ID A0A0M4CRX8_SPHS1 Unreviewed; 431 AA.
AC A0A0M4CRX8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ALC10758.1};
GN ORFNames=LH20_02215 {ECO:0000313|EMBL:ALC10758.1};
OS Sphingopyxis sp. (strain 113P3).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC10758.1, ECO:0000313|Proteomes:UP000061305};
RN [1] {ECO:0000313|EMBL:ALC10758.1, ECO:0000313|Proteomes:UP000061305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=113P3 {ECO:0000313|EMBL:ALC10758.1,
RC ECO:0000313|Proteomes:UP000061305};
RX PubMed=26472829;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT Sphingopyxis sp. 113P3 (NBRC 111507).";
RL Genome Announc. 3:e01169-15(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009452; ALC10758.1; -; Genomic_DNA.
DR RefSeq; WP_053552816.1; NZ_CP009452.1.
DR AlphaFoldDB; A0A0M4CRX8; -.
DR STRING; 292913.LH20_02215; -.
DR KEGG; sphp:LH20_02215; -.
DR PATRIC; fig|292913.6.peg.443; -.
DR OrthoDB; 9780544at2; -.
DR Proteomes; UP000061305; 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 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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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:UP000061305}.
FT DOMAIN 152..251
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 264..415
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 431 AA; 49329 MW; 91E3E430FCFF1311 CRC64;
MDFAVPADLK AYLDELDAFI EAEIKPLEEA DDNIRFFDHR REHSRTDWDN QGLPRHEWEE
LLNEAKRRAD AAGHWRFSAP KKYGGKDGSN LWMAVIREHF AAKGLGLHND LQNEHSIVGN
FPFVEMFEQF ATSEEQKQEF ILGGFEGKRR TAFGLTEPDH GSDATHMETR AVREVRDGEE
GWRINGEKMW TTGMHVATHC ATFCRTSGED GDAKGITCLL VPNPSPGLVI EEYLWTFNMP
TDHPRVSFTD VWVPDSARLG PVDGGLSIAQ SFVHQNRIRQ AASSLGAAVY CIEESVRYAR
ERKPFGEALA KNQAIQFPLV ELATQAEMLR LLIRKTAWEM DNMPHKEVEH RLSDKVSMCN
YWANRLCCQA ADRAMQVHGG IGYSRHKPFE HIYRHHRRYR ITEGAEEIQM RKVAAYLFGY
LGPRRETLGK I
//