ASNH_MYCTU
ID ASNH_MYCTU Reviewed; 652 AA.
AC P9WN33; 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 41.
DE RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing];
DE EC=6.3.5.4;
GN Name=asnB; OrderedLocusNames=Rv2201; ORFNames=MTCY190.12;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44978.1; -; Genomic_DNA.
DR PIR; B70785; B70785.
DR RefSeq; NP_216717.1; NC_000962.3.
DR RefSeq; WP_003411413.1; NZ_NVQJ01000008.1.
DR AlphaFoldDB; P9WN33; -.
DR SMR; P9WN33; -.
DR STRING; 83332.Rv2201; -.
DR PaxDb; P9WN33; -.
DR DNASU; 888472; -.
DR GeneID; 888472; -.
DR KEGG; mtu:Rv2201; -.
DR TubercuList; Rv2201; -.
DR eggNOG; COG0367; Bacteria.
DR OMA; IEHSHQP; -.
DR PhylomeDB; P9WN33; -.
DR UniPathway; UPA00134; UER00195.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; 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_0000056935"
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
