ID   ASNH_MYCTO              Reviewed;         652 AA.
AC   P9WN32; L0TAH2; P64247; Q10374;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
GN   Name=asnB; OrderedLocusNames=MT2257;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (L-Gln route): step 1/1.
CC   -!- SIMILARITY: Belongs to the asparagine synthetase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46543.1; -; Genomic_DNA.
DR   PIR; B70785; B70785.
DR   RefSeq; WP_003411413.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WN32; -.
DR   SMR; P9WN32; -.
DR   EnsemblBacteria; AAK46543; AAK46543; MT2257.
DR   KEGG; mtc:MT2257; -.
DR   PATRIC; fig|83331.31.peg.2432; -.
DR   HOGENOM; CLU_014658_3_0_11; -.
DR   UniPathway; UPA00134; UER00195.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01991; Asn_Synthase_B_C; 1.
DR   CDD; cd00712; AsnB; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.20.10; -; 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   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..652
FT                   /note="Putative asparagine synthetase [glutamine-
FT                   hydrolyzing]"
FT                   /id="PRO_0000427197"
FT   DOMAIN          2..231
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..64
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         89..91
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         382..383
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            384
FT                   /note="Important for beta-aspartyl-AMP intermediate
FT                   formation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   652 AA;  72150 MW;  C4624495A845F790 CRC64;
     MCGLLAFVAA PAGAAGPEGA DAASAIARAS HLMRHRGPDE SGTWHAVDGA SGGVVFGFNR
     LSIIDIAHSH QPLRWGPPEA PDRYVLVFNG EIYNYLELRD ELRTQHGAVF ATDGDGEAIL
     AGYHHWGTEV LQRLRGMFAF ALWDTVTREL FCARDPFGIK PLFIATGAGG TAVASEKKCL
     LDLVELVGFD TEIDHRALQH YTVLQYVPEP ETLHRGVRRL ESGCFARIRA DQLAPVITRY
     FVPRFAASPI TNDNDQARYD EITAVLEDSV AKHMRADVTV GAFLSGGIDS TAIAALAIRH
     NPRLITFTTG FEREGFSEID VAVASAEAIG ARHIAKVVSA DEFVAALPEI VWYLDEPVAD
     PALVPLFFVA REARKHVKVV LSGEGADELF GGYTIYREPL SLRPFDYLPK PLRRSMGKVS
     KPLPEGMRGK SLLHRGSLTL EERYYGNARS FSGAQLREVL PGFRPDWTHT DVTAPVYAES
     AGWDPVARMQ HIDLFTWLRG DILVKADKIT MANSLELRVP FLDPEVFAVA SRLPAGAKIT
     RTTTKYALRR ALEPIVPAHV LHRPKLGFPV PIRHWLRAGE LLEWAYATVG SSQAGHLVDI
     AAVYRMLDEH RCGSSDHSRR LWTMLIFMLW HAIFVEHSVV PQISEPQYPV QL