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Database: UniProt
Entry: A0A1Y5SQ51_9RHOB
LinkDB: A0A1Y5SQ51_9RHOB
Original site: A0A1Y5SQ51_9RHOB 
ID   A0A1Y5SQ51_9RHOB        Unreviewed;       435 AA.
AC   A0A1Y5SQ51;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Putative acyl-CoA dehydrogenase YdbM {ECO:0000313|EMBL:SLN44557.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:SLN44557.1};
GN   Name=ydbM {ECO:0000313|EMBL:SLN44557.1};
GN   ORFNames=PSJ8397_02310 {ECO:0000313|EMBL:SLN44557.1};
OS   Pseudooctadecabacter jejudonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooctadecabacter.
OX   NCBI_TaxID=1391910 {ECO:0000313|EMBL:SLN44557.1, ECO:0000313|Proteomes:UP000193623};
RN   [1] {ECO:0000313|EMBL:SLN44557.1, ECO:0000313|Proteomes:UP000193623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8397 {ECO:0000313|EMBL:SLN44557.1,
RC   ECO:0000313|Proteomes:UP000193623};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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; FWFT01000003; SLN44557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SQ51; -.
DR   OrthoDB; 7316074at2; -.
DR   Proteomes; UP000193623; 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   CDD; cd00567; ACAD; 1.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF41; ACYL-COA DEHYDROGENASE YDBM-RELATED; 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   PIRSF; PIRSF016578; HsaA; 2.
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   ECO:0000313|EMBL:SLN44557.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193623}.
FT   DOMAIN          29..102
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          153..237
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          268..385
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   435 AA;  49117 MW;  C5D5DDB54C119524 CRC64;
     MNFADYYDLS RFRPEHIAML EKINALGPKF AERAPEHDRD ASFPTQNYNE LREHGFLKLV
     IPEEFGGMGF TLGEYATIGA EIGKYCGATA LTFNMHTSSM MWLRFMYEMD NLTPEERTAF
     KRMRELQFAK VVNDGAVFSQ PISEGGANWT SEPIKTNCRR VDGGWVINGF KKFASLAGNC
     DYYSIVCTEH FEGKEPAHED TMDFAVHKDA PGLSIVGEWD PIGMRGTVSR DLILKDVFVS
     EDDMMMPAGV FGKTLSQWPH MMATLTPAYM GVAQSAYNFT VDYLAGTLPD LPPIDRRVYP
     TKRATVGKMF QKLTEMRNLW INAFLEAKPF PSKAEVMRIY AAQYSVMEGV QEMAALAIRT
     CGGQSMLKSL PLERIYRDSR CGALMLPYTT EIMEDYLAMM SVYDMDDIDK VNTETVSARI
     SMWRPAQTAD DIAAE
//
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