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LOCUS WP_000121487 672 aa linear BCT 17-NOV-2023 ACCESSION WP_000121487 VERSION WP_000121487.1 KEYWORDS RefSeq. SOURCE Shigella ORGANISM Shigella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 672) AUTHORS Tu,X., Hubbard,P.A., Kim,J.J. and Schulz,H. TITLE Two distinct proton donors at the active site of Escherichia coli 2,4-dienoyl-CoA reductase are responsible for the formation of different products JOURNAL Biochemistry 47 (4), 1167-1175 (2008) PUBMED 18171025 REFERENCE 2 (residues 1 to 672) AUTHORS Hubbard,P.A., Liang,X., Schulz,H. and Kim,J.J. TITLE The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase JOURNAL J. Biol. Chem. 278 (39), 37553-37560 (2003) PUBMED 12840019 REFERENCE 3 (residues 1 to 672) AUTHORS Liang,X., Thorpe,C. and Schulz,H. TITLE 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid beta-oxidation JOURNAL Arch. Biochem. Biophys. 380 (2), 373-379 (2000) PUBMED 10933894 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 :: NBR011095 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..672 /organism="Shigella" /db_xref="taxon:620" gene 1..672 /gene="fadH" Protein 1..672 /product="NADPH-dependent 2,4-dienoyl-CoA reductase" /EC_number="1.3.1.34" /calculated_mol_wt=72599 Region 6..358 /region_name="DCR_FMN" /note="2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the...; cd02930" /db_xref="CDD:239240" Site order(25,27,59,101,165,167,176,215,253,256,311..312,335, 338,342,354) /site_type="active" /db_xref="CDD:239240" Site order(25,27,59,101,215,311..312) /site_type="other" /note="FMN binding site [chemical binding]" /db_xref="CDD:239240" Site order(165,167,176,253,256) /site_type="other" /note="2,4-decadienoyl-CoA binding site" /db_xref="CDD:239240" Site 167 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:239240" Site order(335,338,342,354) /site_type="other" /note="4Fe-4S cluster binding site [ion binding]" /db_xref="CDD:239240" Region <362..>512 /region_name="GltD" /note="NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; COG0493" /db_xref="CDD:440259" Region 399..>652 /region_name="FadH2" /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism]; COG0446" /db_xref="CDD:440215" ORIGIN 1 msypslfapl dlgfttlknr vlmgsmhtgl eeypdgaerl aafyaerarh gvalivsggi 61 apdltgvgme ggamlndasq iphhrtitea vhqeggkial qilhtgrysy qphlvapsal 121 qapinrfvph eltheeilql iddfarcaql areagydgve vmgsegylin efltlrtnqr 181 sdqwggdyrn rmrfavevvr tvrervgndf iiiyrlsmld lvegggtfae tvelaqaiea 241 agatiintgi gwhearipti atpvprgafs wvtrklkghv slplvttnri ndpqvaddil 301 srgdadivsm arpfladael lskaqsgrad eintcigcnq gcldqifvgk vtsclvnpra 361 chetkmpilp avqkknlavv gagpaglafa inaaarghqv tlfdahseig gqfniakqip 421 gkeefyetlr yyrrmievtg vtlklnhtvt adqlqafdet ilasgivprv ppidgidhpk 481 vlsyldvlrd kapvgnkvai igcggigfdt amylsqpges tsqniarfcn ewgidsslqq 541 agglspqgmq iprsprqivm lqrkaskpgq glgkttgwih rttllsrgvk mipgvsyqki 601 dddglhvvin getqvlavdn vvicagqepn ralaqplids gktvhliggc dvameldarr 661 aiaqgtrlal ei