ID A3U7G3_CROAH Unreviewed; 333 AA.
AC A3U7G3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=CA2559_05455 {ECO:0000313|EMBL:EAP88180.1};
OS Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceibacter.
OX NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP88180.1, ECO:0000313|Proteomes:UP000002297};
RN [1] {ECO:0000313|EMBL:EAP88180.1, ECO:0000313|Proteomes:UP000002297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090
RC {ECO:0000313|Proteomes:UP000002297};
RX PubMed=20639333; DOI=10.1128/JB.00733-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "The complete genome sequence of Croceibacter atlanticus HTCC2559T.";
RL J. Bacteriol. 192:4796-4797(2010).
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; CP002046; EAP88180.1; -; Genomic_DNA.
DR RefSeq; WP_013186855.1; NC_014230.1.
DR AlphaFoldDB; A3U7G3; -.
DR STRING; 216432.CA2559_05455; -.
DR KEGG; cat:CA2559_05455; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_0_10; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000002297; Chromosome.
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:UP000002297};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 15..310
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 333 AA; 37795 MW; 2BD319AB54243BC4 CRC64;
MKKITKATYL KWYEDMLFWR KFEDKLAQVY IQQKVRGFLH LYNGQEAILA GTLHAMDTDK
DRLITAYRNH VQPIGMGVDP KRVMAELYGK GTGTSQGLGG SMHIFSKEHR FYGGHGIVGG
QIPLGAGLAF ADQYHDRDNV TITYFGDGAA RQGSLHETFN LAMLWNLPVV FCVENNGYAM
GTSVARTANH TDIWKLGLGY EMPCGPVDAM NPVKVAEAMS EAIERARTGG GPTFLELKTY
RYRGHSMSDA QKYRTKDEVA EYQKIDPITQ VKEIILDKKY ATEDEVKEID QRVKDLVKEC
EEFAENSDFP EKNVMYDVVY EQEDYPFLSH KPV
//
