GLN1B_PSETA
ID GLN1B_PSETA Reviewed; 468 AA.
AC Q3V5W6;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:15388964};
DE Short=GS {ECO:0000303|PubMed:15388964};
DE EC=6.3.1.2 {ECO:0000269|PubMed:15388964, ECO:0000269|PubMed:16495669};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000305};
DE Short=GSI beta {ECO:0000305};
GN Name=glnA {ECO:0000303|PubMed:15388964};
OS Pseudomonas taetrolens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=47884;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, AMPYLATION AT TYR-397, AND SUBUNIT.
RC STRAIN=Y-30;
RX PubMed=16495669; DOI=10.1271/bbb.70.500;
RA Yamamoto S., Wakayama M., Tachiki T.;
RT "Cloning and expression of Pseudomonas taetrolens Y-30 gene encoding
RT glutamine synthetase: an enzyme available for theanine production by
RT coupled fermentation with energy transfer.";
RL Biosci. Biotechnol. Biochem. 70:500-507(2006).
RN [2]
RP PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=Y-30;
RX PubMed=15388964; DOI=10.1271/bbb.68.1888;
RA Yamamoto S., Uchimura K., Wakayama M., Tachiki T.;
RT "Purification and characterization of glutamine synthetase of Pseudomonas
RT taetrolens Y-30: an enzyme usable for production of theanine by coupling
RT with the alcoholic fermentation system of baker's yeast.";
RL Biosci. Biotechnol. Biochem. 68:1888-1897(2004).
CC -!- FUNCTION: Catalyzes the formation of glutamine from glutamate and
CC ammonia (PubMed:16495669, PubMed:15388964). In vitro, can also use
CC hydroxylamine, methylamine and ethylamine, with 32%, 7% and 1% activity
CC compared to ammonia, respectively (PubMed:15388964).
CC {ECO:0000269|PubMed:15388964, ECO:0000269|PubMed:16495669}.
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:0000269|PubMed:15388964, ECO:0000269|PubMed:16495669};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15388964, ECO:0000269|PubMed:16495669};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15388964, ECO:0000269|PubMed:16495669};
CC Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit, however the activity
CC with Mg(2+) is about 10-fold higher than with Mn(2+).
CC {ECO:0000269|PubMed:15388964};
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-397. Conversely, when
CC nitrogen levels are low, the N-terminal adenylyl removase (AR) of GlnE
CC activates GlnA by removing the adenylyl group by phosphorolysis. The
CC fully adenylated enzyme complex is inactive (Probable).
CC {ECO:0000269|PubMed:16495669}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 (in the presence 30 mM Mg(2+)) and 7.5 (in the
CC presence of 3 mM Mn(2+)). {ECO:0000269|PubMed:15388964};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000269|PubMed:15388964, ECO:0000305|PubMed:16495669}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AB233456; BAE44186.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3V5W6; -.
DR SMR; Q3V5W6; -.
DR STRING; 47884.SAMN04490203_4421; -.
DR PRIDE; Q3V5W6; -.
DR SABIO-RK; Q3V5W6; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:UniProtKB.
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; Direct protein sequencing; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15388964"
FT CHAIN 2..468
FT /note="Glutamine synthetase"
FT /id="PRO_0000431888"
FT DOMAIN 11..96
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 104..468
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 264..265
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 265
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 321
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 327
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 339
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 359
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT MOD_RES 397
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0A9C5,
FT ECO:0000305|PubMed:16495669"
SQ SEQUENCE 468 AA; 51766 MW; 8576AA78C93B3C66 CRC64;
MSKSVQLIKD HDVKWIDLRF TDTKGTQHHV TMPARDALED DFFEVGKMFD GSSIAGWKGI
EASDMILLPD DDTAVLDPFT EDATLILVCD IIEPSTMQGY DRDPRAIAHR AEEYLKTTGI
GDTVFAGPEP EFFIFDEVKF KSDISGSMFK IYSEQGSWMS DQDIEGGNKG HRPGVKGGYF
PVPPFDHDHE IRTAMCNALE EMGQTVEVHH HEVATAGQNE IGVKFNTLVK KADEVQTLKY
VVHNVADAYG RTATFMPKPL YGDNGSGMHV HMSIAKDGKN TFAGEGYAGL SETALYFIGG
IIKHGKALNG FTNPATNSYK RLVPGFEAPV MLAYSARNRS ASIRIPYVNS PRGRRIEARF
PDPAANPYLA FAALLMAGLD GIQNKIHPGD AADKNLYDLP PEEAKEIPQV CGSLKEALEE
LDKGRAFLTK GGVFSDDFID AYIALKSEEE IKVRTFVHPL EYELYYSC
