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LOCUS WP_000543457 314 aa linear BCT 14-MAR-2024 acid 1,2-dioxygenase [Bacteria]. ACCESSION WP_000543457 VERSION WP_000543457.1 KEYWORDS RefSeq. SOURCE Bacteria (eubacteria) ORGANISM Bacteria Unclassified. REFERENCE 1 (residues 1 to 314) AUTHORS Xu,Y. and Zhou,N.Y. TITLE MhpA Is a Hydroxylase Catalyzing the Initial Reaction of 3-(3-Hydroxyphenyl)Propionate Catabolism in Escherichia coli K-12 JOURNAL Appl Environ Microbiol 86 (4), e02385-19 (2020) PUBMED 31811039 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 314) AUTHORS Mendel,S., Arndt,A. and Bugg,T.D. TITLE Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB) JOURNAL Biochemistry 43 (42), 13390-13396 (2004) PUBMED 15491145 REFERENCE 3 (residues 1 to 314) AUTHORS Ferrandez,A., Garcia,J.L. and Diaz,E. TITLE Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12 JOURNAL J Bacteriol 179 (8), 2573-2581 (1997) PUBMED 9098055 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 :: BlastRule Evidence Accession :: NBR016300 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..314 /organism="Bacteria" /db_xref="taxon:2" gene 1..314 /gene="mhpB" Protein 1..314 /product="2,3-dihydroxyphenylpropionate/2, 3-dihydroxicinnamic acid 1,2-dioxygenase" /EC_number="1.13.11.16" /calculated_mol_wt=34065 Region 1..311 /region_name="MhpB_like" /note="Subunit B of the Class III Extradiol ring-cleavage dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB), which catalyzes the oxidization and subsequent ring-opening of 2,3-dihydroxyphenylpropionate; cd07365" /db_xref="CDD:153377" Site order(10..12,53,115,179,271,302..303) /site_type="active" /note="putative active site [active]" /db_xref="CDD:153377" Site order(10,53,271) /site_type="other" /note="Fe(II) binding site [ion binding]" /db_xref="CDD:153377" Site order(12,53..55,58..59,77..78,141..145,232..234,258..259, 262..264,267..268,271,297..298,302) /site_type="other" /note="putative dimer interface [polypeptide binding]" /db_xref="CDD:153377" Site order(59,61..65,88..89,92..93,96..97,99..100,102,104..110, 144,147,149..150,164) /site_type="other" /note="putative tetramer interface [polypeptide binding]" /db_xref="CDD:153377" ORIGIN 1 mhaylhclsh splvgyvdpa qevldevngv iasareriaa fspelvvlfa pdhyngffyd 61 vmppfclgvg ataigdfgsa agelpvpvel aeacahavmk sgidlavsyc mqvdhgfaqp 121 lefllggldk vpvlpvfing vatplpgfqr trmlgeaigr ftstlnkrvl flgsgglshq 181 ppvpelakad ahmrdrllgs gkdlpasere lrqqrvisaa ekfvedqrtl hplnpiwdnq 241 fmtlleqgri qeldavsnee lsaiagksth eiktwvaafa aisafgnwrs egryyrpipe 301 wiagfgslsa rten