GLNA3_BACFR
ID GLNA3_BACFR Reviewed; 729 AA.
AC P15623; Q64XI6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2576872};
DE Short=GS {ECO:0000303|PubMed:2576872};
DE EC=6.3.1.2 {ECO:0000305|Ref.3};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase III {ECO:0000303|PubMed:2576872};
DE Short=GSIII {ECO:0000305};
GN Name=glnA {ECO:0000303|PubMed:2576872}; OrderedLocusNames=BF1040;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BF1;
RX PubMed=2576872; DOI=10.1099/00221287-136-4-787;
RA Hill R.T., Parker J.R., Goodman H.J.K., Jones D.T., Woods D.R.;
RT "Molecular analysis of a novel glutamine synthetase of the anaerobe
RT Bacteroides fragilis.";
RL J. Gen. Microbiol. 135:3271-3279(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=BF1;
RA Southern J.A., Parker J.R., Woods D.R.;
RT "Novel structure, properties and inactivation of glutamine synthetase
RT cloned from Bacteroides fragilis.";
RL J. Gen. Microbiol. 133:2437-2446(1987).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000305|Ref.3}.
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|Ref.3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P12425};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
CC -!- ACTIVITY REGULATION: Inhibited by L-histidine (46%), L-arginine (38%)
CC and L-methionine-DL-sulphoximine. The activity of this enzyme is not
CC controlled by adenylation. {ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; M28252; AAA62314.1; -; Genomic_DNA.
DR EMBL; AP006841; BAD47790.1; -; Genomic_DNA.
DR PIR; A37191; A37191.
DR RefSeq; WP_005785391.1; NC_006347.1.
DR RefSeq; YP_098324.1; NC_006347.1.
DR AlphaFoldDB; P15623; -.
DR SMR; P15623; -.
DR DIP; DIP-59116N; -.
DR STRING; 295405.BF1040; -.
DR PRIDE; P15623; -.
DR EnsemblBacteria; BAD47790; BAD47790; BF1040.
DR KEGG; bfr:BF1040; -.
DR PATRIC; fig|295405.11.peg.1032; -.
DR HOGENOM; CLU_024307_0_0_10; -.
DR OMA; QFLVFCA; -.
DR BRENDA; 6.3.1.2; 755.
DR Proteomes; UP000002197; 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:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR InterPro; IPR040577; Gln-synt_C.
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; IPR022147; GSIII_N.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF18318; Gln-synt_C-ter; 1.
DR Pfam; PF12437; GSIII_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF55931; SSF55931; 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.
FT CHAIN 1..729
FT /note="Glutamine synthetase"
FT /id="PRO_0000153277"
FT DOMAIN 85..174
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 179..615
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 337..338
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 338
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 458
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT CONFLICT 152
FT /note="V -> G (in Ref. 1; AAA62314)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="P -> L (in Ref. 1; AAA62314)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="T -> M (in Ref. 1; AAA62314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 82825 MW; 1916071619EB9562 CRC64;
MSKMRFFALQ ELSNRKPLEI TTPSNKLSDY YASHVFDRKK MQEYLPKEAY KAVVDATEKG
TPISREMADL IANGMKSWAK SLNVTHYTHW FQPLTDGTAE KHDGFIEFGE DGEVIERFSG
KLLIQQEPDA SSFPNGGIRN TFEARGYTAW DVSSPAFVVD TTLCIPTIFI SYTGEALDYK
TPLLKALAAV DKAATEVCQL FDKNITRVFT NLGWEQEYFL VDTSLYNARP DLRLTGRTLM
GHSSAKDQQL EDHYFGSIPP RVTAFMKELE IECHKLGIPV KTRHNEVAPN QFELAPIFEN
CNLANDHNQL VMDLMKRIAR KHHFAVLFHE KPYNGVNGSG KHNNWSLCTD TGINLFAPGK
NPKGNMLFLT FLVNVLMMVH KNQDLLRASI MSAGNSHRLG ANEAPPAILS IFLGSQLSAT
LDEIVRQVTN SKMTPEEKTT LKLGIGRIPE ILLDTTDRNR TSPFAFTGNR FEFRAAGSSA
NCAAAMIAIN AAMANQLNEF KASVDKLMEE GIGKDEAIFR ILKENIIASE PIRFEGDGYS
EEWKQEAARR GLTNICHVPE ALMHYTDNQS RAVLIGERIF NETELACRLE VELEKYTMKV
QIESRVLGDL AINHIVPIAV SYQNRLLENL CRMKEIFSEE EYEVMSADRK ELIKEISHRV
SAIKVLVRDM TEARKVANHK ENFKEKAFAY EETVRPYLES IRDHIDHLEM EIDDEIWPLP
KYRELLFTK
