ID A4X144_SALTO Unreviewed; 391 AA.
AC A4X144;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) {ECO:0000313|EMBL:ABP52594.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:ABP52594.1};
GN OrderedLocusNames=Strop_0109 {ECO:0000313|EMBL:ABP52594.1};
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS 105044 / CNB-440).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP52594.1, ECO:0000313|Proteomes:UP000000235};
RN [1] {ECO:0000313|Proteomes:UP000000235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC {ECO:0000313|Proteomes:UP000000235};
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP000667; ABP52594.1; -; Genomic_DNA.
DR RefSeq; WP_011904031.1; NC_009380.1.
DR AlphaFoldDB; A4X144; -.
DR STRING; 369723.Strop_0109; -.
DR KEGG; stp:Strop_0109; -.
DR PATRIC; fig|369723.5.peg.109; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_11; -.
DR Proteomes; UP000000235; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABP52594.1}; Pyruvate {ECO:0000313|EMBL:ABP52594.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000235}.
FT DOMAIN 67..355
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43469 MW; BE4C76001CE55093 CRC64;
MAKGDPGVNT RGRRAVPRSR KGATGDPELV QLLTPEGERI ESVTGPDGTE YRVDFTDEEY
RGFYRDLVLV RKLDAEATAL QRQGELGLWA SLLGQEAAQV GSGRALRTQD MAFPTYREHG
VLYCRGIDPI MPLGLFRGVD QGGWDPNEFK FNMYTIVIGA QALHATGYAM GITMDGKTGT
DEGEAVIAYF GDGATSQGDV NEAFVWASVF NAPMVFFCQN NQYAISEPLE RQTRIPLYRR
AAGFGFPGLR VDGNDVLATY AVTRHALDNA RHGQGPSLIE AYTYRMGAHT TSDDPTRYRI
ASEVEAWQAK DPIARMKTFL EKQKIADDGF FAEVDEQAKR ESVHLRERVL EMPNPEPSSM
FDHVYPNGSP LVDQQRAQFN QYLESFEGSA H
//
