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LOCUS WP_001287046 321 aa linear BCT 17-JUL-2023 ACCESSION WP_001287046 VERSION WP_001287046.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 321) AUTHORS Piskol,F., Neubauer,K., Eggers,M., Bode,L.M., Jasper,J., Slusarenko,A., Reijerse,E., Lubitz,W., Jahn,D. and Moser,J. TITLE Two-component carnitine monooxygenase from Escherichia coli: functional characterization, inhibition and mutagenesis of the molecular interface JOURNAL Biosci Rep 42 (9) (2022) PUBMED 36066069 REFERENCE 2 (residues 1 to 321) AUTHORS Kalnins,G., Sevostjanovs,E., Hartmane,D., Grinberga,S. and Tars,K. TITLE CntA oxygenase substrate profile comparison and oxygen dependency of TMA production in Providencia rettgeri JOURNAL J Basic Microbiol 58 (1), 52-59 (2018) PUBMED 29110324 REFERENCE 3 (residues 1 to 321) AUTHORS Koeth,R.A., Levison,B.S., Culley,M.K., Buffa,J.A., Wang,Z., Gregory,J.C., Org,E., Wu,Y., Li,L., Smith,J.D., Tang,W.H.W., DiDonato,J.A., Lusis,A.J. and Hazen,S.L. TITLE gamma-Butyrobetaine is a proatherogenic intermediate in gut microbial metabolism of L-carnitine to TMAO JOURNAL Cell Metab 20 (5), 799-812 (2014) PUBMED 25440057 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 :: NBR007840 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..321 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..321 /gene="yeaX" Protein 1..321 /product="carnitine monooxygenase reductase subunit YeaX" /EC_number="1.14.13.239" /calculated_mol_wt=35498 Region 12..226 /region_name="PDR_like" /note="Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur...; cd06185" /db_xref="CDD:99782" Site order(56..57,59,73..75,81,83..84,125,225) /site_type="other" /note="FMN-binding pocket [chemical binding]" /db_xref="CDD:99782" Site order(56,58..59) /site_type="active" /note="flavin binding motif [active]" /db_xref="CDD:99782" Site order(81,84,87,94) /site_type="other" /note="phosphate binding motif [ion binding]" /db_xref="CDD:99782" Site order(117,121..124,126) /site_type="other" /note="beta-alpha-beta structure motif" /db_xref="CDD:99782" Site order(122..123,146..148,198..199) /site_type="other" /note="NAD binding pocket [chemical binding]" /db_xref="CDD:99782" Region 236..321 /region_name="Fdx" /note="Ferredoxin [Energy production and conversion]; COG0633" /db_xref="CDD:440398" ORIGIN 1 msdyqmfevq vsqveplteq vkrftpvatd gkplpaftgg shiivqmsdg dnqysnaysl 61 lssphntssy qiavrleens rggsrflhqq vkvgdrltis tpnnlfalip sarkhlfiag 121 gigippflsh maelqhsdvd wqlhycsrnp escafrdelv qhpqaekvhl hqsstgtrle 181 larlladiep gthvytcgpe alieavrsea arldiaadtl hfeqfaiedk tgdaftlvla 241 rsgkefvvpe emtilqvien nkaakveclc regvcgtcet ailegeadhr dqyfsdeera 301 sqqsmliccs rakgkrlvld l