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Database: UniProt
Entry: D0SVR5_ACILW
LinkDB: D0SVR5_ACILW
Original site: D0SVR5_ACILW 
ID   D0SVR5_ACILW            Unreviewed;       238 AA.
AC   D0SVR5;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Class I glutamine amidotransferase {ECO:0000313|EMBL:EEY89972.1};
GN   ORFNames=HMPREF0017_01389 {ECO:0000313|EMBL:EEY89972.1};
OS   Acinetobacter lwoffii SH145.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY89972.1, ECO:0000313|Proteomes:UP000018425};
RN   [1] {ECO:0000313|Proteomes:UP000018425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
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DR   EMBL; GG705059; EEY89972.1; -; Genomic_DNA.
DR   RefSeq; WP_004279966.1; NZ_GG705059.1.
DR   AlphaFoldDB; D0SVR5; -.
DR   eggNOG; COG0518; Bacteria.
DR   HOGENOM; CLU_054974_3_1_6; -.
DR   Proteomes; UP000018425; 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:EEY89972.1}; Transferase {ECO:0000313|EMBL:EEY89972.1}.
FT   DOMAIN          30..187
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        180
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   238 AA;  26633 MW;  B06B1CDD2A94BDE3 CRC64;
     MLNLAHLPDT VYAIQHLAFE DLGAWEDIFY QLGLRVRYFE AGIDDLTKAF EHPGLTVILG
     GPIAVYETED YPFLQQEMDL LKVRLQKNLP TLGICLGAQL IAAALNAKVY PGDVKEIGWS
     KLSLTSIENN PLKALEDIDI LHWHGDTFDL PEQAELLASS DLYPNQAFQV GQNILALQFH
     AEVASESLEK WLIGHTCELR KAQINIPALR ADHQSYATAL EQAASSVLMH YLENLQLK
//
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