ID A0A2A8HRY7_9SPHN Unreviewed; 435 AA.
AC A0A2A8HRY7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=B2G71_15215 {ECO:0000313|EMBL:PEQ11795.1};
OS Novosphingobium sp. PC22D.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1962403 {ECO:0000313|EMBL:PEQ11795.1, ECO:0000313|Proteomes:UP000220675};
RN [1] {ECO:0000313|EMBL:PEQ11795.1, ECO:0000313|Proteomes:UP000220675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC22D {ECO:0000313|EMBL:PEQ11795.1,
RC ECO:0000313|Proteomes:UP000220675};
RA Peterson S.W.;
RL Submitted (FEB-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:PEQ11795.1}.
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DR EMBL; MWMO01000010; PEQ11795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8HRY7; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000220675; 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:UP000220675};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 16..55
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 93..388
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 435 AA; 48276 MW; EF05D16AD457EE0E CRC64;
MAVNKPGAGK PRGNLPPLEL YVPEPQFRPG DTVDYSGLVI PEAGRQPRPD EACAASETRP
LCDDMIRVLD AEGRAVGPWD PALDPETLRR MLRAMALTRA FDDRMYRGQR QGKTSFYMKC
TGEEATSVAS AFALADDDMV FPSYRQQGIL ITRGFPLVEM VNQIYSNRAD RLKGRQLPIM
YSARDYGFFS ISGNLATQYP QAVGWAMASA IKGDTRIATS FIGEGSSAEG DFHAAMTFAA
VYNAPVVLNV VNNQWAISSF SGFAGGERAT FAARAIGYGI AGLRVDGNDA LAVYAAMQWA
ANRARANAGP TLIEHFTYRA EGHSTSDDPS AYRSAQEREE WPLGDPIMRL KQHLVALGEW
DDERHAAMDL ELAEEVKKAT KEAEKNGILG HGLHHPFHTM FEDVFEELPW HLEEQAEQAI
HERRIKWPSW KEFSK
//
