ID A0A3L7DS94_9GAMM Unreviewed; 410 AA.
AC A0A3L7DS94;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DWB85_17095 {ECO:0000313|EMBL:RLQ20537.1};
OS Seongchinamella sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Seongchinamella.
OX NCBI_TaxID=2283635 {ECO:0000313|EMBL:RLQ20537.1, ECO:0000313|Proteomes:UP000265509};
RN [1] {ECO:0000313|EMBL:RLQ20537.1, ECO:0000313|Proteomes:UP000265509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0301 {ECO:0000313|EMBL:RLQ20537.1,
RC ECO:0000313|Proteomes:UP000265509};
RA Ye M.-Q., Du Z.-J.;
RT "Halioglobus sp. genome submission.";
RL Submitted (JUL-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:RLQ20537.1}.
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DR EMBL; QRAN01000024; RLQ20537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L7DS94; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000265509; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 6..44
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 82..375
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45289 MW; 58137021258B1275 CRC64;
MDPHRQLSLH VPEPSSRPGD QPDFSYLKLL PAGGARRPEP DCPPQDMHDL AFDLVRVLDD
EHAAVGPWAM ELDPSLLLRG LRAMEKTRIF DERMLMAQRQ GKTSIYVQCR GEEAIACGQR
LALGPHDMCF PTYRQQGLLI AQDFPLVDMI CQIYSNARDK LGGRSLPFFY SERDHGFFSI
SGNLGTQFMQ AVGWAMASAI KGDNRIASGW IGDGSTAESD FHAALVYASV YKPPVVMNVV
NNQWAISSFQ GIAGGQAANF ACRGHGFNIP SLRVDGNDFL AVHAASKWAI DRARANLGPT
LIEWVTYRAA AHSTSDDPGK YRPADEYAAW PLGDPIERLK QHLIALGHWS EARHEAMVEE
LRAEVKAAAK QAESFGTLGK GPAPSASEMF NHVYKEMPPH LRRQRQQGGV
//
