ID A0A3S5EGV7_9ACTO Unreviewed; 443 AA.
AC A0A3S5EGV7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Probable glutamine synthetase 2 {ECO:0000313|EMBL:VEG25817.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:VEG25817.1};
GN Name=glnA {ECO:0000313|EMBL:VEG25817.1};
GN ORFNames=NCTC11636_00227 {ECO:0000313|EMBL:VEG25817.1};
OS Actinomyces howellii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=52771 {ECO:0000313|EMBL:VEG25817.1, ECO:0000313|Proteomes:UP000266895};
RN [1] {ECO:0000313|EMBL:VEG25817.1, ECO:0000313|Proteomes:UP000266895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11636 {ECO:0000313|EMBL:VEG25817.1,
RC ECO:0000313|Proteomes:UP000266895};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; LR134350; VEG25817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S5EGV7; -.
DR KEGG; ahw:NCTC11636_00227; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000266895; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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; IPR027303; Gln_synth_gly_rich_site.
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; 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 Ligase {ECO:0000313|EMBL:VEG25817.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000266895}.
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 107..443
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 443 AA; 49224 MW; EB71C3DBF7B2BEB6 CRC64;
MDKQQEYVFR AIEERDIRFI RLWFSDVLGQ LKSVAIAPAE VEGAFEEGIG FDGSAIEGLT
RVFEADMLLS PDPSTFQMLP WRNGTNGVAR MFCDVLTPDG EPARTDPRAV LERQLARVAD
AGFTCYVHPE IEFYLVKRDE AGRIQPTDYA GYFDHVPGGT AHEFRRRACL MLEQMGISVE
FSHHEGGPGQ NEIDLRFADA LSMADNIMTF RAVVEEVALQ EGCLATFMPK PFVDQPGSGM
HTHFSLFEGD RNAFYDPSGQ YQLSSTGRSF IAGLLRHANE ISAVTNQHVN SYKRLWGGGE
APSYVCWGHN NRSALVRVPM HKPGKGQSVR VEYRSLDPAA NPYLAYAVIL AAGLKGIEEG
YELPPEAEDD VWALTEGERQ ALGIGALPTS LKSAVAAMSG SDLVADTLGE AAFEFFMRNK
RREFMAYDAQ VTDYEINQFF PRS
//
