ID C8W334_DESAS Unreviewed; 201 AA.
AC C8W334;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Glutamine amidotransferase of anthranilate synthase {ECO:0000313|EMBL:ACV61801.1};
GN OrderedLocusNames=Dtox_0907 {ECO:0000313|EMBL:ACV61801.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61801.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV61801.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
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DR EMBL; CP001720; ACV61801.1; -; Genomic_DNA.
DR RefSeq; WP_015756517.1; NC_013216.1.
DR AlphaFoldDB; C8W334; -.
DR STRING; 485916.Dtox_0907; -.
DR MEROPS; C26.955; -.
DR KEGG; dae:Dtox_0907; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_9; -.
DR OrthoDB; 9804328at2; -.
DR Proteomes; UP000002217; 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:ACV61801.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW Transferase {ECO:0000313|EMBL:ACV61801.1}.
FT DOMAIN 3..185
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 201 AA; 22477 MW; 869C9DD65C875EA2 CRC64;
MILMIDNYDS FTYNLVQYFA KLGERVTVVR NDKITLTEVK SMKPEGIVIS PGPGNPDSAG
ISLELVKNFS GRLPILGVCL GHQVIGQAFG GRVVRAARLM HGKTSAVVHD GETIFNQVPT
PFTAVRYHSL LVEKESLPDC LEITAWTEQG EIMGLRHKVY PVEGVQFHPE SMLSEYGMDM
LANFLNMVQK HKEYRIIEKV V
//
