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LOCUS WP_002910650 109 aa linear BCT 27-JUL-2024 [Klebsiella]. ACCESSION WP_002910650 VERSION WP_002910650.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 109) AUTHORS Oakley,A.J., Coggan,M. and Board,P.G. TITLE Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism JOURNAL J Biol Chem 285 (13), 9642-9648 (2010) PUBMED 20110353 REFERENCE 2 (residues 1 to 109) AUTHORS Oakley,A.J., Yamada,T., Liu,D., Coggan,M., Clark,A.G. and Board,P.G. TITLE The identification and structural characterization of C7orf24 as gamma-glutamyl cyclotransferase. An essential enzyme in the gamma-glutamyl cycle JOURNAL J Biol Chem 283 (32), 22031-22042 (2008) PUBMED 18515354 REMARK Erratum:[J Biol Chem. 2008 Nov 14;283(46):32152] COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10159924 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..109 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..109 /product="gamma-glutamylcyclotransferase family protein" /EC_number="2.3.2.-" /GO_function="GO:0016746 - acyltransferase activity [Evidence IEA]" /calculated_mol_wt=11983 Region 4..105 /region_name="GGCT_like" /note="GGCT-like domains, also called AIG2-like family. Gamma-glutamyl cyclotransferase (GGCT) catalyzes the formation of pyroglutamic acid (5-oxoproline) from dipeptides containing gamma-glutamyl, and is a dimeric protein. In Homo sapiens, the protein is...; cd06661" /db_xref="CDD:119400" Site order(4,7,9..10,79..80,83,105) /site_type="active" /note="putative active site pocket [active]" /db_xref="CDD:119400" Site order(51..52,54,83..87,89,101,104) /site_type="other" /note="dimerization interface [polypeptide binding]" /db_xref="CDD:119400" Site 80 /site_type="active" /note="putative catalytic residue [active]" /db_xref="CDD:119400" ORIGIN 1 mkplfvygtl cpgrsnahil eaiggewrpg yvtgtfyarg wgaaadfpgi vldahgprvn 61 gylflsdrla ahwpmlddfe egydrvpvev ttddgqqisa wiyqlqprg