ID A0A2V4NRP1_9RHOB Unreviewed; 444 AA.
AC A0A2V4NRP1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:PYC49227.1};
GN ORFNames=DI396_01720 {ECO:0000313|EMBL:PYC49227.1};
OS Litorivita pollutaquae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Litorivita.
OX NCBI_TaxID=2200892 {ECO:0000313|EMBL:PYC49227.1, ECO:0000313|Proteomes:UP000248012};
RN [1] {ECO:0000313|EMBL:PYC49227.1, ECO:0000313|Proteomes:UP000248012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSX-11 {ECO:0000313|EMBL:PYC49227.1,
RC ECO:0000313|Proteomes:UP000248012};
RA Hetharua B.H., Min D., Liao H., Tian Y.;
RT "Oceanovita maritima gen. nov., sp. nov., a marine bacterium in the family
RT Rhodobacteraceae isolated from surface seawater of Lundu port Xiamen,
RT China.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000256|ARBA:ARBA00003117}.
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|PROSITE-ProRule:PRU01330, 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:PYC49227.1}.
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DR EMBL; QFVT01000002; PYC49227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4NRP1; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000248012; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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 PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000248012}.
FT DOMAIN 9..104
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 111..444
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 444 AA; 48559 MW; 0C7087A318D5213E CRC64;
MKNWLRKHPL VRTIRVAAAD LNGQARGKRV PTRFADKVVE DGTRFPLSVL NLDIWGEDID
DSPLVFDSGD ADGVLKPTER GFMPMPWLKA PTALLPIWMF RENGQPYEGD PRHALRAVVD
RYTARGLTPV CAMELEFFLI DDSGKNPQIP ISPRSGIRRK GAETLSIRAL DAFDDFFTDL
YDACEEMDIP ADTAISEAGL GQFEVNLMHC DDALRAADDA WLFKMLVKGL ARSHGFAASF
MAKPYADYAG SGLHTHFSVL NKNGDNIFDD GGAKGTPALR HAVTGCLNAM SGSTLLFAPH
ANSYDRMVPG AHAPTGICWA YENRTSAIRI PSGAPAARRI EHRVAGGDVN PYLLLASILG
AALNGIEDGI EPPEPITGNA YAADLPQMPT QWGAAIDAFE ASPEIARIFA PELIRNLVLT
KRQELHFMSE LDATEQVEIY LDTV
//
