ID A0A3N6F5K6_9ACTN Unreviewed; 454 AA.
AC A0A3N6F5K6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative glutamine synthetase 2 {ECO:0000313|EMBL:RPK68194.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:RPK68194.1};
GN Name=glnA1 {ECO:0000313|EMBL:RPK68194.1};
GN ORFNames=EES43_01960 {ECO:0000313|EMBL:RPK68194.1};
OS Streptomyces sp. ADI96-02.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522760 {ECO:0000313|EMBL:RPK68194.1, ECO:0000313|Proteomes:UP000273170};
RN [1] {ECO:0000313|EMBL:RPK68194.1, ECO:0000313|Proteomes:UP000273170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI96-02 {ECO:0000313|EMBL:RPK68194.1,
RC ECO:0000313|Proteomes:UP000273170};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RPK68194.1}.
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DR EMBL; RPGW01000008; RPK68194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6F5K6; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000273170; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF16; GLUTAMINE SYNTHETASE GLNA4 (GLUTAMINE SYNTHASE) (GS-II)-RELATED; 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; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:RPK68194.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000273170}.
FT DOMAIN 20..116
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 123..454
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 454 AA; 49945 MW; 794550E6EE849A00 CRC64;
MADRTPPLSV DDLRSRVVDG SIDTVVLAFP DMQGRLQGKR FAAGFFLDEV LEHGTEGCNY
LLAVDTEMST VEGYAMSSWE NGYGDFGMVP DAATLRPVPW HEGTALLIAD LAWHDGSPVV
AAPRQILRRQ LDRLAALGHR AQVGTELEFI VFRDSYEEAW DRDYRGLTPA NQYNIDYSIL
GTGRIEPLLR RIRNEMQAAG LTVESAKGEC NPGQHEIVFR YDEALTTCDQ HAVYKTGAKE
IASQEGVSLT FMAKYDEREG NSCHIHLSLT DEDGANMMAG DGPDGMSELM RHFLAGQLAA
LRDFSLLYAP NINSYKRFQP GSFAPTAVAW GVDNRTCALR VVGHGPSMRF ENRLPGGDVN
PHLAVAGLVA AGLYGVEHRL PLPPACTGNA YTAGYEQVPT TLREAAELWA ASPIAKEAFG
EEVVAHYLNM ARVELAAYDS AVTDWELRRS FERL
//
