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Database: UniProt
Entry: D3H7F0_STRM6
LinkDB: D3H7F0_STRM6
Original site: D3H7F0_STRM6 
ID   D3H7F0_STRM6            Unreviewed;       188 AA.
AC   D3H7F0;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Anthranilate synthase component II (Glutamine amido-transferase) {ECO:0000313|EMBL:CBJ21792.1};
DE            EC=4.1.3.27 {ECO:0000313|EMBL:CBJ21792.1};
GN   OrderedLocusNames=smi_0542 {ECO:0000313|EMBL:CBJ21792.1};
OS   Streptococcus mitis (strain B6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ21792.1, ECO:0000313|Proteomes:UP000008563};
RN   [1] {ECO:0000313|EMBL:CBJ21792.1, ECO:0000313|Proteomes:UP000008563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:CBJ21792.1,
RC   ECO:0000313|Proteomes:UP000008563};
RX   PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA   Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA   Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT   "The genome of Streptococcus mitis B6--what is a commensal?";
RL   PLoS ONE 5:E9426-E9426(2010).
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DR   EMBL; FN568063; CBJ21792.1; -; Genomic_DNA.
DR   RefSeq; WP_000601934.1; NC_013853.1.
DR   RefSeq; YP_003445660.1; NC_013853.1.
DR   AlphaFoldDB; D3H7F0; -.
DR   STRING; 365659.smi_0542; -.
DR   MEROPS; C26.959; -.
DR   KEGG; smb:smi_0542; -.
DR   PATRIC; fig|365659.3.peg.513; -.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_014340_1_2_9; -.
DR   OrthoDB; 9804328at2; -.
DR   Proteomes; UP000008563; 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:0019438; P:aromatic compound 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   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound 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; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43418:SF8; SYNTHASE COMPONENT II, PUTATIVE-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};
KW   Lyase {ECO:0000313|EMBL:CBJ21792.1};
KW   Transferase {ECO:0000313|EMBL:CBJ21792.1}.
FT   DOMAIN          3..184
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        77
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   188 AA;  20938 MW;  9CCFEC9AB7EEC518 CRC64;
     MILLIDNYDS FTYNLAQYIG NFSEVQVLRN DDPKLYEEAE KADGLVFSPG PGWPVDAGKM
     EDMIRDFAGK KPILGICLGH QAIAEVFGGK LGLAPKVMHG KQSNISFEAP SILYQGIEDG
     RAVMRYHSIL IEEMPEDFEV TARSTDDQAI MGIQHKILPI YGFQYHPESI GTPDGLSSIR
     NFIEKVVK
//
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