ID A0A1L9NYG8_9RHOB Unreviewed; 444 AA.
AC A0A1L9NYG8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamine synthetase 3 {ECO:0000313|EMBL:OJI94307.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:OJI94307.1};
GN Name=glnT {ECO:0000313|EMBL:OJI94307.1};
GN ORFNames=PFRI_14380 {ECO:0000313|EMBL:OJI94307.1};
OS Planktotalea frisia.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Planktotalea.
OX NCBI_TaxID=696762 {ECO:0000313|EMBL:OJI94307.1, ECO:0000313|Proteomes:UP000184514};
RN [1] {ECO:0000313|EMBL:OJI94307.1, ECO:0000313|Proteomes:UP000184514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH6-1 {ECO:0000313|EMBL:OJI94307.1,
RC ECO:0000313|Proteomes:UP000184514};
RA Poehlein A., Bakenhus I., Voget S., Brinkhoff T., Simon M.;
RT "Genome sequence of Planktotalea frisia SH6-1.";
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, 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:OJI94307.1}.
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DR EMBL; MLCB01000106; OJI94307.1; -; Genomic_DNA.
DR RefSeq; WP_072630062.1; NZ_QKZM01000022.1.
DR AlphaFoldDB; A0A1L9NYG8; -.
DR STRING; 696762.PFRI_14380; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000184514; Unassembled WGS sequence.
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; IPR017536; Glutamine_synthetase_typeIII.
DR NCBIfam; TIGR03105; gln_synth_III; 1.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 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; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:OJI94307.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000184514}.
FT DOMAIN 12..94
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 100..444
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 444 AA; 49433 MW; 902E9EFD141218DE CRC64;
MTVDLAKFAQ ENGVKYFMIS FTDLFGGQRA KLVPARAIAD MQEDGAGFAG FATWLDLTPA
HPDMLAVPDP DAVIILPWNK EIAWVPADCV MEGEPVEQAP RNVLRKLIAE AAEEGMHVKT
GIEAEFFLLT PEGDQISDSF DTAAKPCYDQ QAFMRRLDVI REISDYMLEM EWGAYQNDHE
DANGQWEMNW DFDDALKTAD KHSFFKFMTK CVAEKHGYRA TFMPKPIEGL TGNGCHAHVS
VWDAPGKASK TNVFAMEAND SSQTAELGLS EKGRHFLGGI MKHASALAAI TNPTVNSYKR
INAPRTMSGA TWAPNTVTWT GNNRTHMVRV PGPGRFELRL PDGAVNPYLL QAVIIAAGLS
GVRSKADPGK RHDIDMYAEG HKITDAPKLP LNMLDAMREY DKDEGLKAAM GEEFSRSYLK
MKMQEWDSFV SYFSGWEKDN TLDI
//
