ID Q2IM24_ANADE Unreviewed; 236 AA.
AC Q2IM24;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:ABC79854.1};
GN OrderedLocusNames=Adeh_0076 {ECO:0000313|EMBL:ABC79854.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79854.1, ECO:0000313|Proteomes:UP000001935};
RN [1] {ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000251; ABC79854.1; -; Genomic_DNA.
DR RefSeq; WP_011419137.1; NC_007760.1.
DR AlphaFoldDB; Q2IM24; -.
DR STRING; 290397.Adeh_0076; -.
DR KEGG; ade:Adeh_0076; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_0_7; -.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000001935; 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:UP000001935}.
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 236 AA; 24940 MW; 2B56B4BDD23E10D9 CRC64;
MSPRPRIGIT LDADATGRRY ELPRGYVEAV LDAGGLPILL PHAVDVAGAY LSLLDGLVVS
GGDFDLPPEL YGEARRPGCG PSRPERTRFE KDLLEAALAA RLPVLGVCGG MQLLDVVRGG
TLWQDLPGEA GLRGHEQPAP KDVPSHEVTI APGTQLAALA GAGPLMVNST HHQAVREPGP
GVLVSARAPD GVVEAIELPD LPFALGVQWH PEATRDDPRH AAIYRGLVDA ARSLRR
//
