ID B1XYY8_LEPCP Unreviewed; 256 AA.
AC B1XYY8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:ACB34007.1};
GN OrderedLocusNames=Lcho_1740 {ECO:0000313|EMBL:ACB34007.1};
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:ACB34007.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB34007.1, 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; ACB34007.1; -; Genomic_DNA.
DR RefSeq; WP_012346768.1; NC_010524.1.
DR AlphaFoldDB; B1XYY8; -.
DR STRING; 395495.Lcho_1740; -.
DR MEROPS; C26.961; -.
DR KEGG; lch:Lcho_1740; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_0_0_4; -.
DR OrthoDB; 9813383at2; -.
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 111
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 256 AA; 27508 MW; C626DE657DDB8475 CRC64;
MSRLPVVLVP ACNRMLGQHP FHVAGQKYVD AVRLAGALPL VVPSAHHDEI DALLDLADGV
LLSGSPSNVH PSRFGEDVHD PSLPLDPVRD DWTLPLIPLA LARGLPLFAI CRGFQEVNVA
LGGSLHQAVQ TLPGHLDHRA LAVLPVATQY GPAHRVAIRP GGLFERLFDG EGIDGFEVNS
LHGQGVNRLA DGLRIEALAP DGLVEAFSVT DTPGFGLGVQ WHPEWQAAHN PVSMTLLRAF
GAACQEYRDT HRPPSR
//
