ID A0A5C4U6C0_9CORY Unreviewed; 478 AA.
AC A0A5C4U6C0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN Name=glnA {ECO:0000313|EMBL:TNL99442.1};
GN ORFNames=FHE74_03580 {ECO:0000313|EMBL:TNL99442.1};
OS Corynebacterium tapiri.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1448266 {ECO:0000313|EMBL:TNL99442.1, ECO:0000313|Proteomes:UP000312032};
RN [1] {ECO:0000313|EMBL:TNL99442.1, ECO:0000313|Proteomes:UP000312032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28165 {ECO:0000313|EMBL:TNL99442.1,
RC ECO:0000313|Proteomes:UP000312032};
RA Li J.;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000777,
CC ECO:0000256|RuleBase:RU004356};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000256|ARBA:ARBA00011354}.
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:TNL99442.1}.
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DR EMBL; VDHJ01000003; TNL99442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C4U6C0; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000312032; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
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 InterPro; IPR027302; Gln_synth_N_conserv_site.
DR NCBIfam; TIGR00653; GlnA; 1.
DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR43407:SF1; LENGSIN; 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; PS00180; GLNA_1; 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 ECO:0000256|RuleBase:RU004356};
KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:TNL99442.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW ECO:0000256|RuleBase:RU004356};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|PIRSR:PIRSR604809-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000312032}.
FT DOMAIN 16..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 108..478
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 230..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 271..272
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 329
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 335
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 347
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 368
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 406
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 478 AA; 53545 MW; D0B63DA232B47B5E CRC64;
MAFETNQDVV KFIKDEGIEF LDIRFTDVPG MEHHFTLPAS EFTEESAEEG LAFDGSSIRG
FTTIDESDMT LLPDPASAYV DPFREVKTLN MQFFVNDPFT YEPFSRDPRN VAKKAEEYLA
SSGIADSASF GMEAEFYLFD KVSYAAETNE SFYHVDSNEG WWNRGNETNL DGTPNTGFKT
RVKGGYFPNT PVDKTQEVRD AIVKRLQGAG FDVERFHHEV GTGGQNEINY RFDTLLRAAD
DLQTFKYIVK NTAAEYGKAA TFMPKPLAGD NGSGMHAHQS LWKDGKPLFY DESGYGGLSD
TARYYIGGLL HHAPAVLAFT NPTLNSYHRL VPGFEAPINL VYSQRNRSAA IRIPITGNNP
KAKRLEFRAP DPSGNPYLGL AAMLMAGIDG IKNRIEPHAP VDKDLYELPP EEAASIPQAP
TSLEAAIEAL RDDHEFLLEG DVFTEDLIET YINYKVDNEI MPTRLRPTPL EFEMYFDC
//
