ID A0A132MXM7_9ACTN Unreviewed; 457 AA.
AC A0A132MXM7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:KWX02122.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:KWX02122.1};
GN ORFNames=LI90_3163 {ECO:0000313|EMBL:KWX02122.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWX02122.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, 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:KWX02122.1}.
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DR EMBL; LAXD01000001; KWX02122.1; -; Genomic_DNA.
DR RefSeq; WP_066888984.1; NZ_LAXD01000001.1.
DR AlphaFoldDB; A0A132MXM7; -.
DR STRING; 1469144.LI90_3163; -.
DR PATRIC; fig|1469144.10.peg.3407; -.
DR OrthoDB; 3277468at2; -.
DR Proteomes; UP000070188; 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; 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: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; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KWX02122.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188}.
FT DOMAIN 121..457
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 457 AA; 49049 MW; C33CAD16F137CE70 CRC64;
MTLPDPLAVQ RALRLTDRLS AAGIRGIALT WVDNAGVTRV KTIPIDRLEY TVTWGIDMSP
VFDVFLIDDS VTTSRHIAGP DGDLRMFPDL DRLTELAAQP GWAWAPVDRY TQEREPYAAC
QRGFARRMVK RAAERGLTLK VGFETEWFCG EDTAGGEPVP ACTGPAYGMT RVLELSDYLD
ELYEAFADQG VEVLQIHPEY APGQLAISTG YDDPVTAADT VVLVRQTIRA VAGHFGLRVS
FAPVVVPGQA GNGGHLHLSL WRNGENLCGG GDGPYGMRGE GEAFLAGVLD ALPALCAVGA
PGVASYLRLI PSHWAGAFQC WGRENREAAL RFVTSATSSV GTASAEIKCF DASANPYLVV
GAVIAAGLAG LDAGLRLPPE LTGDPALLSE PDLLARGIRR LPASLPEALE HLERCAFLRD
AMGDPLFQAF TAVRRGEIAL FDGAAPDEIT AATRWRY
//
