ID A0A0F6TCN7_9CORY Unreviewed; 442 AA.
AC A0A0F6TCN7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamine synthetase, type I {ECO:0000313|EMBL:AKE40979.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:AKE40979.1};
GN Name=glnA {ECO:0000313|EMBL:AKE40979.1};
GN ORFNames=UL82_03870 {ECO:0000313|EMBL:AKE40979.1};
OS Corynebacterium kutscheri.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=35755 {ECO:0000313|EMBL:AKE40979.1, ECO:0000313|Proteomes:UP000033457};
RN [1] {ECO:0000313|EMBL:AKE40979.1, ECO:0000313|Proteomes:UP000033457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20755 {ECO:0000313|EMBL:AKE40979.1,
RC ECO:0000313|Proteomes:UP000033457};
RX PubMed=26021937;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium kutscheri DSM 20755, a
RT Corynebacterial Type Strain with Remarkably Low G+C Content of Chromosomal
RT DNA.";
RL Genome Announc. 3:e00571-15(2015).
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; CP011312; AKE40979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F6TCN7; -.
DR STRING; 35755.UL82_03870; -.
DR KEGG; cku:UL82_03870; -.
DR HOGENOM; CLU_017290_1_3_11; -.
DR Proteomes; UP000033457; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 InterPro; IPR004809; Gln_synth_I.
DR NCBIfam; TIGR00653; GlnA; 1.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF11; 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; 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 Ligase {ECO:0000313|EMBL:AKE40979.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000033457}.
FT DOMAIN 11..98
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 105..442
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 243..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 294
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 300
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 312
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 334
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
SQ SEQUENCE 442 AA; 49532 MW; 12B5C47C69D6643A CRC64;
MEYVLRTVEE QDVRFVRLWF TDILGYLKSV SVAPAELESA FEEGISFDGS SIEGYSRISE
SDTIALPDPS TFQLLPFEAP ESPLKSARMI CDISNPDGNP SYSDPRQVLR RQIQLAADEG
FQCMVAPEIE FYLVETLKTQ GTPPVPTDNG GYFDQASYNQ APLFRRQAMI ALEDMGIPVE
FSHHEASPGQ QEIDLRHADA LTMADSIMTF RYVAKQVALA NGIGATFMPK PFVDYSGSAM
HTHISLFEGD TNAFHDPDGE FNLSLTAKQF IAGILCHARE FSAITNQWTN SYKRLLFGNE
APTAATWGAS NRSALVRVPT YRMGKAESRR VEVRSPDSAC NPYLALAVLL AAGLKGISEG
YELMSPAEDD IAALSRRERL AMGYTDLPTS LDQALREMEK SEFVAEVLGE QAFEYFLRNK
WREWHDYQSQ ITPWELKNNL EY
//
