ID A0A2P7QNQ7_9SPHN Unreviewed; 384 AA.
AC A0A2P7QNQ7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00018258};
DE EC=1.3.8.4 {ECO:0000256|ARBA:ARBA00012044};
GN ORFNames=C7I55_13350 {ECO:0000313|EMBL:PSJ39584.1};
OS Sphingomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2116704 {ECO:0000313|EMBL:PSJ39584.1, ECO:0000313|Proteomes:UP000241167};
RN [1] {ECO:0000313|EMBL:PSJ39584.1, ECO:0000313|Proteomes:UP000241167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GL-C-18 {ECO:0000313|EMBL:PSJ39584.1,
RC ECO:0000313|Proteomes:UP000241167};
RA Liu L., Li L., Liang L., Zhang X., Wang T.;
RT "The draft genome of Sphingosinicella sp. GL-C-18.";
RL Submitted (MAR-2018) 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}.
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:PSJ39584.1}.
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DR EMBL; PXYI01000004; PSJ39584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7QNQ7; -.
DR OrthoDB; 9780544at2; -.
DR Proteomes; UP000241167; Unassembled WGS sequence.
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; COMPLEX I ASSEMBLY FACTOR ACAD9, 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000241167}.
FT DOMAIN 14..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 232..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-1"
FT BINDING 128..137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 161..163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 243..246
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 339..343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 366..367
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 368..370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
SQ SEQUENCE 384 AA; 41554 MW; A56ADC128C19507C CRC64;
MADFGLDFAL GEMADAIRET TARFAADRIA PLAARIDAED WFPTELWPEM GALGLHGITV
EEEYGGLGLG YLEHVVAQEE VARASASIGL SYGAHSNLCV NQIRRWGNAE QKQKYLPKLI
SGEHIGSLAM SEAGAGSDVV SMKLRAEKRG DRYVLNGTKF WITNAHHADT LVVYAKTGEG
SRGITTFIIE KDMPGFSLGQ KLDKMGMRGS PTGELVFNDC EVPEEQVMGP ENGGVGVLMS
GLDYERTVLA GIQLGIMQAC LDVVLPYIRE RKQFGQAIGS FQLMQAKVAD MYVALISARA
YVYAVARACD AGKTTRFDAA GAILYASENA VRVALEAIQA LGGAGYTKDW PVERYMRDAK
LLDIGAGTNE IRRMLIGREL IGAA
//
