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Database: UniProt
Entry: Q1MNZ8_LAWIP
LinkDB: Q1MNZ8_LAWIP
Original site: Q1MNZ8_LAWIP 
ID   Q1MNZ8_LAWIP            Unreviewed;       626 AA.
AC   Q1MNZ8;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=asparagine synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012737};
DE            EC=6.3.5.4 {ECO:0000256|ARBA:ARBA00012737};
GN   Name=asnB {ECO:0000313|EMBL:CAJ53906.1};
GN   OrderedLocusNames=LIB007 {ECO:0000313|EMBL:CAJ53906.1};
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OG   Plasmid pLaw2 {ECO:0000313|Proteomes:UP000002430}.
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ53906.1, ECO:0000313|Proteomes:UP000002430};
RN   [1] {ECO:0000313|EMBL:CAJ53906.1, ECO:0000313|Proteomes:UP000002430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ53906.1,
RC   ECO:0000313|Proteomes:UP000002430};
RC   PLASMID=pLaw2 {ECO:0000313|Proteomes:UP000002430};
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate +
CC         H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001778};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (L-Gln route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005187}.
CC   -!- SIMILARITY: Belongs to the asparagine synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005752}.
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DR   EMBL; AM180254; CAJ53906.1; -; Genomic_DNA.
DR   RefSeq; WP_011527302.1; NC_008013.1.
DR   AlphaFoldDB; Q1MNZ8; -.
DR   KEGG; lip:LIB007; -.
DR   eggNOG; COG0367; Bacteria.
DR   HOGENOM; CLU_014658_3_1_7; -.
DR   OMA; VFKHIQE; -.
DR   OrthoDB; 9763290at2; -.
DR   Proteomes; UP000002430; Plasmid pLaw2.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01991; Asn_Synthase_B_C; 1.
DR   CDD; cd00712; AsnB; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR006426; Asn_synth_AEB.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR033738; AsnB_N.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR01536; asn_synth_AEB; 1.
DR   PANTHER; PTHR43284:SF1; ASPARAGINE SYNTHETASE; 1.
DR   PANTHER; PTHR43284; ASPARAGINE SYNTHETASE (GLUTAMINE-HYDROLYZING); 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW   Asparagine biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR001589-
KW   2};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PIRSR:PIRSR001589-1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR001589-2}; Plasmid {ECO:0000313|EMBL:CAJ53906.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002430}.
FT   DOMAIN          2..213
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001589-1"
FT   BINDING         100
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
SQ   SEQUENCE   626 AA;  73156 MW;  F8B10BD276E44814 CRC64;
     MCGVCGIICL DGDKPSKEVL SHMLDAIRHR GPDKANVVVD GCIALGHCRL AILDLTDAAA
     QPMSTSDKLF TIVYNGEIYN FEEIRRELIK LGHTFISRSD TEVILHAYIQ WGAQCVTKFN
     GMFVFVIYDV IRKQIFIARD RYGIKPLYYT IIQNNFLFSS EAKAFLRYPQ FCTKLDYEAL
     LEYFTFQNIL TDKTLLHNVY IFPPGHYAIL PLNTGQLTFS QYWDYCFDES KNIHSDKEYE
     EELTYLIQQA VQRQLQSDVE LGTYLSGGMD SGSITALASK RFPYIKSFTC GFDLHSISGL
     ELAFDERNAA EAMSYLFKTE HYEMVLKSGD MERVFPRLAW HIEEPRTGQS YPNFCIAHLV
     SKFVKVVLAG TGSDELFGGY PWRYYRALGE KGENSFEKYI DRYYLFWQRL IPNRYLLSMF
     KPIETHVRHV RTRDIFRNIF GDNNSPVTSH EESINRSLYF EAKTFLHGLL VVEDKLSMAH
     SLETRLPFLD NDLVDFAMRL PVRCKIHRLN ETLRINENES AKASRYYKKT NDGKWLLRRA
     MERYVPTHII EAVKQGFSAP DASWFRGESI DFVHRYLFSQ NVRLYEYFDR KVVHELVTEH
     LEGNANRRLF IWSLLSFEEW LHQYLP
//
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