ID A8G698_PROM2 Unreviewed; 357 AA.
AC A8G698;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=acoA {ECO:0000313|EMBL:ABV51129.1};
GN Synonyms=pdhA {ECO:0000256|RuleBase:RU361139};
GN OrderedLocusNames=P9215_15161 {ECO:0000313|EMBL:ABV51129.1};
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV51129.1, ECO:0000313|Proteomes:UP000002014};
RN [1] {ECO:0000313|EMBL:ABV51129.1, ECO:0000313|Proteomes:UP000002014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV51129.1,
RC ECO:0000313|Proteomes:UP000002014};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000825; ABV51129.1; -; Genomic_DNA.
DR RefSeq; WP_012008176.1; NC_009840.1.
DR AlphaFoldDB; A8G698; -.
DR STRING; 93060.P9215_15161; -.
DR KEGG; pmh:P9215_15161; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_1_3; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000002014; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 42..345
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 357 AA; 40079 MW; 3AC24D2FED1EF7A6 CRC64;
MLTNQNFVKV FFLETHVERI SNLQDIKKAK LDRETGLFLY EDMTLGRRFE DKCAEMYYRG
KMFGFVHLYN GQEAISTGVI GAMKKKHDWF CSTYRDHVHA LSAGVPSFEV MSELFGKATG
CSKGRGGSMH LFSKEHHLLG GYAFIGEGIP VALGAAFSSK YKKEVAGNST SDAVTAAFFG
DGTCNNGQFF ECLNMAQLWK LPIIFVVENN KWAIGMAHDR ATSNPEIWRK AAAFGMQGEE
IDGMDVLAVR GAAQRAIERA RAGEGPTLLE CLTYRYRGHS LADPDELRSE KEKEFWGKRD
PIKKLAQEII NGKFATEEEL KIIEKRIDTE ISESVKNAIE APEPPSQELT KYIWAED
//
