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Database: UniProt
Entry: A0A212QQ14_9PROT
LinkDB: A0A212QQ14_9PROT
Original site: A0A212QQ14_9PROT 
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
//
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