ID Q6AMS6_DESPS Unreviewed; 213 AA.
AC Q6AMS6;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Probable para-aminobenzoate/anthranilate synthase glutamine amidotransferase, component II {ECO:0000313|EMBL:CAG36349.1};
GN OrderedLocusNames=DP1620 {ECO:0000313|EMBL:CAG36349.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36349.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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DR EMBL; CR522870; CAG36349.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6AMS6; -.
DR STRING; 177439.DP1620; -.
DR MEROPS; C26.955; -.
DR KEGG; dps:DP1620; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_7; -.
DR Proteomes; UP000000602; Chromosome.
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; 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 ECO:0000313|EMBL:CAG36349.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000602};
KW Transferase {ECO:0000313|EMBL:CAG36349.1}.
FT DOMAIN 13..201
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 213 AA; 23629 MW; 3DE89A9F6A02C6E6 CRC64;
MCPAKKKERP MLVVIDNYDS FTYNIVQTIA ANSLAEGRQE DIRVYRNDQI TVAEIEALKP
DRLLISPGPC SPDKAGISVA AIRHFAGKIP ILGVCLGHQS IAEAFGGRVV RAERLMHGKT
SPMSHDGRGI FVGLASPFAG MRYHSLLVEE RGLPDCLEIS CRSDQGELMA MRHRDYKIEG
VQFHPESIMT PAGVQLLANF MSADYEKNYP QER
//
