ID   E6XA57_CELAD            Unreviewed;       728 AA.
AC   E6XA57;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Glutamine synthetase catalytic region {ECO:0000313|EMBL:ADV47747.1};
GN   OrderedLocusNames=Celal_0404 {ECO:0000313|EMBL:ADV47747.1};
OS   Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV47747.1, ECO:0000313|Proteomes:UP000008634};
RN   [1] {ECO:0000313|EMBL:ADV47747.1, ECO:0000313|Proteomes:UP000008634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14237 / IC166 / ACAM 630
RC   {ECO:0000313|Proteomes:UP000008634};
RX   PubMed=21475589; DOI=10.4056/sigs.1543845;
RA   Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL   Stand. Genomic Sci. 4:72-80(2010).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; CP002453; ADV47747.1; -; Genomic_DNA.
DR   RefSeq; WP_013549242.1; NC_014934.1.
DR   AlphaFoldDB; E6XA57; -.
DR   STRING; 688270.Celal_0404; -.
DR   KEGG; cao:Celal_0404; -.
DR   eggNOG; COG3968; Bacteria.
DR   HOGENOM; CLU_024307_0_0_10; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000008634; Chromosome.
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          84..173
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          178..615
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   728 AA;  81972 MW;  D80B870CBA231BAD CRC64;
     MSKIRLEAIS KSQDRERIPI EEKGRRSELF GVNVFNEERM LQYLTKDALE SVQSAIFSGS
     KIDRKIADQV AESMKSWAIT MGATHYTHWF QPLTGATAEK HDAFFDLLPD GRALEKFGGG
     QLVQQEPDAS SFPSGGIRNT FEARGYTAWD PTSAAFIYGT TLCIPTIFVS YTGEALDNKA
     PLLRALGAVD EAATAVAKYF DKNVSKVNAT LGWEQEYFLL DKALAVSRPD IVMTGRTLIG
     HQAAKGQQLD DHYFGVIPDR VLSFMSDLEK ECTKLGIPVK TRHNEVAPNQ FELAPVFEEA
     NLAVDHNLLL MDVMDKIADK HHFKVLFHEK PFAGINGSGK HNNWSLATDT GVNLLSPGST
     PMKNLQFLTF FINTIKAVDT YEELLRASIA SASNDHRLGA NEAPPAIFSI FVGTQLSNVL
     DELEGVSHGK LSPEEKTELK LNVVGKIPEI LLDNTDRNRT SPFAFTGNKF EMRGVGAKTN
     CAKPMTVLNT IVAKQLIDFK KEVDILIDKK SLKKDEAVFN VLREYIKTSK RIRFDGDGYS
     DEWEKEAERR KLSNNKNTPS ALQVLTSKES LDLFRTMKVM SEVEISARKE VELETYIFQL
     QIEGRMYNEL VYSYIIPAAV KYQNELIKNV MGLKDIYGAA HKKLTDGQLS LIEQIAEHIA
     DVKKQSDLMT DARRSANRLK DIDKKAFAYC DTVKPYFNKI RLHCDKLESL MDNNLWPLTK
     YRELLFQK
//