ID B1Y1M2_LEPCP Unreviewed; 285 AA.
AC B1Y1M2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:ACB35484.1};
GN OrderedLocusNames=Lcho_3226 {ECO:0000313|EMBL:ACB35484.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35484.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB35484.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001013; ACB35484.1; -; Genomic_DNA.
DR AlphaFoldDB; B1Y1M2; -.
DR STRING; 395495.Lcho_3226; -.
DR MEROPS; C26.A28; -.
DR KEGG; lch:Lcho_3226; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_1_4; -.
DR Proteomes; UP000001693; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 285 AA; 31546 MW; 3FB76D2218807C95 CRC64;
MPTLGRAGAL SRVPAYPLPV RERPLLIGMS ARLMHVPPVE LGFRGKTLQY LEQSLAHWIM
AHGAMAVMIP TLGFDAEVER RKVGVHHYVD MLDGLVLQGG ADVSPLSYGQ QPLRPEWAGD
AVRDRYEIEL IDGFLTQGKP MLGICRGCQL LNVAFGGSLL QDINTQRPDT RRHVDGVLYD
QLQHGLRFEP GSRLEKIYDG HASPRVNSIH HQAVDRLGSD LVVEARCDED GVVEAIRSRG
DLFVAGVQWH PEFHLHTREL LDAEPLMNAW LAAVKARRDG TAAPG
//
