ID D6ZB55_SEGRD Unreviewed; 213 AA.
AC D6ZB55;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Glutamine amidotransferase of anthranilate synthase {ECO:0000313|EMBL:ADG96814.1};
GN OrderedLocusNames=Srot_0327 {ECO:0000313|EMBL:ADG96814.1};
OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS 44985 / JCM 13578).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC Segniliparus.
OX NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96814.1, ECO:0000313|Proteomes:UP000002247};
RN [1] {ECO:0000313|EMBL:ADG96814.1, ECO:0000313|Proteomes:UP000002247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC {ECO:0000313|Proteomes:UP000002247};
RX PubMed=21304703; DOI=10.4056/sigs.791633;
RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT 1076).";
RL Stand. Genomic Sci. 2:203-211(2010).
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DR EMBL; CP001958; ADG96814.1; -; Genomic_DNA.
DR RefSeq; WP_013137270.1; NC_014168.1.
DR AlphaFoldDB; D6ZB55; -.
DR STRING; 640132.Srot_0327; -.
DR MEROPS; C26.955; -.
DR KEGG; srt:Srot_0327; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_11; -.
DR OrthoDB; 9803598at2; -.
DR Proteomes; UP000002247; 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:ADG96814.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW Transferase {ECO:0000313|EMBL:ADG96814.1}.
FT DOMAIN 6..191
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 213 AA; 22643 MW; DF12172144935E24 CRC64;
MTARVLVVDN YDSFVFNLVQ YLRQLEAAVS VWRNDDPRLA DPDGAIAEYD GVLVSPGPSS
PEKAGASIPV VLSAARQRKP LLGVCLGHQA IGVAFGGVVG RAPELLHGKT SKITHTDSGV
FAGLPQGFIA TRYHSLSIQE DTLPSVLAVT ARSESGVIMG VAHRELPVQG VQFHPESILT
QGGHRMLANW LGDCGRPVED SLVRELAAHV LPA
//