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Database: UniProt
Entry: F6F111_SPHCR
LinkDB: F6F111_SPHCR
Original site: F6F111_SPHCR 
ID   F6F111_SPHCR            Unreviewed;       399 AA.
AC   F6F111;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Isovaleryl-CoA dehydrogenase {ECO:0000313|EMBL:AEG51227.1};
DE            EC=1.3.8.4 {ECO:0000313|EMBL:AEG51227.1};
GN   ORFNames=Sphch_3637 {ECO:0000313|EMBL:AEG51227.1};
OS   Sphingobium chlorophenolicum L-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG51227.1, ECO:0000313|Proteomes:UP000007150};
RN   [1] {ECO:0000313|EMBL:AEG51227.1, ECO:0000313|Proteomes:UP000007150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-1 {ECO:0000313|EMBL:AEG51227.1,
RC   ECO:0000313|Proteomes:UP000007150};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT   "Complete sequence of chromosome 2 of Sphingobium chlorophenolicum L-1.";
RL   Submitted (MAY-2011) 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; CP002799; AEG51227.1; -; Genomic_DNA.
DR   RefSeq; WP_013849456.1; NC_015594.1.
DR   AlphaFoldDB; F6F111; -.
DR   STRING; 690566.Sphch_3637; -.
DR   KEGG; sch:Sphch_3637; -.
DR   HOGENOM; CLU_018204_9_0_5; -.
DR   Proteomes; UP000007150; Chromosome 2.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008470; F:isovaleryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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   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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007150}.
FT   DOMAIN          6..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..223
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          235..397
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   399 AA;  44370 MW;  D0DE22F80E08920F CRC64;
     MKLDFTPEET AFRDEVRSFL NDALPDDLRR KMINRDHLTK EDTVRWQRIL NARGWAVTHW
     PVEYGGQAWT PAQRYIFQEE MALAHAPEGS PFNVNMIGPV LCKFGTPAQK ERFLSATANI
     DIWWCQGFSE PGAGSDLASL KTMAVRATDA DGDHYVLNGQ KIWTTQAQHA DWMFGLFRTD
     NSGKKQQGIT FLLLDMQTPG ITVRPIETID GEHDANEVFF DDVRVPAENV IGEEGRGWDV
     AKHLLGSERS GIARIGLSKE RLSQLRALET RLARDGTLGE EEQRRLAHKL AEVEVELRAL
     ELTQLRVVAA DAHGGGANAA ASILKVKGTE MQQRMTELVT ELAGPAGLAM PDHDHAPNDP
     DDGWINAAAP FYFTMRKVSI FGGSNEVQKN IIAKTMLGL
//
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