ID A0A098R077_9SPIO Unreviewed; 331 AA.
AC A0A098R077;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=DC28_05150 {ECO:0000313|EMBL:KGE73166.1};
OS Spirochaeta lutea.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73166.1, ECO:0000313|Proteomes:UP000029692};
RN [1] {ECO:0000313|EMBL:KGE73166.1, ECO:0000313|Proteomes:UP000029692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC230 {ECO:0000313|EMBL:KGE73166.1,
RC ECO:0000313|Proteomes:UP000029692};
RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT "De novo Genome Sequence of Spirocheata sp.";
RL Submitted (MAY-2014) 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:KGE73166.1}.
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DR EMBL; JNUP01000045; KGE73166.1; -; Genomic_DNA.
DR RefSeq; WP_037546508.1; NZ_JNUP01000045.1.
DR AlphaFoldDB; A0A098R077; -.
DR STRING; 1480694.DC28_05150; -.
DR eggNOG; COG1071; Bacteria.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000029692; 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:UP000029692};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 18..320
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 331 AA; 37062 MW; 25F341026F94D5EC CRC64;
MSSLKKYDKD FLHGLLKDML LIRRFEEKAG QMYGLKKIGG FCHLYNGQEG VALGSIRALD
LTRDYVLTAY RDHGHAIACG MDPKGIMAEL YGKITGVSRG KGGSMHMFDK ERHMFGGNGI
VGAQIPVATG VAFKSAYEYK LGKTKDMGVT LCYFGDGAIH QGAFHESLNL AAVWKLPIVY
IVENNQFGMG TAVKRVSAVE DFAIKAEGYG LEGRTLDGMN VLSVYEGVKE VVEESRKTGK
AYLLDIKTYR YKGHSMSDPA KYRTKDELEN YKQQDPIVQL KSDLLEAKLL KEEEFKEYDN
QVKKIVQEAV DFADESPEPP LHTMYEDIYA E
//
