ID   R5AEN3_9CLOT            Unreviewed;       326 AA.
AC   R5AEN3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) {ECO:0000313|EMBL:CCX41720.1};
GN   ORFNames=BN454_01029 {ECO:0000313|EMBL:CCX41720.1};
OS   Clostridium sp. CAG:1024.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262770 {ECO:0000313|EMBL:CCX41720.1, ECO:0000313|Proteomes:UP000017946};
RN   [1] {ECO:0000313|EMBL:CCX41720.1, ECO:0000313|Proteomes:UP000017946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1024 {ECO:0000313|Proteomes:UP000017946};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:CCX41720.1}.
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DR   EMBL; CAWJ010000136; CCX41720.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5AEN3; -.
DR   STRING; 1262770.BN454_01029; -.
DR   Proteomes; UP000017946; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
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   Pyruvate {ECO:0000313|EMBL:CCX41720.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017946}.
FT   DOMAIN          14..311
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   326 AA;  36116 MW;  EB8F1A860C7B0588 CRC64;
     MEISNEKLIQ MFRYMYLTRR FDEVATQLNK EKRIIGSVHT GVGEEGASVG ITMALSEGDY
     ISPSYRDVGA ILAGGLSTLE VMAMLYAKDC GHTQGRTRLM HLGDLPKHIL PPNPILGASQ
     AIAIGVAYAN QRKKNGSVVV NIMGDGASNE GAVHESMNFA AVYNLPIVFC LVNNHYAWST
     PTRDILKLDI VADRAKAYGF PGYVCNGNDV LETYETVYNA VERARSGQGP SLVEVRAYRW
     SGHSGNDKNV YRTQNEIIRW QQDDCVTKFE GYLTAVGVLS KEEVKSIKDA VEEEIADAIR
     VSEASPYPDP EKLLDPYCML YKEDQE
//