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LOCUS WP_000852664 202 aa linear BCT 17-JUN-2024 [Salmonella]. ACCESSION WP_000852664 VERSION WP_000852664.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 202) AUTHORS Rousset,M., Dermoun,Z., Wall,J.D. and Belaich,J.P. TITLE Analysis of the periplasmic [NiFe] hydrogenase transcription unit from Desulfovibrio fructosovorans JOURNAL J Bacteriol 175 (11), 3388-3393 (1993) PUBMED 8501043 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 :: TIGR00140.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..202 /organism="Salmonella" /db_xref="taxon:590" gene 1..202 /gene="hybD" Protein 1..202 /product="HyaD/HybD family hydrogenase maturation endopeptidase" /GO_component="GO:0009375 - ferredoxin hydrogenase complex [Evidence IEA]" /GO_function="GO:0004190 - aspartic-type endopeptidase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_process="GO:0051604 - protein maturation [Evidence IEA]" /calculated_mol_wt=22014 Region 4..182 /region_name="H2MP" /note="Hydrogenase specific C-terminal endopeptidases, also called Hydrogen Maturation Proteases (H2MP). These enzymes belong to the peptidase family M52. Maturation of [FeNi] hydrogenases includes formation of the nickel metallocenter, proteolytic processing...; cl00477" /db_xref="CDD:444928" Site order(11,25,41..43) /site_type="active" /note="putative substrate-binding site [active]" /db_xref="CDD:99873" Site order(17,63,94) /site_type="other" /note="nickel binding site [ion binding]" /db_xref="CDD:99873" ORIGIN 1 maevtilglg nllwadegfg vraaeklfeq yadnekvdvv dggtqglall pwlqqtekll 61 imdaidfgma pgslamfrde qvpayltakk lslhqtsfse vlallqltgg qlseivligv 121 qpeclddygg sltpqvkaql mpavylaqev laqwgitass aalpterlnh yslcmeryed 181 erpdaqsacr vgdirvlqre ks