ID A0A3S0ILM3_9FLAO Unreviewed; 332 AA.
AC A0A3S0ILM3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:RTE52933.1};
GN ORFNames=EHW67_14810 {ECO:0000313|EMBL:RTE52933.1};
OS Arenibacter aquaticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=2489054 {ECO:0000313|EMBL:RTE52933.1, ECO:0000313|Proteomes:UP000267585};
RN [1] {ECO:0000313|EMBL:RTE52933.1, ECO:0000313|Proteomes:UP000267585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUO666 {ECO:0000313|EMBL:RTE52933.1,
RC ECO:0000313|Proteomes:UP000267585};
RA Guo J., Sun J.;
RT "Arenibacter aquaticus sp.nov., a marine bacterium isolated from surface
RT seawater in the South China Sea.";
RL Submitted (NOV-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:RTE52933.1}.
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DR EMBL; RQPJ01000014; RTE52933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0ILM3; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000267585; 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 15..311
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 332 AA; 37755 MW; 535FD7F3D36A928A CRC64;
MEKITKEVYL KWYEDMLFWR KFEDKLAAVY IQQKVRGFLH LYNGQEAVLA GALHAMDLKK
DRMITAYRNH VQPIGMGVDP KKVMAELYGK VTGTSKGMGG SMHIFSKEHR FYGGHGIVGG
QIPLGAGLAF ADKYFKRDSV TLCYMGDGAV RQGSLHESFN LAMLWQLPVV FVCENNGYAM
GTSVARTSHS TDIWKLGLGY EMPCGPVDGM DPVTVAKEMS KAIERARSGG GPTFLEMKTY
RYRGHSMSDA QHYRTKEEVE EYKKIDPITQ VLSVIKEKKY ASEDQIKEID ARVKKQVSEC
EKFAEESDYP PVNQLYDMVY DQEDYPFVQH KI
//
