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LOCUS WP_001130633 372 aa linear BCT 08-JUN-2023 ACCESSION WP_001130633 VERSION WP_001130633.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 372) AUTHORS Lehmann,C., Doseeva,V., Pullalarevu,S., Krajewski,W., Howard,A. and Herzberg,O. TITLE YbdK is a carboxylate-amine ligase with a gamma-glutamyl:Cysteine ligase activity: crystal structure and enzymatic assays JOURNAL Proteins 56 (2), 376-383 (2004) PUBMED 15211520 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 :: HMM Evidence Accession :: NF010040.1 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK13516 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..372 /organism="Escherichia coli" /db_xref="taxon:562" Protein 1..372 /product="YbdK family carboxylate-amine ligase" /EC_number="6.3.2.2" /GO_function="GO:0004357 - glutamate-cysteine ligase activity [Evidence IEA]" /GO_process="GO:0042398 - cellular modified amino acid biosynthetic process [Evidence IEA]" /calculated_mol_wt=41553 Region 1..372 /region_name="PRK13516" /note="gamma-glutamyl:cysteine ligase; Provisional" /db_xref="CDD:237407" ORIGIN 1 mplpdfhvse pftlgielem qvvnppgydl sqdssmlida vknkitagev khditesmle 61 latdvcrdin qaagqfsamq kvvlqaaadh hleicgggth pfqkwqrqev cdneryqrtl 121 enfgyliqqa tvfgqhvhvg casgddaiyl lhglsrfvph fialsaaspy mqgtdtrfas 181 srpnifsafp dngpmpwvsn wqqfealfrc lsyttmidsi kdlhwdirps phfgtvevrv 241 mdtpltlsha vnmagliqat ahwllterpf khkekdylly kfnrfqacry glegvitdpy 301 tgdrrplted tlrllekiap sahkigassa iealhrqvvs glneaqlmrd fvadggslig 361 lvkkhceiwa gd