ID A0A2S5T2Y5_9BURK Unreviewed; 472 AA.
AC A0A2S5T2Y5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN Name=glnA {ECO:0000313|EMBL:PPE69258.1};
GN ORFNames=C1702_13380 {ECO:0000313|EMBL:PPE69258.1};
OS Caldimonas thermodepolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=215580 {ECO:0000313|EMBL:PPE69258.1, ECO:0000313|Proteomes:UP000239406};
RN [1] {ECO:0000313|EMBL:PPE69258.1, ECO:0000313|Proteomes:UP000239406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15344 {ECO:0000313|EMBL:PPE69258.1,
RC ECO:0000313|Proteomes:UP000239406};
RA Tang B.;
RT "Reclassifiation of [Polyangium] brachysporum DSM 7029 as Guopingzhaonella
RT breviflexa gen. nov., sp. nov., a member of the family Comamonadaceae.";
RL Submitted (FEB-2018) 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|RuleBase:RU004356};
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:PPE69258.1}.
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DR EMBL; PSNY01000014; PPE69258.1; -; Genomic_DNA.
DR Proteomes; UP000239406; Unassembled WGS sequence.
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:SF2; 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; 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|RuleBase:RU004356};
KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:PPE69258.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004356};
KW Reference proteome {ECO:0000313|Proteomes:UP000239406}.
SQ SEQUENCE 472 AA; 52567 MW; 9B6042C712E57B8B CRC64;
MANKTVADVM KMVKDHEVKF VDFRFTDTRG KEQHVTVPIS AFDEDKFTSG HAFDGSSIAG
WKGIEASDML LMPDPNTANI DPFFEEPTLF LTCDVIEPGD GKPYDRDPRS LAKRAEAYLK
SSGIGDAAYF GPEPEFFVFD SVRWQVDMSG SFVKVESEEA AWNTGKDYEH GNTGYRPSVK
GGYFPVPPVD SGQDLRSEMC LILEQLGIPV EVHHHEVATA GQMEIGTKFS TLVQRADWLQ
LQKYVVQNVA HAYGKTATFM PKPIVGDNGS GMHVHQSVWK DGKNLFAGDG YAGLSEFALY
YIGGIIKHAR ALNAITNPTT NSYKRLVPGF EAPVKLAYSS RNRSASIRIP YVANPKARRI
EARFPDPMAN PYLCFAALLM AGLDGVENKI HPGEAATKDL YHLPPEEDAK IPTVCHSLDQ
ALEYLDKDRA FLTKGGVFTD SFIDAYIELK MQEVTRFRMT PHPVEFDMYY AL
//
