ID A0A2H9TKX8_9FUNG Unreviewed; 420 AA.
AC A0A2H9TKX8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00018258};
DE EC=1.3.8.4 {ECO:0000256|ARBA:ARBA00012044};
GN ORFNames=PSACC_01757 {ECO:0000313|EMBL:PJF18418.1};
OS Paramicrosporidium saccamoebae.
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Paramicrosporidium.
OX NCBI_TaxID=1246581 {ECO:0000313|EMBL:PJF18418.1, ECO:0000313|Proteomes:UP000240830};
RN [1] {ECO:0000313|EMBL:PJF18418.1, ECO:0000313|Proteomes:UP000240830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSL3 {ECO:0000313|EMBL:PJF18418.1,
RC ECO:0000313|Proteomes:UP000240830};
RA Quandt C.A., Beaudet D., Corsaro D., Michel R., Corradi N., James T.;
RT "The genome of Paramicrosporidium saccamoebae is the missing link in
RT understanding Cryptomycota and Microsporidia evolution.";
RL Submitted (OCT-2016) 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:PJF18418.1}.
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DR EMBL; MTSL01000125; PJF18418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9TKX8; -.
DR STRING; 1246581.A0A2H9TKX8; -.
DR Proteomes; UP000240830; 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:UP000240830}.
FT DOMAIN 46..155
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 159..254
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 266..413
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-1"
FT BINDING 160..169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 193..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 277..280
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 305
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 373..377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 400..401
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 402..404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
SQ SEQUENCE 420 AA; 44885 MW; B135B87AA26E3952 CRC64;
MLRLVTTATA TATATAAATI ANAIVQTRRY SSHLNPYSLA HLNDLQSQLV TAVNRFADEQ
VAPRAAKIDE TNTFPRDLWP QLGAIGLLGI TAPESAGGLG MGYFEHVLAM EALSRASASV
ALSYGAHSNL CVNQIVRNGN EEQKERFLPK LISGEHVGAL AMSEAGAGSD VVSMRTSATK
EGDFYVLNGT KMWITNGPDA EVLVVYAKTD PSAGPKGISA FLVEKGMAGF TTSQKLDKLG
MRGSNTCELV FENCRVPKAN LMGKEGDGVY ILMSGLDYER AVLSGGPLGI MQACMDVVLP
YVNTREQFGR PIGQFQLLQG LIADMHTSLS ASRAYVYSVA RACDAGVRDS KECAGAILFA
AENATRVALS AIQCLGGNGY INEYPTGRLL RDAKLYEIGA GTSEIRRMII GREYNKLFSS
//
