ID A0A2S9BS24_9MICO Unreviewed; 246 AA.
AC A0A2S9BS24;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glutamine amidotransferase {ECO:0000313|EMBL:PRB64030.1};
GN ORFNames=CQ034_07520 {ECO:0000313|EMBL:PRB64030.1};
OS Microbacterium sp. MYb45.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1827294 {ECO:0000313|EMBL:PRB64030.1, ECO:0000313|Proteomes:UP000238044};
RN [1] {ECO:0000313|EMBL:PRB64030.1, ECO:0000313|Proteomes:UP000238044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb45 {ECO:0000313|EMBL:PRB64030.1,
RC ECO:0000313|Proteomes:UP000238044};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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:PRB64030.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PCPG01000002; PRB64030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9BS24; -.
DR OrthoDB; 5196541at2; -.
DR Proteomes; UP000238044; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01741; GATase1_1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR044992; ChyE-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR42695; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR PANTHER; PTHR42695:SF5; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR Pfam; PF00117; GATase; 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:PRB64030.1}; Transferase {ECO:0000313|EMBL:PRB64030.1}.
FT DOMAIN 29..191
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 246 AA; 27084 MW; F300D585676AA9A2 CRC64;
MTIDSSRSRS ALAFRHVHFE DLGILEPLLI ERGYHVEYVD LGVQAIDIER VDDADLLIVL
GGPIGVYDTV HYPFLHASKE AIAHRLRQDR AMLGICLGAQ LIAEEMGAVV APTGSVEIGY
APLELTAEGL DSPLRPLDGL PVLHWHGDAF AIPEGARQLA RTPDFPNQAF ATDTVLALQF
HLEADHRTIG NWLIGHAHEL HHHDIDPRTI REQARIHGPR LETAARTAIA AWLDEVDSPA
HHADAN
//
