ID C1D1Q2_DEIDV Unreviewed; 207 AA.
AC C1D1Q2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Putative Anthranilate synthase component II {ECO:0000313|EMBL:ACO45776.1};
GN OrderedLocusNames=Deide_09000 {ECO:0000313|EMBL:ACO45776.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO45776.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO45776.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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DR EMBL; CP001114; ACO45776.1; -; Genomic_DNA.
DR RefSeq; WP_012692899.1; NC_012526.1.
DR AlphaFoldDB; C1D1Q2; -.
DR STRING; 546414.Deide_09000; -.
DR MEROPS; C26.955; -.
DR PaxDb; 546414-Deide_09000; -.
DR KEGG; ddr:Deide_09000; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_0; -.
DR OrthoDB; 9804328at2; -.
DR Proteomes; UP000002208; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 7..190
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 207 AA; 23097 MW; EAC3B7ED370F8380 CRC64;
MTPLRILLID NYDSFTYNLV QYLGELGAEL TVWRNDAFTL DDVRALNPDG IVVSPGPCTP
AEAGQSVDVI RAFGPSVPML GVCLGHQSIG EAYGARVDRA MLPVHGKTSP VRHDGQDLFA
GLEQDVRVTR YHSLVVRDLP EELQATAWTT DPEEEVVMAL RHREYPVYGL QFHPESIETQ
AGMDMLRNFL ALVREHRTVS TRPEQQA
//