ID A0A139NT37_9STRE Unreviewed; 230 AA.
AC A0A139NT37;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Glutamine amidotransferase, class I {ECO:0000313|EMBL:KXT79092.1};
GN ORFNames=STRDD13_00211 {ECO:0000313|EMBL:KXT79092.1};
OS Streptococcus sp. DD13.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT79092.1, ECO:0000313|Proteomes:UP000070387};
RN [1] {ECO:0000313|EMBL:KXT79092.1, ECO:0000313|Proteomes:UP000070387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD13 {ECO:0000313|EMBL:KXT79092.1,
RC ECO:0000313|Proteomes:UP000070387};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-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:KXT79092.1}.
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DR EMBL; LQRH01000009; KXT79092.1; -; Genomic_DNA.
DR RefSeq; WP_067100707.1; NZ_KQ969506.1.
DR AlphaFoldDB; A0A139NT37; -.
DR STRING; 1777881.STRDD13_00211; -.
DR PATRIC; fig|1777881.3.peg.219; -.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000070387; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:KXT79092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070387};
KW Transferase {ECO:0000313|EMBL:KXT79092.1}.
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 230 AA; 25722 MW; 048A3070AC132E80 CRC64;
MKKPIIGIAG NERPFPEDPD VTMNYIPSGF VEGVQTVGGL PLHIPLSDIR QVPTYIQLID
KLILTGGQNV LPQFYKEEQT IESDDYLLKR DEFELALITE AIRQKKPIFG VCRGLQLFNV
AMGGTLHQEI EGHWQEASGL KATHGITVDP SSVLYAIYQE KAVVNSFHHQ SIHQLAPNLT
VIARATEDQV IEAVTTTDET RFLGVQWHPE LRQGVSKADL ALFDYVVHKL
//