ID A0A418ZRT4_9RHOB Unreviewed; 344 AA.
AC A0A418ZRT4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ECO:0000313|EMBL:RJK98857.1};
GN ORFNames=D3P06_15275 {ECO:0000313|EMBL:RJK98857.1};
OS Paracoccus aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=453842 {ECO:0000313|EMBL:RJK98857.1, ECO:0000313|Proteomes:UP000285530};
RN [1] {ECO:0000313|EMBL:RJK98857.1, ECO:0000313|Proteomes:UP000285530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19484 {ECO:0000313|EMBL:RJK98857.1,
RC ECO:0000313|Proteomes:UP000285530};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Laiz L.,
RA Saiz-Jimenez C.;
RT "Paracoccus onubensis nov. sp. a moderate halophilic bacterium isolated
RT from Gruta de las Maravillas (Aracena, Spain).";
RL Submitted (SEP-2018) 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}.
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:RJK98857.1}.
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DR EMBL; QZEV01000105; RJK98857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418ZRT4; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000285530; 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 Reference proteome {ECO:0000313|Proteomes:UP000285530};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 26..322
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 344 AA; 38065 MW; FC2B8C10B6EA7414 CRC64;
MARKPSSQPE TQANVSKDEL LQYYRDMLLI RRFEEKAGQL YGMGLIGGFC HLYIGQEAVV
VGLEACAKEG DKRITSYRDH GHMLACGMEA RGVMAELTGR EGGYSKGKGG SMHMFSREKH
FYGGHGIVAA QVPLGAGLAF ADKYLGNDNV TFTYFGDGAA NQGQVYETYN MAELWDLPVI
FVIENNQYAM GTSVKRSTKS TSLFGRGEAF GIPGEQVDGM DVLAVKAAGE KAVAHCRAGK
GPYILEVMTY RYRGHSMSDP AKYRTREEVQ KMRDERDPIE NIREMLLTGK HATEEDLKAL
DKEIKDIVND SAEFAKESPE PALDQLWTDI YADDLPQGSA EEHA
//
