ID Q73QJ9_TREDE Unreviewed; 241 AA.
AC Q73QJ9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Glutamine amidotransferase class-I domain protein {ECO:0000313|EMBL:AAS10939.1};
GN OrderedLocusNames=TDE_0444 {ECO:0000313|EMBL:AAS10939.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS10939.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS10939.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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DR EMBL; AE017226; AAS10939.1; -; Genomic_DNA.
DR RefSeq; NP_971058.1; NC_002967.9.
DR RefSeq; WP_002681526.1; NC_002967.9.
DR AlphaFoldDB; Q73QJ9; -.
DR STRING; 243275.TDE_0444; -.
DR PaxDb; 243275-TDE_0444; -.
DR GeneID; 2740426; -.
DR KEGG; tde:TDE_0444; -.
DR PATRIC; fig|243275.7.peg.431; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_1_12; -.
DR OrthoDB; 9806430at2; -.
DR Proteomes; UP000008212; Chromosome.
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:AAS10939.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008212};
KW Transferase {ECO:0000313|EMBL:AAS10939.1}.
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 241 AA; 26851 MW; EBD929B734476AEF CRC64;
MKKPLIGITG SCLYETSQSL FAGYERMYTN ADYVNSVLAA GGVPLMLPII DDEDAIQRQL
ENLSGIIIMG GHDVEPHFFN EEPLSCLGEI LPKRDVYELS LIKAAKALKK PVLGICRGMQ
ILNVAFGGSL YQDLSLIKRD IQIQHVQKAR PQERTHSIKT EAASIMQKVF GKEDMVNSYH
HMAVKDLAKD FKITAYAPDG VVEAIEYTGE GFIMGVQFHP EMMAAVHKAS LDLFKEFINR
C
//
