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Database: UniProt
Entry: F6AIN5_PSEF1
LinkDB: F6AIN5_PSEF1
Original site: F6AIN5_PSEF1 
ID   F6AIN5_PSEF1            Unreviewed;       393 AA.
AC   F6AIN5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00018258};
DE            EC=1.3.8.4 {ECO:0000256|ARBA:ARBA00012044};
GN   OrderedLocusNames=Psefu_1712 {ECO:0000313|EMBL:AEF21686.1};
OS   Pseudomonas fulva (strain 12-X).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF21686.1, ECO:0000313|Proteomes:UP000000686};
RN   [1] {ECO:0000313|EMBL:AEF21686.1, ECO:0000313|Proteomes:UP000000686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA   Woyke T.;
RT   "Complete sequence of Pseudomonas fulva 12-X.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = 3-methyl-(2E)-butenoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:12276, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57344,
CC         ChEBI:CHEBI:57345, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00023730};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR634183-3, ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC       3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004898}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP002727; AEF21686.1; -; Genomic_DNA.
DR   RefSeq; WP_013790817.1; NC_015556.1.
DR   AlphaFoldDB; F6AIN5; -.
DR   STRING; 743720.Psefu_1712; -.
DR   KEGG; pfv:Psefu_1712; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_1_6; -.
DR   OMA; CFITNSG; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000000686; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:1901565; P:organonitrogen compound catabolic process; IEA:UniProt.
DR   CDD; cd01156; IVD; 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; IPR006089; Acyl-CoA_DH_CS.
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   InterPro; IPR034183; IVD.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; ISOVALERYL-COA DEHYDROGENASE, MITOCHONDRIAL-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.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR634183-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW   ECO:0000313|EMBL:AEF21686.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000686}.
FT   DOMAIN          13..124
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          128..223
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          235..388
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-1"
FT   BINDING         129..138
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT   BINDING         162..164
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT   BINDING         246..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT   BINDING         274
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT   BINDING         285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT   BINDING         347..351
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT   BINDING         374..375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT   BINDING         376..378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
SQ   SEQUENCE   393 AA;  42499 MW;  F36181E16B5436CD CRC64;
     MSTLPGLNFF LGEEIDMLRD AVAGFAAKEI APRAAEADRT DQFPMDLWRK FGDMGLLGLT
     VSEEYGGAGM GYLAHMVAME EISRAAGGIG LSYGAHSNLC VNQINRNGSD EQKRRFLPKL
     ISGEHIGALA MSEPNAGSDV VSMKLRADRK GDHYVLNGSK MWITNGPDCD VLVVYAKTDL
     AAGAKGMTAF ILEKGSKGFS VAQKLDKLGM RGSHTGELVF QDVEVPAENV LGGVGEGARV
     LMSGLDYERA VLSGGPLGLM QAAMDVVVPY VHDRKQFGQS IGEFQLIQGK LADMYTTQQA
     CRAYLYAVGK QLDALGREHV RQVRKDCAGV ILYAAEKATW LAGEAIQILG GNGYINEFSV
     GRLWRDAKLY EIGAGTSEIR RMLIGRELFN ETA
//
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