ID F6EEL1_HOYSD Unreviewed; 478 AA.
AC F6EEL1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN OrderedLocusNames=AS9A_1256 {ECO:0000313|EMBL:AEF39708.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39708.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF39708.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
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|ARBA:ARBA00000777,
CC ECO:0000256|RuleBase:RU004356};
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 hexagons.
CC {ECO:0000256|ARBA:ARBA00011354, ECO:0000256|RuleBase:RU000387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU000387}.
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; CP002786; AEF39708.1; -; Genomic_DNA.
DR RefSeq; WP_013806057.1; NC_015564.1.
DR AlphaFoldDB; F6EEL1; -.
DR STRING; 443218.AS9A_1256; -.
DR KEGG; asd:AS9A_1256; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_2_11; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000009235; 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: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; IPR001637; Gln_synth_I_adenylation_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR NCBIfam; TIGR00653; GlnA; 1.
DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR43407:SF1; LENGSIN; 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; PS00182; GLNA_ADENYLATION; 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}; Cytoplasm {ECO:0000256|RuleBase:RU000387};
KW Ligase {ECO:0000256|RuleBase:RU004356};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW ECO:0000256|RuleBase:RU004356};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|PIRSR:PIRSR604809-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT DOMAIN 16..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 108..478
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 230..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 271..272
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 329
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 335
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 347
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 368
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 406
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 478 AA; 53367 MW; 686F86FA3A352C6E CRC64;
MAFSNAEEVF KFIADENVEY VDVRFCDLPG VQQHFSIPAS AFNQDVIDDG LAFDGSSVRG
FQSIHESDML LLPDVTTAGI DPFRAAKTLN VVFSVHDPFT REAYSRDPRN VARKAEAYLA
STGIADTAFF GAEAEFYLFD SVRFDSQANG TFYEIDSESG WWNTGVDREA DGSPNRGYKV
RYKGGYFPVA PYDHYVDLRD DITTNLTNAG FEIERGHHEV GTAGQAEINY KFNTLTHAAD
DLLLFKYIVK NTAWQGGKSA TFMPKPLFGD NGSGMHMHQS LWKDGKPLFH DEAGYAGLSD
MARHYIGGIL HHAPSLLAFT NPTINSYHRL VPGYEAPINL VYSQRNRSAA VRIPITGNNP
KAKRLEFRAP DSSGNPYLAF AACMMAGLDG IRNKIEPPAP VDKDLYELPP EEAKGIPQAP
TSLEAVIDNL ERDNDFLTEG GVFTNDLIET WIALKREQEI EPVRLRPHPY EFNLYYDV
//
