_00555,
CC       ECO:0000256|SAAS:SAAS00964852}.
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DR   EMBL; FN667742; CBJ88130.1; -; Genomic_DNA.
DR   RefSeq; WP_010846121.1; NC_014228.1.
DR   STRING; 406817.XNC1_0037; -.
DR   EnsemblBacteria; CBJ88130; CBJ88130; XNC1_0037.
DR   KEGG; xne:XNC1_0037; -.
DR   eggNOG; ENOG4105CU9; Bacteria.
DR   eggNOG; COG2502; LUCA.
DR   HOGENOM; HOG000284502; -.
DR   KO; K01914; -.
DR   OMA; QSRICMF; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000008075; 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   HAMAP; MF_00555; AsnA; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004618; AsnA.
DR   PANTHER; PTHR30073; PTHR30073; 1.
DR   Pfam; PF03590; AsnA; 1.
DR   PIRSF; PIRSF001555; Asp_ammon_ligase; 1.
DR   TIGRFAMs; TIGR00669; asnA; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VG40.
DR   SWISS-2DPAGE; D3VG40.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00555,
KW   ECO:0000256|SAAS:SAAS00964850};
KW   Asparagine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00555,
KW   ECO:0000256|SAAS:SAAS00964847};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00555,
KW   ECO:0000256|SAAS:SAAS00964849};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00555,
KW   ECO:0000256|SAAS:SAAS00964845};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00555,
KW   ECO:0000256|SAAS:SAAS00964851, ECO:0000313|EMBL:CBJ88130.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00555,
KW   ECO:0000256|SAAS:SAAS00964844};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN       13    320       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   330 AA;  37291 MW;  F44139FB06E592AA CRC64;
     MKTSFIEKQQ QISFVKSYFS RLLEKQLGLI EVQGPILSRL GDGTQDNLSG HEKAVQVKVK
     TLPDATFEVV HSLAKWKRKT LGRFGFQAEQ GLYTHMKALR PDEDRLTPIH SVFVDQWDWE
     KTMGEGQRSL DYLKQTVGKI YEAIKETQQA VSKEFGLAPF LPDQIHFIHS EELLKRYPDL
     DAKGREREAA KEFGAIFLMG IGGKLSDDQS HDVRAPDYDD WTSPNSDGFF GLNGDIIVWN
     PVLQDAFEIS SMGIRVDAEA LQRQLELTGD EDRLQYDWHQ ALVKGDMPQS IGGGIGQSRL
     VMLMLQMPHI GQVQCGVWSP EIIESVEGVL
//

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