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Database: UniProt
Entry: A0A0M4CRX8_SPHS1
LinkDB: A0A0M4CRX8_SPHS1
Original site: A0A0M4CRX8_SPHS1 
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}.
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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
//
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