ID A0A2U2IZV9_9SPHN Unreviewed; 422 AA.
AC A0A2U2IZV9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha {ECO:0000256|RuleBase:RU365014};
DE EC=1.2.4.4 {ECO:0000256|RuleBase:RU365014};
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain {ECO:0000256|RuleBase:RU365014};
GN ORFNames=DF286_01070 {ECO:0000313|EMBL:PWG01616.1};
OS Sphingosinicella humi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Sphingosinicella.
OX NCBI_TaxID=2068657 {ECO:0000313|EMBL:PWG01616.1, ECO:0000313|Proteomes:UP000245916};
RN [1] {ECO:0000313|EMBL:PWG01616.1, ECO:0000313|Proteomes:UP000245916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QZX222 {ECO:0000313|EMBL:PWG01616.1,
RC ECO:0000313|Proteomes:UP000245916};
RA Qiao Z., Wang G.;
RT "Genome of Sphingosinicella humi QZX222.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3). {ECO:0000256|RuleBase:RU365014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 +
CC N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase];
CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC Evidence={ECO:0000256|RuleBase:RU365014};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU365014};
CC -!- SIMILARITY: Belongs to the BCKDHA family.
CC {ECO:0000256|RuleBase:RU365014}.
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:PWG01616.1}.
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DR EMBL; QFFF01000001; PWG01616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2IZV9; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000245916; Unassembled WGS sequence.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR022593; Oxoisoval_DH_suAlpha_N_dom.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF12573; OxoDH_E1alpha_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365014};
KW Reference proteome {ECO:0000313|Proteomes:UP000245916};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 11..51
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 89..382
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 357..384
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 422 AA; 46831 MW; 01F9409ABB4B420B CRC64;
MNRDKERRNR PALALHVPEP DARPGDEIDF SHIPIPAAGA APRPDVSARP DAIRDLAYGL
VRVLDEEGRA VGPWDPRLDA DTLRRMLRDM MMVRVYDDRM YRAQRQGKTS FYMKSTGEEA
IAVAGTHALD REDMTFPTYR QQGILVARDY PLIDMMCQVY SNRGDPLKGR QLPIMYSTKE
YGFFSISGNL GTQYPQAVGW AMGSAIKGDS RIAVGYIGDG ATAEGDFHNA VTFAGVYRAP
VILNIVNNQW AISTFSGIAG AELTTFAARA VGYGIPGLRV DGNDALAVYA ATRWAADRAR
SNLGPTLIEF FTYRVEGHST SDDPSAYRPQ GAGKAWPLGD PIERLKQHLI GLGEWDEERH
AAQHEELNAE VRAAQKEAEK LGTLQSDPWS DIGSMFEDVY EDVPWHLAEQ RDQALAEKEA
KR
//
