GLNA3_BUTFI
ID GLNA3_BUTFI Reviewed; 700 AA.
AC Q05650;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:8103789};
DE Short=GS {ECO:0000303|PubMed:8103789};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P15623};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase III {ECO:0000303|PubMed:8103789};
DE Short=GSIII {ECO:0000303|PubMed:8103789};
GN Name=glnA {ECO:0000303|PubMed:8103789};
OS Butyrivibrio fibrisolvens.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=831;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ACTIVITY REGULATION.
RC STRAIN=H17C;
RX PubMed=8103789; DOI=10.1099/00221287-139-7-1487;
RA Goodman H.J., Woods D.R.;
RT "Cloning and nucleotide sequence of the Butyrivibrio fibrisolvens gene
RT encoding a type III glutamine synthetase.";
RL J. Gen. Microbiol. 139:1487-1493(1993).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000250|UniProtKB:P15623}.
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:0000250|UniProtKB:P15623};
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: The activity of this enzyme is not controlled by
CC adenylation. {ECO:0000305|PubMed:8103789}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P15623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15623}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000250|UniProtKB:P15623}.
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DR EMBL; L08256; AAA71923.1; -; Unassigned_DNA.
DR PIR; I40596; I40596.
DR AlphaFoldDB; Q05650; -.
DR SMR; Q05650; -.
DR PRIDE; Q05650; -.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..700
FT /note="Glutamine synthetase"
FT /id="PRO_0000153278"
FT DOMAIN 65..155
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 159..589
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 318..319
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 319
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 435
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
SQ SEQUENCE 700 AA; 78541 MW; 32DDD0FA10B542E7 CRC64;
MIEASKLTTE FGSLVFNDKI MKERLPKDIY KAVHKTIEKE PHLEPGCSYS CSSNHEGVGN
REQCYHFTPP GSSPMTGLTA EKHDSFISPT EDGRSSWSSQ EKSWLRANLM HQASQWWSSC
HNSSMRGYQH GILHHHAFIK DGSLLLPTAF CSYGGEALDR DSLLRSMEAL SNEAVKMMRL
LGYEDVNRVN TTIGSEQEYF LIDKDFYKKR KDLLLTGRTL IGAPASKGQE MEDHYFGVIK
PKVSAYMHDL DEELWKLGIP AKTKHNEVAP SQHELAPVFE TANIAVDHNQ LTMEVMKKVA
DKHNYACLLH EKPFEGVNGS GKHNNWSICT DTGINLLDPG KNPGENIPFL VFLMSVIAAV
DEYAPILRLS VASAGNDHRL GGNEAPPAII SIFVGDELAE VLKAVEAGEA YKAAGKSQMT
WEQQYFTFTK DNTDRNRTSP FAFTGNKFES DGGHSSVANG KYGPQHMQLQ KEVATLNAKL
SAYSGDELKE KVKEVLKETL LAHKRVLFNG NGYTDEWVEE AAKRGLPNLK ALPDCMPYWI
SDESIDLFTR HGIFTKEEIY SRYEILLENY SKSIHIESLT MQEMIRKDLT EGLVAYEKDL
SKEIVQKKSL LDGDCCALEL GVLKSLDKSS AEMGKALSKL FEDTKKAEGM TEALETASYY
ESTVLADMDE LRKYADEAEA LIPEKYLSYP TYGEMLFSLR
