ID A0A1H8Y538_9PROT Unreviewed; 350 AA.
AC A0A1H8Y538;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|ARBA:ARBA00014159, ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU361139};
GN Name=pdhA {ECO:0000256|RuleBase:RU361139};
GN ORFNames=SAMN02990966_06799 {ECO:0000313|EMBL:SEP47196.1};
OS Rhodospirillales bacterium URHD0017.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEP47196.1, ECO:0000313|Proteomes:UP000198826};
RN [1] {ECO:0000313|EMBL:SEP47196.1, ECO:0000313|Proteomes:UP000198826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URHD0017 {ECO:0000313|EMBL:SEP47196.1,
RC ECO:0000313|Proteomes:UP000198826};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|RuleBase:RU361139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|RuleBase:RU361139};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU361139};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870, ECO:0000256|RuleBase:RU361139}.
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DR EMBL; FODP01000023; SEP47196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8Y538; -.
DR STRING; 1380357.SAMN02990966_06799; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000198826; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361139};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU361139};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 42..339
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"
FT COMPBIAS 13..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 38164 MW; D6E1C963071C3202 CRC64;
MAKPATKPKV ESSPAKPTAS TKPPGAGDNS VTADQLKSFY RDMLLIRRFE ERAGQLYGMG
LIGGFCHLYI GQEAVVVGMQ STVIDKDAII TSYRDHGHML ACGMDPKGVM AELTGRASGY
SKGKGGSMHM FSREKSFYGG HGIVGAQVPI GTGLAFAHKY NGNKNVSLTY FGDGSANQGQ
VYEAMNMAAL WKLPVVYIIE NNRYGMGTSV ERASATTELY RHGESFGIPG ERVDGMDVVA
VKAAGEKAVE HARNGEGPYI LEMQTYRYRG HSMSDPAKYR TKEEVDKYRN ERDPIDHVRK
ILLDGKMTDE AALKAVDANI RKIVNDAAEF AQHSPEPDPS ELWTDVLVGA
//
