ID A0A1V1V1Z0_9CAUL Unreviewed; 415 AA.
AC A0A1V1V1Z0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Name=bkdA1 {ECO:0000313|EMBL:GAW42118.1};
GN ORFNames=SH203_02532 {ECO:0000313|EMBL:GAW42118.1};
OS Brevundimonas sp. SH203.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=345167 {ECO:0000313|EMBL:GAW42118.1, ECO:0000313|Proteomes:UP000195546};
RN [1] {ECO:0000313|EMBL:GAW42118.1, ECO:0000313|Proteomes:UP000195546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH203 {ECO:0000313|EMBL:GAW42118.1,
RC ECO:0000313|Proteomes:UP000195546};
RA Suzuki T., Kikuchi M., Habu N., Konno N.;
RT "Draft Genome Sequence of Brevundimonas sp. SH203, producing Cellouronate
RT (beta-1,4-linked polyglucuronate) lyase.";
RL Submitted (MAR-2017) 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:GAW42118.1}.
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DR EMBL; BDMM01000005; GAW42118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1V1Z0; -.
DR Proteomes; UP000195546; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365014};
KW Reference proteome {ECO:0000313|Proteomes:UP000195546};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 11..50
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 88..381
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45990 MW; 0F98DBD79777A94A CRC64;
MNDKMSKKNS QPLSLHVPEP SGRPGDAPDF SHLKMDPAGV VERPEVGSTP YAMRDLAFRL
IRVLDDEGQA VGPWNPRLDP ETLRRGLKAM ILTRAFDDRM HRAHRQGKTS FYMKCTGEEA
IAVAQGMLLS REDMGFPTYR QQGLLIARGY PLVDMMNQIY SNAADPIKGR QLPIMYSAKD
YGFFTISGNL GTQVPQAVGW AMASAYKGDD KIAISWIGDG ATAEGDFHNA LTFASVYRAP
VILNVVNNQW AISSFMGIAG GLETTFASKA IGYGLPALRV DGNDFLAVWA ATQWAEERAR
SNQGATVIEL FTYRGAPHST SDDPSRYRPG DEHDKWPLGD PLERLRQHLT VIGEWDDERH
TAALKEAVEQ VRAAGKEAEA IGTLGQSRPS VKTMFEEVYA TEDWRLVEQR REVGV
//
