ID A0A0B5DYF3_9RHOB Unreviewed; 518 AA.
AC A0A0B5DYF3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AJE46185.1};
GN ORFNames=P73_1470 {ECO:0000313|EMBL:AJE46185.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE46185.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE46185.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE46185.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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; CP004393; AJE46185.1; -; Genomic_DNA.
DR RefSeq; WP_043869112.1; NZ_FNNW01000004.1.
DR AlphaFoldDB; A0A0B5DYF3; -.
DR STRING; 1208324.P73_1470; -.
DR KEGG; cid:P73_1470; -.
DR HOGENOM; CLU_018204_12_2_5; -.
DR OrthoDB; 7801364at2; -.
DR Proteomes; UP000031521; 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; 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; 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.
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:UP000031521}.
FT DOMAIN 31..151
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 156..258
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 268..424
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 518 AA; 54549 MW; 1D2449BEA79121DE CRC64;
MIPFAAPVED ILLCLRDVAG ADRLPDWDDE TAEGILRHFA AFAEGVLAPL DETGDAQGCR
LENGRVILPD GFRDAFAQLA AGGWQGLTAP EAFGGMAQNA AIAAGVSEIF SGANHSLQMV
CNLVPGAIST LMKFGSEAQQ TRWIPRLAAG ETLSTMCLTE PGAGSDLSRI RTRALREGEA
WRIEGEKIFI SGGDQDLSRD ILHLVLARTG APGDGVKGLS LFLCPSATGG ARNAVSVTRI
EEKLGLHASP TCQLAFDGAG AELIGQEGGG LAAMFTMMNH ARLDVALQGV AHASRAHQIA
AGYAAERRQG RRADGTGAVL SDHPDVRRML GEQRSLALGA RAMACLTMTE LAMGDAPALV
DFLTPVCKVF CTEAGIRAAD LGIQVLGGYG YLTEYRISQT WRDARITSIY EGANGIHASA
LATRGLRDPA GADAFAARVG ELAAGDAGCL ALRDDWQRMR AGMGDDPLAQ AHEFMALTGE
LLFRAVWCRL AATGGPELLR LSRAVARRPL PVALPRAA
//