ODPA_GEOSE
ID ODPA_GEOSE Reviewed; 369 AA.
AC P21873;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE EC=1.2.4.1;
GN Name=pdhA;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-35; 54-111 AND
RP 269-331.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=2200674; DOI=10.1111/j.1432-1033.1990.tb19128.x;
RA Hawkins C.F., Borges A., Perham R.N.;
RT "Cloning and sequence analysis of the genes encoding the alpha and beta
RT subunits of the E1 component of the pyruvate dehydrogenase multienzyme
RT complex of Bacillus stearothermophilus.";
RL Eur. J. Biochem. 191:337-346(1990).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; 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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- INTERACTION:
CC P21873; P21874: pdhB; NbExp=3; IntAct=EBI-1040686, EBI-1040700;
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DR EMBL; X53560; CAA37628.1; -; Genomic_DNA.
DR PIR; S10798; DEBSPF.
DR RefSeq; WP_033016215.1; NZ_RCTK01000001.1.
DR PDB; 1W85; X-ray; 2.00 A; A/C/E/G=2-369.
DR PDB; 1W88; X-ray; 2.30 A; A/C/E/G=2-369.
DR PDB; 3DUF; X-ray; 2.50 A; A/C/E/G=1-369.
DR PDB; 3DV0; X-ray; 2.50 A; A/C/E/G=1-369.
DR PDB; 3DVA; X-ray; 2.35 A; A/C/E/G=1-369.
DR PDBsum; 1W85; -.
DR PDBsum; 1W88; -.
DR PDBsum; 3DUF; -.
DR PDBsum; 3DV0; -.
DR PDBsum; 3DVA; -.
DR AlphaFoldDB; P21873; -.
DR SMR; P21873; -.
DR DIP; DIP-29596N; -.
DR IntAct; P21873; 2.
DR GeneID; 58572153; -.
DR SABIO-RK; P21873; -.
DR EvolutionaryTrace; P21873; -.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR11516:SF41; PTHR11516:SF41; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycolysis; Oxidoreductase;
KW Pyruvate; Thiamine pyrophosphate.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2200674"
FT CHAIN 2..369
FT /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT /id="PRO_0000162198"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 44..69
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3DV0"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 147..161
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:1W85"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3DUF"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 312..334
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:1W85"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:1W85"
SQ SEQUENCE 369 AA; 41469 MW; DBF43982C0E1926D CRC64;
MGVKTFQFPF AEQLEKVAEQ FPTFQILNEE GEVVNEEAMP ELSDEQLKEL MRRMVYTRIL
DQRSISLNRQ GRLGFYAPTA GQEASQIASH FALEKEDFIL PGYRDVPQII WHGLPLYQAF
LFSRGHFHGN QIPEGVNVLP PQIIIGAQYI QAAGVALGLK MRGKKAVAIT YTGDGGTSQG
DFYEGINFAG AFKAPAIFVV QNNRFAISTP VEKQTVAKTL AQKAVAAGIP GIQVDGMDPL
AVYAAVKAAR ERAINGEGPT LIETLCFRYG PHTMSGDDPT RYRSKELENE WAKKDPLVRF
RKFLEAKGLW SEEEENNVIE QAKEEIKEAI KKADETPKQK VTDLISIMFE ELPFNLKEQY
EIYKEKESK
