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Database: UniProt
Entry: J2DDB5_9SPHN
LinkDB: J2DDB5_9SPHN
Original site: J2DDB5_9SPHN 
ID   J2DDB5_9SPHN            Unreviewed;       326 AA.
AC   J2DDB5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EJK80742.1};
GN   ORFNames=PMI04_03279 {ECO:0000313|EMBL:EJK80742.1};
OS   Sphingobium sp. AP49.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK80742.1};
RN   [1] {ECO:0000313|EMBL:EJK80742.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP49 {ECO:0000313|EMBL:EJK80742.1};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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:EJK80742.1}.
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DR   EMBL; AJVL01000066; EJK80742.1; -; Genomic_DNA.
DR   RefSeq; WP_007712421.1; NZ_CP124576.1.
DR   AlphaFoldDB; J2DDB5; -.
DR   STRING; 1144307.PMI04_03279; -.
DR   PATRIC; fig|1144307.3.peg.3038; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 7328575at2; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
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:SF20; ACYL-COA DEHYDROGENASE FADE28; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT   DOMAIN          5..72
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          192..310
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   326 AA;  34164 MW;  D99E9EC03C36C8CD CRC64;
     MNMTRAEVQD AADKAFGQSD LAPDAAQSWA LIAEMGWLMM GVPEELGGLG LGREAAGVIH
     QGMGKALVPG PVLAQMLTIE ALAAADDLPG RDALIADAMA GEVMTASLAG GLDGADGLTC
     VPDADTASHI LHVTADRVTL VPTEQVAVTY RTGWDKSRRL FDVAIKGPGL TLAQGDAARA
     MADRIEALRL YCLAGDSLGG AEAALAMTVA YLETRQQFDR PLALFQALKH RVADMRTQLS
     AADALFWSRA QQADADVIAL GALKALACAV YRLVAEEAIQ LHGGIGLTME HPCHLFLKRA
     MLNCVLGGDA DHWDEQAGRA ALTAAA
//
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