ID A1TAV6_MYCVP Unreviewed; 243 AA.
AC A1TAV6;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Glutamine amidotransferase class-I {ECO:0000313|EMBL:ABM14306.1};
GN OrderedLocusNames=Mvan_3511 {ECO:0000313|EMBL:ABM14306.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM14306.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM14306.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000511; ABM14306.1; -; Genomic_DNA.
DR RefSeq; WP_011780710.1; NZ_JACKSD010000223.1.
DR AlphaFoldDB; A1TAV6; -.
DR STRING; 350058.Mvan_3511; -.
DR KEGG; mva:Mvan_3511; -.
DR eggNOG; COG0518; Bacteria.
DR HOGENOM; CLU_054974_3_4_11; -.
DR OMA; VCFGGQL; -.
DR Proteomes; UP000009159; Chromosome.
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:ABM14306.1}; Transferase {ECO:0000313|EMBL:ABM14306.1}.
FT DOMAIN 81..184
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 102
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 243 AA; 26212 MW; 66E7119CE1630F45 CRC64;
MADVASKVLF LVNEHIATEA LLGDAFAEQG FDVDTFEVVP AERVGAPAGE VTFPDPGGYD
VIVPLGASWP VYDESLRDTW VGTEMQLLRD AADAGIAVLG VCFGGQLLAQ AFGGSVARSP
RPEIGWYDVL SDRPEVVPGG PWFQWHFDRW TPPPGATEIA RTPNASQAFV LGRTLALQFH
PEVDGDLLKM WLAADRDGDV IAAGLDHDEL LTRTTELAQD TGPRIRSLVR GFLTHVAGHS
RPS
//