ID A0A255ZEI9_9BURK Unreviewed; 471 AA.
AC A0A255ZEI9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN Name=glnA {ECO:0000313|EMBL:OYQ39953.1};
GN ORFNames=CHU94_11470 {ECO:0000313|EMBL:OYQ39953.1};
OS Rhodoferax sp. TH121.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2022803 {ECO:0000313|EMBL:OYQ39953.1, ECO:0000313|Proteomes:UP000216607};
RN [1] {ECO:0000313|EMBL:OYQ39953.1, ECO:0000313|Proteomes:UP000216607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH121 {ECO:0000313|EMBL:OYQ39953.1,
RC ECO:0000313|Proteomes:UP000216607};
RA Cai H.;
RT "Rhodoferax cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU004356};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYQ39953.1}.
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DR EMBL; NOXW01000021; OYQ39953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255ZEI9; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000216607; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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; IPR027302; Gln_synth_N_conserv_site.
DR NCBIfam; TIGR00653; GlnA; 1.
DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR43407:SF2; GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS00180; GLNA_1; 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 {ECO:0000256|PIRSR:PIRSR604809-2,
KW ECO:0000256|RuleBase:RU004356};
KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:OYQ39953.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW ECO:0000256|RuleBase:RU004356};
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000216607}.
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 107..471
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 163..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 267..268
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 274..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 324
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 330
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 342
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 362
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 400
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 471 AA; 52446 MW; 5CEC168A0C2D7574 CRC64;
MAKTVADVMK MVKENEVKFV DFRFTDTRGK QQHTTVPVSH FDEDKFTSGH AFDGSSIAGW
KGIEASDMLL MPDPNTANID PFFEETTIIM NCDVVEPSDG KAYDRDPRSI AKRAEAYLKA
SGIGDAAYFG PEPEFFIFDG IRWSTDPQNT FYEVEEYEAP WNTGAKLEGG NRGHRPTTKG
GYFPVPPVDS TQDMRAEMSL ILESLGIPVE VFHHEVAGAG QNEIGTKFST LVERADWTML
QKYVVHNVAN AYGKTATFMP KPYHGDNGSG MHVHQSVWKD GKNLFAGDGY AGLSDFALYY
IGGIIKHARA LNAITNPGTN SYKRLVPHFE APVKLAYSAK NRSASIRIPF VANPKGRRVE
ARFPDPLMNP YLGFAALLMA GLDGVENKIH PGEAATKDLY HLPPEEDAKV PTVCHSLDQA
LEHLDKDRAF LTKGGVFTDS MIDAYIDLKM QEVTRYRMSV HPVEYDMYYS L
//
