ID A0A0I9YPY8_9MYCO Unreviewed; 446 AA.
AC A0A0I9YPY8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:KLO36373.1};
GN ORFNames=ABH38_12475 {ECO:0000313|EMBL:KLO36373.1};
OS Mycobacterium haemophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO36373.1, ECO:0000313|Proteomes:UP000036334};
RN [1] {ECO:0000313|EMBL:KLO36373.1, ECO:0000313|Proteomes:UP000036334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium haemophilum.";
RL Submitted (MAY-2015) 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}.
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:KLO36373.1}.
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DR EMBL; LDPR01000009; KLO36373.1; -; Genomic_DNA.
DR RefSeq; WP_047314676.1; NZ_LDPT01000008.1.
DR AlphaFoldDB; A0A0I9YPY8; -.
DR STRING; 1202450.B586_10060; -.
DR PATRIC; fig|29311.18.peg.4081; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000036334; 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 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:UP000036334}.
FT DOMAIN 15..102
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 109..446
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 247..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 298
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 304
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 316
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 338
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
SQ SEQUENCE 446 AA; 49551 MW; 776CA35DCC9E832D CRC64;
MDRQKEFVLR TLEERDIRFV RLWFTDVLGY LKSVAIAPAE LEGAFEEGIG FDGSSIEGFA
RVSESDTVAH PDPSTFQVLP WATPAGHHHS ARMFCDITMP DGSPSWADPR HVLRRQLTKA
NDLGFSCYVH PEIEFFLLKA GSEEGATPIP VDNAGYFDQA VHDSASDFRR QAIEALEFMG
ISVEFSHHEG APGQQEIDLR FADALSMADN VMTFRYVIKE VAIENGARAS FMPKPFAQHP
GSAMHTHMSL FEGDVNAFHS PDDVLQLSEV GKSFIAGILE HASEISAVTN QWVNSYKRLV
HGGEAPTAAS WGAANRSALV RVPMYSPHKA SSRRVEVRSP DSACNPYLAF AVLLAAGLRG
VEKGYVLGPQ AEDNVWDLTP EERRTMGYRE LPTSLDSALR AMEASELVAE ALGEHVFDFF
LRNKRAEWAN YRSHVTPYEL KTYLSL
//
