ID A0A1H1UAD4_9FLAO Unreviewed; 333 AA.
AC A0A1H1UAD4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN04489797_2191 {ECO:0000313|EMBL:SDS69448.1};
OS Winogradskyella sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS69448.1, ECO:0000313|Proteomes:UP000198963};
RN [1] {ECO:0000313|EMBL:SDS69448.1, ECO:0000313|Proteomes:UP000198963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA_55 {ECO:0000313|EMBL:SDS69448.1,
RC ECO:0000313|Proteomes:UP000198963};
RA Varghese N., Submissions S.;
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; LT629774; SDS69448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1UAD4; -.
DR STRING; 1249933.SAMN04489797_2191; -.
DR Proteomes; UP000198963; Chromosome I.
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 15..311
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 333 AA; 37571 MW; 5D052545D8E975BA CRC64;
MQKITKEVYL KWYEDMLFWR KFEDKLAAVY IQQKVRGFLH LYNGQEAVLA GALHAMDLTK
DKMITAYRNH VQPIGMGVDP KRVMAELFGK ATGTSQGLGG SMHIFSKEHR FYGGHGIVGG
QIPLGAGIAF GDKYHDKDAV TICCFGDGAA RQGSLHETFN LAMLWNLPVV FVCENNGYAM
GTSVARTANH TDVWKLGLGY DMPSGPVDGM NPIKVAEAFD EAIQRARKGG GPTFLEVKTY
RYRGHSMSDA QHYRTKDEVE EYKKIDPITQ VKDIILEKEY ATEAELKAID KDVKKRVAEC
EKFADESPFP DTKVMYDVVY EQEDYPFIDH KIK
//
