ID U2R6C9_LEPWF Unreviewed; 242 AA.
AC U2R6C9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:ERK49193.1};
GN ORFNames=HMPREF9015_01383 {ECO:0000313|EMBL:ERK49193.1};
OS Leptotrichia wadei (strain F0279).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=888055 {ECO:0000313|EMBL:ERK49193.1, ECO:0000313|Proteomes:UP000016626};
RN [1] {ECO:0000313|EMBL:ERK49193.1, ECO:0000313|Proteomes:UP000016626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0279 {ECO:0000313|EMBL:ERK49193.1,
RC ECO:0000313|Proteomes:UP000016626};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERK49193.1}.
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DR EMBL; AWVM01000079; ERK49193.1; -; Genomic_DNA.
DR RefSeq; WP_021746052.1; NZ_KI271401.1.
DR AlphaFoldDB; U2R6C9; -.
DR PATRIC; fig|888055.3.peg.1323; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_1_0; -.
DR Proteomes; UP000016626; 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: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}.
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 242 AA; 27433 MW; 2DC5DA4C26AB8854 CRC64;
MNNKRKPLIG ITTSLELNPN RLNDHKTIVS VDYSKAVINS GGIPFILPIT ENIEVIKEQI
QLLDGLLLSG GGDPDPALYG EDCLQEVGSI TPERDKFELV ILDEFMKTGK PILGICRGLQ
IANVYFGGSL YQDVKYIDTT INHMQKWLPD LPTHDINIEE GNILFEIFGK KARTNSYHHQ
MIKDLGNGLT SIAKANDGII EAFQNKNHKF FYAVQWHPEM MAVRGNEKMQ RIFDKFIENC
RK
//
