ID A0A352H5F0_9SPHN Unreviewed; 233 AA. AC A0A352H5F0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 22-FEB-2023, entry version 15. DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:HBC14433.1}; DE Flags: Fragment; GN ORFNames=DC026_01840 {ECO:0000313|EMBL:HBC14433.1}; OS Erythrobacter sp. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter. OX NCBI_TaxID=1042 {ECO:0000313|EMBL:HBC14433.1, ECO:0000313|Proteomes:UP000263926}; RN [1] {ECO:0000313|EMBL:HBC14433.1, ECO:0000313|Proteomes:UP000263926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA9181 {ECO:0000313|EMBL:HBC14433.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974}; CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009347}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HBC14433.1}. 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; DNMX01000023; HBC14433.1; -; Genomic_DNA. DR AlphaFoldDB; A0A352H5F0; -. DR EnsemblBacteria; HBC14433; HBC14433; DC026_01840. DR Proteomes; UP000263926; Unassembled WGS sequence. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1. DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1. DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF12806; Acyl-CoA_dh_C; 1. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1. PE 3: Inferred from homology; FT DOMAIN 15..83 FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00441" FT DOMAIN 100..225 FT /note="Acetyl-CoA dehydrogenase-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF12806" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:HBC14433.1" SQ SEQUENCE 233 AA; 25400 MW; 03A1BA1E8CA73B7E CRC64; LQVDLTHKAK TEEEREQADM LIGLLTPVIK GYGTDKGYEV ATNMQQVFGG HGYIEEWGMS QFVRDARIAQ IYEGTNGVQA MDLCGRKLAQ KGGAAIQAFF KVVGDDIADA KGDDTLAPMA EALEKALGQQ QAATMWFMQN AMQNPNHLGA GAHHYMHIMG IVTLGWMWLR MAKVAQAALA AGGEDKAFYE GKVATARYYM DRYLPDAGAL RRKLEAGSES LMALDEDAFA TAA //