ID A0A212QQ14_9PROT Unreviewed; 469 AA.
AC A0A212QQ14;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN ORFNames=SAMN07250955_102257 {ECO:0000313|EMBL:SNB61469.1};
OS Arboricoccus pini.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Geminicoccaceae; Arboricoccus.
OX NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB61469.1, ECO:0000313|Proteomes:UP000197065};
RN [1] {ECO:0000313|EMBL:SNB61469.1, ECO:0000313|Proteomes:UP000197065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B29T1 {ECO:0000313|EMBL:SNB61469.1,
RC ECO:0000313|Proteomes:UP000197065};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000256|ARBA:ARBA00003117}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric
CC ring. {ECO:0000256|ARBA:ARBA00011258}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; FYEH01000002; SNB61469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212QQ14; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000197065; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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; IPR004809; Gln_synth_I.
DR InterPro; IPR001637; Gln_synth_I_adenylation_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; PS00182; GLNA_ADENYLATION; 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 Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000197065}.
FT DOMAIN 14..98
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 106..469
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 322
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 340
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 360
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 398
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 469 AA; 50887 MW; 13B08DE1AA28F832 CRC64;
MSHAESIIER LQAEGVRVVD FRFTDLAGHW RHTSIDAASL DARQLEQGFM IDGSSIPGWR
DPTEADVALK PDLTSARQDP FAAQPTLILL ANVVDPATGQ GYEGCSRSVA ARAEAWLAGH
AAADRMTTSV ATGYFIFDDV RIETSAARNA IEINGSESEA AGGQAYASGN PGHRPQPCAA
RYALSPADHQ SDIRAEITSI LASLGFTGIR HDHGQSPMQG RLAFKGDHLT GTADRIQLMK
YVVQHVAASY GKSASFMPRP MPESMGSGMS LQHSLWKRGK PVFAGSGYAD LSPQCLSFVA
GIMRHARALN AFTNPTTNSY RRLRKKASEP VYLAYAAYNR SAAVRIPFAA EPAAKTVDIR
FPDPAANPYL ALAAIMMAGI DGIEQKLEPG DAMDRNLYDL GPDEVDDLPT VALSLREALD
ALEHDQDFLL RGDVMSEDLI ASYVSLKRQE IERISQAVIP LEYELYYGS
//