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LOCUS WP_000211172 453 aa linear BCT 04-SEP-2023 alpha [Enterobacteriaceae]. ACCESSION WP_000211172 VERSION WP_000211172.1 KEYWORDS RefSeq. SOURCE Enterobacteriaceae ORGANISM Enterobacteriaceae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales. REFERENCE 1 (residues 1 to 453) AUTHORS Diaz,E., Ferrandez,A. and Garcia,J.L. TITLE Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12 JOURNAL J Bacteriol 180 (11), 2915-2923 (1998) PUBMED 9603882 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 :: NF042946.1 Evidence Source :: NCBIFAM ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..453 /organism="Enterobacteriaceae" /db_xref="taxon:543" gene 1..453 /gene="hcaE" Protein 1..453 /product="3-phenylpropionate/cinnamic acid dioxygenase subunit alpha" /EC_number="1.14.12.19" /GO_function="GO:0008695 - 3-phenylpropionate dioxygenase activity [Evidence IEA]" /GO_process="GO:0019380 - 3-phenylpropionate catabolic process [Evidence IEA]" /calculated_mol_wt=50978 Region 18..>226 /region_name="HcaE" /note="Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only]; COG4638" /db_xref="CDD:443676" Region 184..433 /region_name="RHO_alpha_C_NDO-like" /note="C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related aromatic ring hydroxylating dioxygenases; cd08881" /db_xref="CDD:176890" Site order(189..196,219..220,355,358..359,364,366,369..370, 372..373,376) /site_type="other" /note="beta subunit interface [polypeptide binding]" /db_xref="CDD:176890" Site order(205..206,210,212..213,217,373..375,377..378, 380..387,390..396,418) /site_type="other" /note="alpha subunit interface [polypeptide binding]" /db_xref="CDD:176890" Site order(206..207,210..211,213..214,218,304,306,316,361,367, 371) /site_type="active" /db_xref="CDD:176890" Site order(206..207,210..211,213..214,218,304,306,316,361,367) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:176890" Site order(213,218,371) /site_type="other" /note="Fe binding site [ion binding]" /db_xref="CDD:176890" ORIGIN 1 mttpsdlniy qlidtqngrv tpriytdpdi yqlelerifg rcwlflahes qipkpgdffn 61 tymgedavvv vrqkdgsika flnqcrhram rvsyadcgnt raftcpyhgw sygingelid 121 vplepraypq glckshwgln evpcvesykg lifgnwdtsa pglrdylgdi awyldgmldr 181 reggteivgg vqkwvincnw kfpaeqfasd qyhalfshas avqvlgakdd gsdkrlgdgq 241 tarpvwetak dalqfgqdgh gsgffftekp danvwvdgav ssyyretyae aeqrlgevra 301 lrlaghnnif ptlswlngta tlrvwhprgp dqvevwafci tdkaasdevk aafensatra 361 fgpagfleqd dsenwceiqk llkghrarns klclemglgq ekrrddgipg itnyifseta 421 argmyqrwad llsseswqev ldktaayqqe vmk