ID Q120B8_POLSJ Unreviewed; 381 AA.
AC Q120B8;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Acyl-CoA dehydrogenase-like {ECO:0000313|EMBL:ABE47124.1};
GN OrderedLocusNames=Bpro_5265 {ECO:0000313|EMBL:ABE47124.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OG Plasmid pPol338 {ECO:0000313|Proteomes:UP000001983}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE47124.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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 ---------------------------------------------------------------------------
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; CP000318; ABE47124.1; -; Genomic_DNA.
DR RefSeq; WP_011486103.1; NC_007950.1.
DR AlphaFoldDB; Q120B8; -.
DR KEGG; pol:Bpro_5265; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_3_4; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000001983; Plasmid pPol338.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; IPR006089; Acyl-CoA_DH_CS.
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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:ABE47124.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT DOMAIN 9..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..221
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..381
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 381 AA; 42389 MW; 1D2A60A6E5FFF198 CRC64;
MNDPIYFDEQ HRQFRDNLRR FVEQEVVPQA APWEEQGMVP RAVLRKMGEL GYLGIRYDEQ
YGGSKLDTVY SAILAEELGR STFGGFAVTV MVHTDMASPH LANFGSPEQL QRYLPPIIRG
EKICAVAVTE PDAGSDVAGI RTRAVREGDE WVINGSKMFI TNGVQGDVYF VAAKTDPTAK
GSRGISIFIV EKGTPGFRVG RALNKSGWLC SDTAELVFEN CRIPAANLLG EENKGFYQIM
RNFQNERMVL GAQTMGEAAR AIELTLDYVR ERKAFGATLW DKQAIRQRLA MRASQVAAAR
QLVYHAAWLD AQGRECVKEV SMVKALCGNL VNDVVYDCQQ FHGGFGYMRE AAIERMVRDA
RVQAIGGGAT EVMLEEVAKR L
//
