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Database: UniProt
Entry: D9W1V6_9ACTN
LinkDB: D9W1V6_9ACTN
Original site: D9W1V6_9ACTN 
ID   D9W1V6_9ACTN            Unreviewed;       198 AA.
AC   D9W1V6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=GMP synthase domain-containing protein {ECO:0000313|EMBL:EFL18149.1};
GN   ORFNames=SSNG_05401 {ECO:0000313|EMBL:EFL18149.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL18149.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL18149.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL18149.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657750; EFL18149.1; -; Genomic_DNA.
DR   RefSeq; WP_007267074.1; NZ_GG657750.1.
DR   AlphaFoldDB; D9W1V6; -.
DR   STRING; 253839.SSNG_05401; -.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_014340_1_2_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
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; PR00099; CPSGATASE.
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}.
FT   DOMAIN          4..186
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        79
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   198 AA;  21037 MW;  1AF37F89535EAB08 CRC64;
     MKVLLVDAYD SFTHIIDQYL RTLGADTEVV RSRTESPDEL AARLPDAVVL GPGPGHPAES
     GHVELVHRFA GRVPLLGICL GHQAIGLAYG GRVRVADRLK HGKTSEVAHD GAGVFAGLGE
     TMTATRYHSL IVAEPLPQEL LATAHAVDDG YVMGLRHRTL AVEGVQFHPE SITTVGGMPL
     LRNFLTGART RPAGTLAG
//
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