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Database: UniProt
Entry: A0A1M6YR02_9RHOB
LinkDB: A0A1M6YR02_9RHOB
Original site: A0A1M6YR02_9RHOB 
ID   A0A1M6YR02_9RHOB        Unreviewed;       572 AA.
AC   A0A1M6YR02;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN05444414_107148 {ECO:0000313|EMBL:SHL20678.1};
OS   Roseovarius marisflavi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL20678.1, ECO:0000313|Proteomes:UP000184191};
RN   [1] {ECO:0000313|EMBL:SHL20678.1, ECO:0000313|Proteomes:UP000184191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL20678.1,
RC   ECO:0000313|Proteomes:UP000184191};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FRBN01000007; SHL20678.1; -; Genomic_DNA.
DR   RefSeq; WP_073197197.1; NZ_FRBN01000007.1.
DR   AlphaFoldDB; A0A1M6YR02; -.
DR   STRING; 1054996.SAMN05444414_107148; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000184191; Unassembled WGS sequence.
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}.
FT   DOMAIN          3..33
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          81..156
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          161..270
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          281..443
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          456..565
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   572 AA;  61018 MW;  4FFE7980218BEF96 CRC64;
     MPYRAPVEEY QFLFDHVVDL ERVAATDRFA EATPDMTAAI LSEAGRMCQD VLYPLQRPGD
     LHPAHLENGV VRTSPGYGDG YRAIAEGGWV SISASPEHGG MGLPMTVTTA VNEMMSSACL
     SLQLNPLMTQ GQIEALEHHA SDALKDIYLP KLVSGEWSGT MNLTEPQAGS DVGALRSKAE
     DNGDGSYAVT GQKIYISWGD NDFTENVCHL VLARLPDGVP GTKGISLFLV PKFIPDETGT
     PGRANSLKVV SLEHKMGLHG SPTAVMQFDG ATGWLVGKPH DGMRAMFTMM NNARLGVGGQ
     GIGVAEGAYQ HALAYALDRK QGRTPVEGGT GTIIDHADVR RMLSTMKADI FAARSIALTC
     AAATDMQTAT NDAGWGARAA FLTPIVKAFG TETGMAVSEM GVQVHGGMGF IEETGAAQYY
     RDVRVTAIYE GTNGIQAMDL VARKLMDGGE AGFAILDEIE TLAEAARGQL PDLAEPVWQA
     SESLREAMEW MLENSDLNQR FAGASPFLRA FARVLGGHFH LKAALAEGGN GARTRLARFY
     ITRLLPEHAG LLAHATSGAD DLYALSTEDL GA
//
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