ID A0A2P8CKJ8_9BACT Unreviewed; 729 AA.
AC A0A2P8CKJ8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:PSK85471.1};
GN ORFNames=CLV93_101427 {ECO:0000313|EMBL:PSK85471.1};
OS Prolixibacter denitrificans.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Prolixibacter.
OX NCBI_TaxID=1541063 {ECO:0000313|EMBL:PSK85471.1, ECO:0000313|Proteomes:UP000240621};
RN [1] {ECO:0000313|EMBL:PSK85471.1, ECO:0000313|Proteomes:UP000240621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27267 {ECO:0000313|EMBL:PSK85471.1,
RC ECO:0000313|Proteomes:UP000240621};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PSK85471.1}.
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DR EMBL; PYGC01000001; PSK85471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8CKJ8; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000240621; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.1560; -; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR040577; Gln-synt_C.
DR InterPro; IPR008147; Gln_synt_N.
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; IPR022147; GSIII_N.
DR PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF18318; Gln-synt_C-ter; 1.
DR Pfam; PF12437; GSIII_N; 1.
DR SMART; SM01230; Gln-synt_C; 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;
FT DOMAIN 85..174
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 179..615
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 729 AA; 81987 MW; 1DF1E49BC9212BA8 CRC64;
MATFRFKALE TLLERKPVCV PREANLTSDY YGKLVFDREK MKKYLSKEGY KAVTDAIDKG
TTIDRKSADL VAVGMKAWAL ENGATHYTHW FHPLTDGTAE KHDAFIEYSE LGGVVENFSG
KLLAQQEPDA SSFPSGGLRN TFEARGYTAW DVSSPAFIVG TTLCIPTVFI SYTGEALDYK
APLLKALNAV DKAAVAVCQY FDKNVSKVQA NLGWEQEYFL IDEALYNARP DLILTGRTLM
GHSSSKDQQL DDHYFGSIPE RVSYFMRDLE NEAYKLGIPV KTRHNEVAPN QFEVAPIFEE
VNLANDHNQL IMDTMSRIAR HHGFRVLLHE KPFAGINGSG KHNNWSLSTD TGVNLYSPGK
NPKANMQFLT FVVNTLKTLH DNQDLLRASI LTAANAHRLG ANEAPPAIIS AFLGTEVNRM
LDYLEEAVVD RKMTPDEKTA LKLDIGRIPE ILLDNTDRNR TSPFAFTGNR FEFRAVGSSA
NCASAMIALN TALAKQLTVF KKDVDVIIES GVKKDEAIFQ VLKKYIVECK DIRFDGNGYS
EEWVEEAARR GLTNVKNVPE ALDAYLSDKV VNLFGEMGIY TPKELEGRTE VEFEKFTKKI
QIEARVLGDL AINHIVPTAI RYQTALIENV QGLKDLFPAS EFEKLAGARL DMIRTISGHI
SNIKAKVSEM IETRKVANAI ESEREKAYAY DKTVRPFLDD IRYHIDKLEL IVDDELWPLP
KYRELLFAR
//
