ID G9C9M0_DELAC Unreviewed; 256 AA.
AC G9C9M0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=DcaT {ECO:0000313|EMBL:AEX00485.1};
GN Name=dcaT {ECO:0000313|EMBL:AEX00485.1};
OS Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OG Plasmid pLME1 {ECO:0000313|EMBL:AEX00485.1}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=80866 {ECO:0000313|EMBL:AEX00485.1};
RN [1] {ECO:0000313|EMBL:AEX00485.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LME1 {ECO:0000313|EMBL:AEX00485.1};
RC PLASMID=pLME1 {ECO:0000313|EMBL:AEX00485.1};
RX PubMed=11229899; DOI=10.1128/AEM.67.3.1107-1115.2001;
RA Boon N., Goris J., De Vos P., Verstraete W., Top E.M.;
RT "Genetic diversity among 3-chloroaniline- and aniline-degrading strains of
RT the Comamonadaceae.";
RL Appl. Environ. Microbiol. 67:1107-1115(2001).
RN [2] {ECO:0000313|EMBL:AEX00485.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LME1 {ECO:0000313|EMBL:AEX00485.1};
RC PLASMID=pLME1 {ECO:0000313|EMBL:AEX00485.1};
RX PubMed=22101050; DOI=10.1128/AEM.07480-11;
RA Krol J.E., Penrod J.T., McCaslin H., Rogers L.M., Yano H., Stancik A.D.,
RA Dejonghe W., Brown C.J., Parales R.E., Wuertz S., Top E.M.;
RT "Role of IncP-1beta Plasmids pWDL7::rfp and pNB8c in Chloroaniline
RT Catabolism as Determined by Genomic and Functional Analyses.";
RL Appl. Environ. Microbiol. 78:828-838(2012).
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DR EMBL; JF274988; AEX00485.1; -; Genomic_DNA.
DR RefSeq; WP_015060609.1; NC_019263.1.
DR RefSeq; YP_006961402.1; NC_019263.1.
DR AlphaFoldDB; G9C9M0; -.
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 Plasmid {ECO:0000313|EMBL:AEX00485.1}.
FT DOMAIN 52..196
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 256 AA; 27402 MW; C818A4C7A949A098 CRC64;
MLIDTVKKKY AVLWCTEVPG DEILQEKMIA TFGRAGEQWD VLEPARDGFL ERAMGYDGYV
ISGSPMSVVD DADSLLVSNL LALIRRVSDE AGSPLIGLCF GSQAIAAALG GRVARNPSGR
FKLGVDALRW DPVAVELLGA ALAQAPSVLV KSHGECVAAL PPGSVLLASS QTIPHEVFLV
QGRILGIQGH PEVDRQFLKD KFMADHRALF DDEQWAHVEQ EASQPLSPDA VIALGRRLLD
EGALAPAAVP TLTETT
//
