ID C7Q7H3_CATAD Unreviewed; 340 AA.
AC C7Q7H3;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) {ECO:0000313|EMBL:ACU72166.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:ACU72166.1};
DE Flags: Precursor;
GN OrderedLocusNames=Caci_3259 {ECO:0000313|EMBL:ACU72166.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU72166.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU72166.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP001700; ACU72166.1; -; Genomic_DNA.
DR AlphaFoldDB; C7Q7H3; -.
DR STRING; 479433.Caci_3259; -.
DR KEGG; cai:Caci_3259; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_0_11; -.
DR InParanoid; C7Q7H3; -.
DR Proteomes; UP000000851; 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; 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 ECO:0000313|EMBL:ACU72166.1}; Pyruvate {ECO:0000313|EMBL:ACU72166.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT DOMAIN 30..319
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 35575 MW; DE0BD6044A356E3C CRC64;
MRSALPGSVA PASASAASPS PDPAALYRTV RLIRRFEERA VELVRAGEVF GGIHPYTGQE
AIAAGTCGAL RADDLITSTH RGHGHVLAKG ADPARMMAEI AGRATGLNRG RGGSMHAADF
GVGILGANAI VGAAAPIATG AAWAARCAGS DRVVVTYFGD GAVSQGVVLE TFNMAALWRA
PVIFVCENNG FATTTRTQDA VAGSITGRAE AFGIPAERVW GMDPEAVYAA TARAVARARS
GEGPTLLECE TYRYDAHHTW EHAARPRYRT PEEVELGRSV DPLDIQGARI DAGVRARIDA
EVDVLLDEAV RFALESPRPD PATALDFLYA DGTTARAGAL
//
