(data stored in SCRATCH zone)

SWISSPROT: D3UY11_XENBS

ID   D3UY11_XENBS            Unreviewed;       330 AA.
AC   D3UY11;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 57.
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:CBJ79189.1};
GN   OrderedLocusNames=XBJ1_0034 {ECO:0000313|EMBL:CBJ79189.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79189.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79189.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79189.1,
RC   ECO:0000313|Proteomes:UP000002045};
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; FN667741; CBJ79189.1; -; Genomic_DNA.
DR   RefSeq; WP_012986662.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0034; -.
DR   EnsemblBacteria; CBJ79189; CBJ79189; XBJ1_0034.
DR   GeneID; 8829661; -.
DR   KEGG; xbo:XBJ1_0034; -.
DR   PATRIC; fig|406818.4.peg.30; -.
DR   eggNOG; ENOG4105CU9; Bacteria.
DR   eggNOG; COG2502; LUCA.
DR   HOGENOM; HOG000284502; -.
DR   KO; K01914; -.
DR   OMA; QSRICMF; -.
DR   BioCyc; XBOV406818:XBJ1_RS00150-MONOMER; -.
DR   UniPathway; UPA00134; UER00194.
DR   Proteomes; UP000002045; 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; D3UY11.
DR   SWISS-2DPAGE; D3UY11.
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:UP000002045};
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:CBJ79189.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00555,
KW   ECO:0000256|SAAS:SAAS00964844};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       13    320       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   330 AA;  37178 MW;  BA0DF0B6234DA734 CRC64;
     MKTSFIEKQQ QISFVKSYFS RLLEKQLGLI EVQGPILSRL GDGTQDNLSG HEKAVQVKVK
     TLPDATFEVV HSLAKWKRKT LGRFGFQAEQ GLYTHMKALR PDEDRLTPIH SVFVDQWDWE
     KVMGEGHRSL GYLKQTVGKI YEAIKETQKA VSKEFGLAPF LPDQIHFLHS EELLKRYPDL
     DAKSREREAA KEFGAIFLMG IGGKLSDGQA HDVRAPDYDD WTTPNSDGLF GLNGDIIVWN
     PVLQDAFEIS SMGIRVDAEA LQRQLELTCD EDRLQYDWHQ ALVKGDMPQS IGGGIGQSRL
     VMLLLQMAHI GQVQCGVWSP EIIESVEGVL
//

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