ID A0A1B9EYR5_9ACTN Unreviewed; 249 AA.
AC A0A1B9EYR5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative glutamine amidotransferase {ECO:0000313|EMBL:OCC12842.1};
DE EC=2.4.2.- {ECO:0000313|EMBL:OCC12842.1};
GN ORFNames=A3Q37_01506 {ECO:0000313|EMBL:OCC12842.1};
OS Streptomyces sp. PTY087I2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1819298 {ECO:0000313|EMBL:OCC12842.1, ECO:0000313|Proteomes:UP000093256};
RN [1] {ECO:0000313|EMBL:OCC12842.1, ECO:0000313|Proteomes:UP000093256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTY087I2 {ECO:0000313|EMBL:OCC12842.1,
RC ECO:0000313|Proteomes:UP000093256};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCC12842.1}.
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DR EMBL; LZRD01000005; OCC12842.1; -; Genomic_DNA.
DR RefSeq; WP_065479417.1; NZ_LZRD01000005.1.
DR AlphaFoldDB; A0A1B9EYR5; -.
DR PATRIC; fig|1819298.4.peg.1570; -.
DR Proteomes; UP000093256; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01745; GATase1_2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR044668; PuuD-like.
DR PANTHER; PTHR43235; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR PANTHER; PTHR43235:SF1; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
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:OCC12842.1};
KW Glycosyltransferase {ECO:0000313|EMBL:OCC12842.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093256};
KW Transferase {ECO:0000313|EMBL:OCC12842.1}.
FT REGION 227..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 249 AA; 26135 MW; 413C29305233E8DC CRC64;
MPRPVIGIST YQDPARWGVW EMPAVLLPAA YPRLVRAAGG LAVLLPPDDA EDAARDTVAA
LDGLVIAGGA DVEPARYGAV ADPRTGPPAR ERDAWELALI RAAIDQRVPL LGICRGMQLL
NVALGGTLIQ HLEDHTGGLG VFGSHPVTPV TGTVYADAVP ETAMVPAYHH QAVDRLGTGL
VASAHAPDGT VEALELPDHA SLVLGVQWHP EMGQDTRVMS VLVRAAGERA APTPRTPDRS
SRAPRTPVS
//
