ID Q128I7_POLSJ Unreviewed; 596 AA.
AC Q128I7;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Acyl-CoA dehydrogenase-like protein {ECO:0000313|EMBL:ABE45055.1};
GN OrderedLocusNames=Bpro_3141 {ECO:0000313|EMBL:ABE45055.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE45055.1, 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}.
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DR EMBL; CP000316; ABE45055.1; -; Genomic_DNA.
DR RefSeq; WP_011484050.1; NC_007948.1.
DR AlphaFoldDB; Q128I7; -.
DR STRING; 296591.Bpro_3141; -.
DR KEGG; pol:Bpro_3141; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_4; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT DOMAIN 2..32
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 38..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 466..591
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 596 AA; 64124 MW; C4D54249482A92A6 CRC64;
MSYVAPLKDM LFDIRHLARI DQVAQIPGFE DAGFETAQAV LEECARFNQD VLSPLNWEGD
KNPSSWKDGV VTTTPGFKQA FKQYAEGGWQ GLQHPAEFGG QGLPKTIGAA CGEMLNSANM
SFALCPLLSD GAIEALLTAG SDDLKAIYLE KLVSGQWTGT MNLTEPQAGS DLAMVRSRAE
PQPDGTYKVF GTKIFITYGE HDMAENIVHL VLARVTGAPE GVKGISLFVV PKFLVNEDGS
LGARNDVHCV SIEHKLGIKA SPTAVLQYGD HGGAVGYIVG EENRGLEYMF IMMNAARYAV
GMQGIAVAER AYQKAVSFAR ERVQSRPVDG SIKASAPIIH HPDVKRMLMT MRAYIEGCRA
MASVAAAAYD ASHHHPDAEV RKQNQAFYEF MVPLVKGYST EMSLEVTSLG VQVHGGMGFI
EETGAAQYMR DAKILTIYEG TTAIQANDLV GRKTSRDGGQ TAKAIAKQIE ATESELIRQG
NADAVAVARR LKAAREALVD VVEFVAGNTK ASPNAVFAGS VPYLMLAGNV VAGWQMARSL
LVAQEQLAQG VDADFMKAKI TTARFYADHL LTKAPGMRDS IVEGADCVTA LALDAF
//
