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LOCUS WP_017005143 117 aa linear BCT 28-AUG-2024 ACCESSION WP_017005143 VERSION WP_017005143.1 KEYWORDS RefSeq. SOURCE Enterovibrio sp. FF113 ORGANISM Enterovibrio sp. FF113 Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; Enterovibrio. REFERENCE 1 (residues 1 to 117) AUTHORS Haussmann,C., Rohdich,F., Schmidt,E., Bacher,A. and Richter,G. TITLE Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase JOURNAL J. Biol. Chem. 273 (28), 17418-17424 (1998) PUBMED 9651328 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 :: TIGR00525.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..117 /organism="Enterovibrio sp. FF113" /db_xref="taxon:3230010" gene 1..117 /gene="folB" Protein 1..117 /product="dihydroneopterin aldolase" /EC_number="4.1.2.25" /GO_function="GO:0004150 - dihydroneopterin aldolase activity [Evidence IEA]" /GO_process="GO:0006760 - folic acid-containing compound metabolic process [Evidence IEA]" /calculated_mol_wt=12885 Region 1..117 /region_name="TFold" /note="Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with different functions: dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA), GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl...; cl00263" /db_xref="CDD:469697" Site order(2..12,18..26,100..101,104..112) /site_type="other" /note="homooctamer interface [polypeptide binding]" /db_xref="CDD:238298" Site order(16..18,21,70..73,98,110) /site_type="active" /db_xref="CDD:238298" ORIGIN 1 mdlvfieqle vittigvydw eqqikqklvf diemahdnkp aassddvafa ldyssvsgai 61 ldlvengrfl lvervaeeia tliqtqfsvp wvrvkvskpg avpqartvgv viergvr