ID A0A1E3LV88_9SPHN Unreviewed; 427 AA.
AC A0A1E3LV88;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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 ORFNames=BFL28_16905 {ECO:0000313|EMBL:ODP37666.1};
OS Sphingomonas turrisvirgatae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP37666.1, ECO:0000313|Proteomes:UP000094487};
RN [1] {ECO:0000313|EMBL:ODP37666.1, ECO:0000313|Proteomes:UP000094487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCT13 {ECO:0000313|EMBL:ODP37666.1,
RC ECO:0000313|Proteomes:UP000094487};
RA D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
RL Submitted (AUG-2016) 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:ODP37666.1}.
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DR EMBL; MDDS01000025; ODP37666.1; -; Genomic_DNA.
DR RefSeq; WP_069320649.1; NZ_MDDS01000025.1.
DR AlphaFoldDB; A0A1E3LV88; -.
DR STRING; 1888892.BFL28_16905; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000094487; 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:UP000094487};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 10..49
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 88..382
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 427 AA; 46843 MW; 5B2397E20187EF9A CRC64;
MTADAGPNLP PLSLHVPEPK FRPGDTVDFA AVDVPPAGMQ PRPDTAADPR DFHDLAYTLV
RVLDGAGQAV GPWNPRLSPD TLRRMLRDMA LVRAFDERMF RAQRQGKTSF YMKCTGEEAV
AIAAAHALSR DDMCFPSYRQ QGLLIARGYA LERMMNQIYS NSADELHGKQ LPIMYSSKDD
GFFSISGNLA TQYPQAVGWA MASAAKGDTR IAATWCGEGS TAEGDFHSAL TFATVYKAPV
IFNVVNNQWA ISSFSGFAGA EATTFAARAL GYGIAGLRVD GNDALAVYAA TQWAAERART
NQGPTLIEHF TYRAEGHSTS DDPTQYRSAG EPTAWPLGDP IARLKDYLVA IGEWDEDRHA
AQDRELAEQV KAAQKNAEKN GILGHGLHQP LDTLFDGVFE DMPWHLKEQR QMMLDEEAAS
GRPWARK
//
