ASNH_MYCBO
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 03-AUG-2022, entry version 97.
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; Actinobacteria; Corynebacteriales; 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}.
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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 EnsemblBacteria; SIU00832; SIU00832; BQ2027_MB2224.
DR PATRIC; fig|233413.5.peg.2440; -.
DR OMA; IEHSHQP; -.
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; 3.40.50.620; -; 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 1: Evidence at protein level;
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_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
