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Database: UniProt
Entry: A0A0B5DYF3_9RHOB
LinkDB: A0A0B5DYF3_9RHOB
Original site: A0A0B5DYF3_9RHOB 
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
//
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