ID A0A142LK46_9PROT Unreviewed; 607 AA.
AC A0A142LK46;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AMS32592.1};
GN ORFNames=AEM42_09760 {ECO:0000313|EMBL:AMS32592.1};
OS Betaproteobacteria bacterium UKL13-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS32592.1, ECO:0000313|Proteomes:UP000075227};
RN [1] {ECO:0000313|Proteomes:UP000075227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Driscoll C.B.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012157; AMS32592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142LK46; -.
DR STRING; 1690485.AEM42_09760; -.
DR KEGG; beb:AEM42_09760; -.
DR PATRIC; fig|1690485.4.peg.2223; -.
DR Proteomes; UP000075227; Chromosome.
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 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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; 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 Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000075227}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 42..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 287..459
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 475..602
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 607 AA; 65357 MW; F5EEC0487B334B81 CRC64;
MSQYTAPLKD ISFVLKHVVG MSDIGKLPGC EEITDDLVDA ILSEAGKFSS EVLAPLNRSG
DQEGAKIING NVTTPKGFKD AYWKYVEGGW SGLEAPVEFG GQGLPHLVAT PVSEMLGSAN
MAFKLCPLLT LGAIEALDQH ASQELKDKFL PNMTAGKWTG TMNLTEPQAG SDLALVRTKA
VPVGDGSYKI TGQKIFITYG DHDYTENIIH LVLARVEGAP EGVKGISLFL VPKVLVNADG
SLGERNDVKC ASIEHKLGIH ASPTCVMIYG EDEKRGGAIG YPIGEINRGL EYMFVMMNAA
RLGVGLEGVS IAERAYQHAL VWARERVQGR PTVPVPASLG TAPKSVPIIY HPDIKRMLMT
MRAYAEACRA MIYWTAKCLD LADRAEDEHT KRFNQALVDL MIPIVKGYST EAGIEVTSLG
VQIHGGMGFI EETGAAQYYR DSRISAIYEG TTGIQANDLV GRKVGREGGQ TALALIAEMQ
KTVSTLEASP DVNLKAIAKT LARGLEDFKR ATEWIAITFK ENQGAVNAGA VHYLMLAGTV
CGGWIMARSG IAAAEMLAKG EGDRDFLKAK LLTVRFFADH ILPFADGYAE AVVNGSSSVL
AMEEAYF
//
