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Database: UniProt
Entry: F6GDI2_LACS5
LinkDB: F6GDI2_LACS5
Original site: F6GDI2_LACS5 
ID   F6GDI2_LACS5            Unreviewed;       187 AA.
AC   F6GDI2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Glutamine amidotransferase of anthranilate synthase {ECO:0000313|EMBL:AEH01586.1};
DE            EC=4.1.3.27 {ECO:0000313|EMBL:AEH01586.1};
GN   OrderedLocusNames=Lacal_1738 {ECO:0000313|EMBL:AEH01586.1};
OS   Lacinutrix sp. (strain 5H-3-7-4).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lacinutrix.
OX   NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH01586.1, ECO:0000313|Proteomes:UP000008297};
RN   [1] {ECO:0000313|EMBL:AEH01586.1, ECO:0000313|Proteomes:UP000008297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH01586.1,
RC   ECO:0000313|Proteomes:UP000008297};
RX   PubMed=21725025; DOI=10.1128/JB.05518-11;
RA   Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA   Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA   Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA   Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT   "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT   Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT   family Flavobacteriaceae.";
RL   J. Bacteriol. 193:4545-4546(2011).
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DR   EMBL; CP002825; AEH01586.1; -; Genomic_DNA.
DR   RefSeq; WP_013870365.1; NC_015638.1.
DR   AlphaFoldDB; F6GDI2; -.
DR   STRING; 983544.Lacal_1738; -.
DR   MEROPS; C26.955; -.
DR   KEGG; lan:Lacal_1738; -.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_014340_1_2_10; -.
DR   OrthoDB; 9786812at2; -.
DR   Proteomes; UP000008297; Chromosome.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProt.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProt.
DR   GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW   ECO:0000313|EMBL:AEH01586.1}; Lyase {ECO:0000313|EMBL:AEH01586.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008297};
KW   Transferase {ECO:0000313|EMBL:AEH01586.1}.
FT   DOMAIN          4..185
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   187 AA;  20854 MW;  50842540B4E89311 CRC64;
     MKVLVIDNYD SFTYNLVHYL EDLNCQVTVK RNDKLTLEDV EPFNKIVLSP GPGIPDEAGL
     LKAIIKKYAP TKSILGVCLG QQAIGEVFGG KLLNLDTVYH GVSTKVNITV DNEPLFNNME
     KTIEVGRYHS WVVAAELPDS LEATSVDENG QIMSLRHKVY DVKGVQYHPE SVLTPNGKQI
     LKNWVNN
//
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