ID B3TMR1_ACTKI Unreviewed; 437 AA. AC B3TMR1; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 66. DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:ACB46491.1}; GN ORFNames=KijD3 {ECO:0000313|EMBL:ACB46491.1}; OS Actinomadura kijaniata. OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales; OC Thermomonosporaceae; Actinomadura. OX NCBI_TaxID=46161 {ECO:0000313|EMBL:ACB46491.1}; RN [1] {ECO:0000313|EMBL:ACB46491.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17985890; DOI=10.1021/ja0744854; RA Zhang H., White-Phillip J.A., Melancon C.E., Kwon H.-J., Yu W.-L., RA Liu H.-W.; RT "Elucidation of the kijanimicin gene cluster: insights into the RT biosynthesis of spirotetronate antibiotics and nitrosugars."; RL J. Am. Chem. Soc. 129:14670-14683(2007). RN [2] {ECO:0007829|PDB:3M9V} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH DTDP. RX PubMed=20334431; DOI=10.1021/bi100318v; RA Bruender N.A., Thoden J.B., Holden H.M.; RT "X-ray structure of kijd3, a key enzyme involved in the biosynthesis of D- RT kijanose."; RL Biochemistry 49:3517-3524(2010). RN [3] {ECO:0007829|PDB:4KCF} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FMN. RX PubMed=23621882; DOI=10.1021/bi400407x; RA Thoden J.B., Branch M.C., Zimmer A.L., Bruender N.A., Holden H.M.; RT "Active site architecture of a sugar N-oxygenase."; RL Biochemistry 52:3191-3193(2013). CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU362125}; CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU301739; ACB46491.1; -; Genomic_DNA. DR PDB; 3M9V; X-ray; 2.05 A; A=1-437. DR PDB; 4KCF; X-ray; 2.10 A; A=1-437. DR PDBsum; 3M9V; -. DR PDBsum; 4KCF; -. DR AlphaFoldDB; B3TMR1; -. DR SMR; B3TMR1; -. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR CDD; cd00567; ACAD; 1. DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom. DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf. DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1. DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR PIRSF; PIRSF016578; HsaA; 2. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3M9V, ECO:0007829|PDB:4KCF}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU362125}; FMN {ECO:0007829|PDB:4KCF}; KW Nucleotide-binding {ECO:0007829|PDB:4KCF}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}. FT DOMAIN 36..107 FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF02771" FT DOMAIN 150..230 FT /note="Acyl-CoA oxidase/dehydrogenase middle" FT /evidence="ECO:0000259|Pfam:PF02770" FT DOMAIN 260..384 FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00441" FT REGION 414..437 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 112 FT /ligand="dTDP" FT /ligand_id="ChEBI:CHEBI:58369" FT /evidence="ECO:0007829|PDB:3M9V" FT BINDING 113 FT /ligand="dTDP" FT /ligand_id="ChEBI:CHEBI:58369" FT /evidence="ECO:0007829|PDB:3M9V" FT BINDING 143 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:4KCF" FT BINDING 171 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:4KCF" FT BINDING 182 FT /ligand="dTDP" FT /ligand_id="ChEBI:CHEBI:58369" FT /evidence="ECO:0007829|PDB:3M9V" FT BINDING 254 FT /ligand="dTDP" FT /ligand_id="ChEBI:CHEBI:58369" FT /evidence="ECO:0007829|PDB:3M9V" FT BINDING 257 FT /ligand="dTDP" FT /ligand_id="ChEBI:CHEBI:58369" FT /evidence="ECO:0007829|PDB:3M9V" FT BINDING 330 FT /ligand="dTDP" FT /ligand_id="ChEBI:CHEBI:58369" FT /evidence="ECO:0007829|PDB:3M9V" FT BINDING 383 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:4KCF" FT BINDING 385 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:4KCF" SQ SEQUENCE 437 AA; 46240 MW; 5ACFDC5E754820DB CRC64; MPPWTARQDS TTGLYAPVTP AGRVLLDRLA AHLPRIRSTA AEHDRDGTFP TDTFDALRKD GLMGATVPAE LGGLGVDRLY DVAVALLAVA RADASTALAL HMQLSRGLTL GYEWRHGDER ARTLAERILR GMVAGDAVVC SGIKDHHTAV TTLRPDGAGG WLLSGRKTLV SMAPVGTHFV INARTDGTDG PPRLASPVVT RDTPGFTVLD NWDGLGMRAS GTVDIVFDDC PIPADHVLMR DPVGARNDAV LAGQTVSSVS VLGVYVGVAQ AAYDTAVAAL ERRPEPPQAA ALTLVAEIDS RLYALRATAG SALTAADALS ADLSGDMDER GRQMMRHFQC AKLAVNRLAP EIVSDCLSLV GGASYTAGHP LARLLRDVQA GRFMQPYAYV DAVDFLSAQA LGIERDNNYM STWAKRSGGN GKSADAAGPR RPTPTSR //