ID A0A2S0WKL8_9ACTN Unreviewed; 445 AA.
AC A0A2S0WKL8; A0A5F2ESY0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Type I glutamate--ammonia ligase {ECO:0000313|EMBL:AWB91883.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:TGN32731.1};
GN Name=glnA {ECO:0000313|EMBL:AWB91883.1};
GN ORFNames=C3E78_06530 {ECO:0000313|EMBL:AWB91883.1}, E4L97_08500
GN {ECO:0000313|EMBL:TGN32731.1};
OS Aeromicrobium chenweiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2079793 {ECO:0000313|EMBL:AWB91883.1, ECO:0000313|Proteomes:UP000244384};
RN [1] {ECO:0000313|EMBL:AWB91883.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=592 {ECO:0000313|EMBL:AWB91883.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000244384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=592 {ECO:0000313|Proteomes:UP000244384};
RA Li J.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TGN32731.1, ECO:0000313|Proteomes:UP000297606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S592 {ECO:0000313|EMBL:TGN32731.1,
RC ECO:0000313|Proteomes:UP000297606};
RA Li J., Ha Z., Lu H., Jin N.;
RL Submitted (MAR-2019) 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; CP026952; AWB91883.1; -; Genomic_DNA.
DR EMBL; SRPI01000003; TGN32731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0WKL8; -.
DR KEGG; aez:C3E78_06530; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000244384; Chromosome.
DR Proteomes; UP000297606; Unassembled WGS sequence.
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:AWB91883.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2}.
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 107..445
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 245..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 296
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 302
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 314
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 336
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
SQ SEQUENCE 445 AA; 49801 MW; 6C47225BB4CE0386 CRC64;
MGKQEDFVLR ALEERDVRFV RLWFTDVLGS LKSVAIAPAE LEGAFAEGIG FDGSAIEGFA
RVHEADMLAM PDPSTFQILP WRGETPATAR MFCDILMPDG TPSYADPRHV LKRALQKAAE
AGFTFYTHPE IEFFLFKGKP DVGDRPVPVD DSGYFDHTAQ GGGQDFRREV ITMLENMGIS
VEFSHHEGGP GQQEIDLRYA DALSTADNIM TFRTVVREVA LSQGKWASFM PKPFTEHPGS
GMHTHVSLFE GDENAFYEAG AEYQLSQTGR AFIAGVLHHT PEITAVTNQW VNSYKRLAGG
GEAPNYVCWG HNNRSALIRV PMYKPHKGNS ARVENRAIDS ACNPYLAFAL ILAAGLKGIE
EKYELPPEAE DDVWSLSENE RRAMGIAPLP RNLDEAIRTM ETSELVAETL GEHVFDFFLR
NKRAEWQDYR SQVTQFEIDR LMPMV
//
