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Database: UniProt
Entry: A0A1H8PTX4_9PROT
LinkDB: A0A1H8PTX4_9PROT
Original site: A0A1H8PTX4_9PROT 
ID   A0A1H8PTX4_9PROT        Unreviewed;       410 AA.
AC   A0A1H8PTX4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN02990966_01916 {ECO:0000313|EMBL:SEO44993.1};
OS   Rhodospirillales bacterium URHD0017.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX   NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEO44993.1, ECO:0000313|Proteomes:UP000198826};
RN   [1] {ECO:0000313|EMBL:SEO44993.1, ECO:0000313|Proteomes:UP000198826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URHD0017 {ECO:0000313|EMBL:SEO44993.1,
RC   ECO:0000313|Proteomes:UP000198826};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FODP01000004; SEO44993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8PTX4; -.
DR   STRING; 1380357.SAMN02990966_01916; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000198826; 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..45
FT                   /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12573"
FT   DOMAIN          83..378
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  45104 MW;  E5C888306CDF2A2F CRC64;
     MSESKALSFH VPAPAVRPGG TPDFSDVKIS SAGEVERPPV DVAPEKIREH AFKIIRVLDR
     NSQAVGPWAG LLSDAELLEG LRHMMTLRAF DARMQMAQRQ GKTSFYMQHM GEEAVSCAFR
     KALEKGDMNF PTYRQAGLLI ADGYPMLDMM NQIYSNELDP MKGRQLPVMY SSREHGFFSI
     SGNLATQYIQ AVGWAMASAI KGDSRIAAGW IGDGSTAESD FHAALVFAST YKAPVVLNIV
     NNQWAISTFQ GIARGGSGTF AARGLGFGIP ALRVDGNDYP AVHAVAKWAV ERARRNLGPT
     LVEYVTYRVG AHSTSDDPSA YRPKTESDGW PLGDPVLRLK NHLILRGVWS EERHKQAEAE
     IMSEVIAVQK EAETHGTLHT GPHPSARDMF EGVFEEMPPH LRRQRQQGGV
//
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