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Database: UniProt
Entry: M3CC61_STRMB
LinkDB: M3CC61_STRMB
Original site: M3CC61_STRMB 
ID   M3CC61_STRMB            Unreviewed;       325 AA.
AC   M3CC61;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:EMF01576.1};
GN   ORFNames=H340_05194 {ECO:0000313|EMBL:EMF01576.1};
OS   Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1223523 {ECO:0000313|EMBL:EMF01576.1, ECO:0000313|Proteomes:UP000011740};
RN   [1] {ECO:0000313|EMBL:EMF01576.1, ECO:0000313|Proteomes:UP000011740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40847 {ECO:0000313|EMBL:EMF01576.1,
RC   ECO:0000313|Proteomes:UP000011740};
RX   PubMed=23558536;
RA   Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT   "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT   mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT   Transglutaminase.";
RL   Genome Announc. 1:E0014313-E0014313(2013).
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:EMF01576.1}.
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DR   EMBL; AORZ01000009; EMF01576.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3CC61; -.
DR   STRING; 1223523.H340_05194; -.
DR   PATRIC; fig|1223523.3.peg.1055; -.
DR   eggNOG; COG1071; Bacteria.
DR   Proteomes; UP000011740; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
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:EMF01576.1}.
FT   DOMAIN          13..305
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   325 AA;  34296 MW;  7E7B71CCCB4D46DE CRC64;
     MGAESRAVRL YRTMRLIREF EERCLAMSLT GEIVGGIHPY IGQEAVAAGV CAALTKDDVV
     ASTHRGHGHV LAKGADPKRM LAELLGTTDG LNRGRGGSMH AADVGLGVYG ANGIVGAGAP
     IAAGAAWSFQ QRGEDRVAVA FFGDGALSQG VVLEAFNLAA LWRLPVVFVC ENNGYATSLP
     VGRALAGDPV ERAAAFGLAA RAVDGMDAEA VADAAAQAVE RCRAGGGPAY LECRTYRFHG
     HHSYEEQVAL NYRDDAEVGD WRARDPLRTQ STRVDAATVR TVDAEITALI DEAVEFARAG
     RAPEPHEALD HLYADGTTTR PGVMI
//
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