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Database: UniProt
Entry: A0A086XRD4_9RHOB
LinkDB: A0A086XRD4_9RHOB
Original site: A0A086XRD4_9RHOB 
ID   A0A086XRD4_9RHOB        Unreviewed;       469 AA.
AC   A0A086XRD4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN   Name=glnA {ECO:0000313|EMBL:KFI24584.1};
GN   ORFNames=CG50_09655 {ECO:0000313|EMBL:KFI24584.1};
OS   Paenirhodobacter enshiensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paenirhodobacter.
OX   NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI24584.1, ECO:0000313|Proteomes:UP000028824};
RN   [1] {ECO:0000313|EMBL:KFI24584.1, ECO:0000313|Proteomes:UP000028824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW2-9 {ECO:0000313|EMBL:KFI24584.1,
RC   ECO:0000313|Proteomes:UP000028824};
RA   Wang D., Wang G.;
RT   "Genome of Paenirhodobacter enshiensis DW2-9.";
RL   Submitted (MAR-2014) 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   -!- 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   -!- 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}.
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:KFI24584.1}.
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DR   EMBL; JFZB01000042; KFI24584.1; -; Genomic_DNA.
DR   RefSeq; WP_036639680.1; NZ_JFZB01000042.1.
DR   AlphaFoldDB; A0A086XRD4; -.
DR   STRING; 1105367.CG50_09655; -.
DR   eggNOG; COG0174; Bacteria.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000028824; 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   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; 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:KFI24584.1};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
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:UP000028824}.
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         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         265..266
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         322
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         328
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         353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
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;  52322 MW;  41CD87D475FC340D CRC64;
     MSAVKKALEL MKAEDVEYVD VRFTDPRGKL QHVTLVVDLI DEDFFEEGFM FDGSSIAGWK
     SIDQSDMKLI PDATSVYIDP FYAEKTMCVH CNVVEPDTNE PYTRDPRSTA EKAEAYLKSS
     GIGDSFFCGP EAEFFIFDDV RYSVTPHKVS YQVDAEAAAW NTDAEIEGGN LAHRANFKGG
     YFPVNPVDEA ADLRGEMLST MKRIGMKVDK HHHEVATCQH ELGMIFGTLT EQADNIQKYK
     YVIHNVAAAY GKTVTFMPKP IKGDNGSGMH VNMSIWKDGK PLFAGDKYAD LSQEALYFIG
     GILKHAKALN ALTNPTTNSY KRLIPGFEAP VLRAYSARNR SGCVRIPWTE SPKAKRVEAR
     FPDPAANPYL AFSALLMAGL DGIKNKIDPG APSDKDLYDL PPEELAEIPT VCGSLREALT
     ELEADMDFLL AGDVFTKDQI EGYIALKWEE VYAFEHTPHP VEYQMYYSC
//
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