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LOCUS WP_010989826 304 aa linear BCT 10-APR-2024 ACCESSION WP_010989826 VERSION WP_010989826.1 KEYWORDS RefSeq. SOURCE Listeria ORGANISM Listeria Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae. REFERENCE 1 (residues 1 to 304) AUTHORS Norager,S., Arent,S., Bjornberg,O., Ottosen,M., Lo Leggio,L., Jensen,K.F. and Larsen,S. TITLE Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function JOURNAL J. Biol. Chem. 278 (31), 28812-28822 (2003) PUBMED 12732650 REFERENCE 2 (residues 1 to 304) AUTHORS Rowland,P., Norager,S., Jensen,K.F. and Larsen,S. TITLE Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster JOURNAL Structure 8 (12), 1227-1238 (2000) PUBMED 11188687 REFERENCE 3 (residues 1 to 304) AUTHORS Rowland,P., Nielsen,F.S., Jensen,K.F. and Larsen,S. TITLE The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis JOURNAL Structure 5 (2), 239-252 (1997) PUBMED 9032071 REFERENCE 4 (residues 1 to 304) AUTHORS Andersen,P.S., Jansen,P.J. and Hammer,K. TITLE Two different dihydroorotate dehydrogenases in Lactococcus lactis JOURNAL J. Bacteriol. 176 (13), 3975-3982 (1994) PUBMED 8021180 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 :: NF005574.0 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK07259 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..304 /organism="Listeria" /db_xref="taxon:1637" Protein 1..304 /product="dihydroorotate dehydrogenase" /EC_number="1.3.1.14" /GO_function="GO:0004152 - dihydroorotate dehydrogenase activity [Evidence IEA]" /GO_process="GO:0006221 - pyrimidine nucleotide biosynthetic process [Evidence IEA]" /calculated_mol_wt=32050 Region 3..297 /region_name="PRK07259" /note="dihydroorotate dehydrogenase" /db_xref="CDD:235982" Site order(29..30,33,45,53,59..60,62,74,218,270,272..273) /site_type="other" /note="heterodimer interface [polypeptide binding]" /db_xref="CDD:240091" Site order(46,69,127,130,165,191..193,217,244,265..266) /site_type="active" /db_xref="CDD:240091" Site order(46,69,127,165,191..192,217,244,265..266) /site_type="other" /note="FMN binding site [chemical binding]" /db_xref="CDD:240091" Site order(63..65,142,170,195..201,204..206,218,221..223, 225..226,253,256..257,297) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:240091" Site order(69,127,129,192..193) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:240091" ORIGIN 1 mnrlaveipg lslknpimpa sgcfgfgqey skyydlnelg aimakavtpe prlgnptprv 61 aetasgmlna iglqnpgleh vlahelpfle qfetpiianv agateddyvq vcarigeska 121 vkaielnisc pnvkhggiaf gtdpevahrl tkavknvasv pvyvklspnv adivsiaqai 181 eaagadgltm intllgmrid lktrkpiian gtgglsgpai kpvairmihq vravsnipii 241 gmggvqtvdd vlefliagad avavgtmnft dpficpklis elpkrmdalg isslqdlkke 301 rtnq