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Database: UniProt
Entry: A0A0J5T7U6_9RHOB
LinkDB: A0A0J5T7U6_9RHOB
Original site: A0A0J5T7U6_9RHOB 
ID   A0A0J5T7U6_9RHOB        Unreviewed;       254 AA.
AC   A0A0J5T7U6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:KMK66027.1};
GN   ORFNames=IMCC21224_11873 {ECO:0000313|EMBL:KMK66027.1};
OS   Puniceibacterium sp. IMCC21224.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Puniceibacterium.
OX   NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK66027.1, ECO:0000313|Proteomes:UP000036046};
RN   [1] {ECO:0000313|EMBL:KMK66027.1, ECO:0000313|Proteomes:UP000036046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK66027.1,
RC   ECO:0000313|Proteomes:UP000036046};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21224 belonging to the
RT   Alphaproteobacteria.";
RL   Submitted (MAY-2015) 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|RuleBase:RU362125}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMK66027.1}.
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DR   EMBL; LDPY01000001; KMK66027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J5T7U6; -.
DR   STRING; 1618204.IMCC21224_11873; -.
DR   PATRIC; fig|1618204.4.peg.889; -.
DR   Proteomes; UP000036046; 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; 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; 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   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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036046}.
FT   DOMAIN          8..93
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          106..253
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   254 AA;  27810 MW;  AC88BC31C23644DB CRC64;
     MTQTWMTDEQ GIKTRALRDG NSYRLSGQKT FITNGQHANL IVVAAKTDPE QGSKGISLVV
     VETENAAGST RGRNLGKIGC HAADTSELFF DHVEVAPENI LGGGPGQGVY QMMKQLPQER
     LIIGCGAVGA MEGAVERTIT YCKEREAFGG PLTQFQNTRF KLAECQTRTV VARTFLGQCI
     TEHLQGALTV EKAAMAKYWL TDTQGDVLDD CLQLHGGYGY MQEYAVAEMW ADARVQRIYG
     GTNEIMKELS ARAF
//
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