ID S9URX5_9TRYP Unreviewed; 434 AA.
AC S9URX5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=STCU_02079 {ECO:0000313|EMBL:EPY33687.1};
OS Strigomonas culicis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY33687.1, ECO:0000313|Proteomes:UP000015354};
RN [1] {ECO:0000313|EMBL:EPY33687.1, ECO:0000313|Proteomes:UP000015354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23560078;
RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA de Souza W., Schenkman S., de Vasconcelos A.T.;
RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT Family.";
RL PLoS ONE 8:E60209-E60209(2013).
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|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:EPY33687.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ATMH01002079; EPY33687.1; -; Genomic_DNA.
DR AlphaFoldDB; S9URX5; -.
DR EnsemblProtists; EPY33687; EPY33687; STCU_02079.
DR OrthoDB; 952at2759; -.
DR Proteomes; UP000015354; 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; 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 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:UP000015354};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 81..389
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 434 AA; 48436 MW; E45D721D0D4C83A5 CRC64;
MDFKDMPVTT STLSFRGSED SSAPIFHILD LDGKIAKPSD FSGGESSTEL MVSPNGDALY
RPLAEDESSI ISRDVAERMM TSMIAHNTMD KIMLEAQRQG RISFYMSMFG EESAVIGAAA
GLASNDELFM QYRESGLLTY RGYTIPQFVA QCMGNSECDL KGRQMPIHYG SVKLHAQVVS
SPLATQIPHG AGAGYAFRLE NAALLKQAPP GTDIAAMPDA RICATFFGEG ASSEGDFHAG
LNFAATMGSH TLFFVRNNGY AISTPTHSQY VGDGVLGRAI GYGMPSARID GQDAVAVYYT
VRKAREMILR TNKPVFIEAM TYRVSHHSTS DDSTAYRTKD EIGHFADLFS PIERFEKFLL
ERNWWNSEKS AEIMEKTRKE LLSELRRQES IPPWPVSTLC DDVYEVMPED LKKQQKELTE
HYQRFKDKYD QEKL
//
