GLN1B_MYCBO
ID GLN1B_MYCBO Reviewed; 478 AA.
AC P0A591; A0A1R3Y0L0; Q10377; X2BKH2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:24112767};
DE Short=GS {ECO:0000303|PubMed:24112767};
DE EC=6.3.1.2 {ECO:0000305|PubMed:24112767};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P9WN39};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P9WN39};
DE Short=GSI beta {ECO:0000250|UniProtKB:P9WN39};
GN Name=glnA1 {ECO:0000303|PubMed:24112767}; Synonyms=glnA;
GN OrderedLocusNames=BQ2027_MB2244;
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 [GENOMIC DNA].
RC STRAIN=BCG;
RA Suh C.-I., Sung H.-C.;
RT "Glutamine synthetase structural gene (glnA) Mycobacterium bovis BCG.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 27294 / H37Rv;
RX PubMed=15037612; DOI=10.1074/jbc.m401652200;
RA Mehta R., Pearson J.T., Mahajan S., Nath A., Hickey M.J., Sherman D.R.,
RA Atkins W.M.;
RT "Adenylylation and catalytic properties of Mycobacterium tuberculosis
RT glutamine synthetase expressed in Escherichia coli versus mycobacteria.";
RL J. Biol. Chem. 279:22477-22482(2004).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24112767; DOI=10.1186/1471-2180-13-226;
RA Tripathi D., Chandra H., Bhatnagar R.;
RT "Poly-L-glutamate/glutamine synthesis in the cell wall of Mycobacterium
RT bovis is regulated in response to nitrogen availability.";
RL BMC Microbiol. 13:226-226(2013).
CC -!- FUNCTION: Involved in nitrogen metabolism via ammonium assimilation
CC (PubMed:24112767). Catalyzes the ATP-dependent biosynthesis of
CC glutamine from glutamate and ammonia (PubMed:24112767). Also plays a
CC key role in controlling the ammonia levels within infected host cells
CC and so contributes to the pathogens capacity to inhibit phagosome
CC acidification and phagosome-lysosome fusion (By similarity). Involved
CC in cell wall biosynthesis via the production of the major component
CC poly-L-glutamine (PLG) (PubMed:24112767). PLG synthesis in the cell
CC wall occurs only in nitrogen limiting conditions and on the contrary
CC high nitrogen conditions inhibit PLG synthesis (PubMed:24112767).
CC {ECO:0000250|UniProtKB:P9WN39, ECO:0000269|PubMed:24112767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC Evidence={ECO:0000305|PubMed:24112767};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WN39};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39};
CC -!- ACTIVITY REGULATION: When cellular nitrogen levels are high, the C-
CC terminal adenylyl transferase (AT) of GlnE inhibits GlnA by covalent
CC transfer of an adenylyl group from ATP to Tyr-406 (PubMed:15037612).
CC Conversely, when nitrogen levels are low, the N-terminal adenylyl
CC removase (AR) of GlnE activates GlnA by removing the adenylyl group by
CC phosphorolysis (PubMed:15037612). The fully adenylated enzyme complex
CC is inactive (Probable). {ECO:0000269|PubMed:15037612}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000250|UniProtKB:P9WN39}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AF458290; AAL58468.1; -; Genomic_DNA.
DR EMBL; LT708304; SIU00852.1; -; Genomic_DNA.
DR RefSeq; NP_855893.1; NC_002945.3.
DR RefSeq; WP_003411475.1; NC_002945.4.
DR AlphaFoldDB; P0A591; -.
DR SMR; P0A591; -.
DR EnsemblBacteria; SIU00852; SIU00852; BQ2027_MB2244.
DR GeneID; 45426197; -.
DR PATRIC; fig|233413.5.peg.2460; -.
DR OMA; PHPHEFE; -.
DR BRENDA; 6.3.1.2; 3494.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR004809; Gln_synth_I.
DR InterPro; IPR001637; Gln_synth_I_adenylation_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR00653; GlnA; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Virulence.
FT CHAIN 1..478
FT /note="Glutamine synthetase"
FT /id="PRO_0000153244"
FT DOMAIN 16..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 108..478
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 230..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 271..272
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 272
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 329
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 335
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 347
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 368
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT MOD_RES 406
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
SQ SEQUENCE 478 AA; 53570 MW; 576E30073484136D CRC64;
MTEKTPDDVF KLAKDEKVEY VDVRFCDLPG IMQHFTIPAS AFDKSVFDDG LAFDGSSIRG
FQSIHESDML LLPDPETARI DPFRAAKTLN INFFVHDPFT LEPYSRDPRN IARKAENYLI
STGIADTAYF GAEAEFYIFD SVSFDSRANG SFYEVDAISG WWNTGAATEA DGSPNRGYKV
RHKGGYFPVA PNDQYVDLRD KMLTNLINSG FILEKGHHEV GSGGQAEINY QFNSLLHAAD
DMQLYKYIIK NTAWQNGKTV TFMPKPLFGD NGSGMHCHQS LWKDGAPLMY DETGYAGLSD
TARHYIGGLL HHAPSLLAFT NPTVNSYKRL VPGYEAPINL VYSQRNRSAC VRIPITGSNP
KAKRLEFRSP DSSGNPYLAF SAMLMAGLDG IKNKIEPQAP VDKDLYELPP EEAASIPQTP
TQLSDVIDRL EADHEYLTEG GVFTNDLIET WISFKRENEI EPVNIRPHPY EFALYYDV
