ID Q7NAZ8_MYCGA Unreviewed; 359 AA.
AC Q7NAZ8;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU366007};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU366007};
GN Name=acoA {ECO:0000313|EMBL:AAP56835.1};
GN Synonyms=pdhA {ECO:0000256|RuleBase:RU366007};
GN ORFNames=MGA_0165 {ECO:0000313|EMBL:AAP56835.1};
OS Mycoplasmoides gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasma gallisepticum).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=710127 {ECO:0000313|EMBL:AAP56835.1, ECO:0000313|Proteomes:UP000001418};
RN [1] {ECO:0000313|EMBL:AAP56835.1, ECO:0000313|Proteomes:UP000001418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2)
RC {ECO:0000313|Proteomes:UP000001418};
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|RuleBase:RU366007}.
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:RU366007};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU366007};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|RuleBase:RU366007}.
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DR EMBL; AE015450; AAP56835.1; -; Genomic_DNA.
DR RefSeq; WP_011113734.1; NC_004829.2.
DR AlphaFoldDB; Q7NAZ8; -.
DR KEGG; mga:MGA_0165; -.
DR PATRIC; fig|233150.7.peg.543; -.
DR HOGENOM; CLU_029393_1_0_14; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|RuleBase:RU366007};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366007};
KW Pyruvate {ECO:0000256|RuleBase:RU366007, ECO:0000313|EMBL:AAP56835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001418};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 44..320
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 261..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 40578 MW; 7C991607EC43B9B7 CRC64;
MAIIVKNKIP ELLHRVIDNE GRVIDPSYVQ KLSDERVIEA YYYMNLSREL DKKMLTWQRS
GKMLTLAPNI GEEALQLGTS LAMTKKDWLV PAFRSGALML HRGVKPYQLM LYWNGNEKGN
VFDEGVRVIP INITIGAQYS QAAGIGYALK QNKERAAAVT FIGDGGTAEG EFYEAMNLAS
IHKWQTVFCV NNNQYAISTR TNLESAVSDL STKAIAVNMP RVRVDGNDLL ACYDAMLEAI
EYSRSGMGPI FVEFVTYRQG PHTTSDDPSV YRTKQEEEEA KKSDPIARIK KFLTAKGLWD
EAKEKTMFEQ IEAKISEEYD VMLQHIQTTV DDVFDHTYAT LPQNLVEQKA VAKKYFGDK
//
