ID   ASNH_MYCBO              Reviewed;         652 AA.
AC   P64248; A0A1R3Y0J6; Q10374; X2BKF1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
GN   Name=asnB; OrderedLocusNames=BQ2027_MB2224;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=BCG / Pasteur;
RX   PubMed=16006064; DOI=10.1016/j.femsle.2005.06.004;
RA   Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y.;
RT   "Thiol specific oxidative stress response in Mycobacteria.";
RL   FEMS Microbiol. Lett. 249:87-94(2005).
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   -!- INDUCTION: Induced in response to the thiol oxidant diamide.
CC       {ECO:0000269|PubMed:16006064}.
CC   -!- SIMILARITY: Belongs to the asparagine synthetase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT708304; SIU00832.1; -; Genomic_DNA.
DR   RefSeq; NP_855873.1; NC_002945.3.
DR   RefSeq; WP_003411413.1; NC_002945.4.
DR   AlphaFoldDB; P64248; -.
DR   SMR; P64248; -.
DR   PATRIC; fig|233413.5.peg.2440; -.
DR   UniPathway; UPA00134; UER00195.
DR   Proteomes; UP000001419; 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; 3.60.20.10; 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; PF13537; GATase_7; 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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome.
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_0000056936"
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
//