ID A0A0U2WRL4_9ACTN Unreviewed; 392 AA.
AC A0A0U2WRL4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:ALV34618.1};
GN ORFNames=AS200_23130 {ECO:0000313|EMBL:ALV34618.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV34618.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV34618.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV34618.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP013743; ALV34618.1; -; Genomic_DNA.
DR RefSeq; WP_058924243.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U2WRL4; -.
DR STRING; 1725411.AS200_23130; -.
DR KEGG; scx:AS200_23130; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000068029; Chromosome.
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; 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 Pyruvate {ECO:0000313|EMBL:ALV34618.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 70..351
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43043 MW; DB8980F3E4CAB615 CRC64;
MTVESTAARK PRRSAGTKST AGKRTTASTA PGAEPELVQL LTPEGERVKN AEYDKYVAGI
TPDELRGLYR DMVLTRRFDA EATSLQRQGE LGLWASLLGQ EAAQIGSGRA TREDDYVFPT
YREHGVAWCR GVDPANLLGM FRGVNNGGWD PNSNNFQLYT IVIGSQTLHA TGYAMGVAKD
GADSAVIAYF GDGASSQGDV AESFTFSAVY NAPVVFFCQN NQWAISEPTE KQTRVPLYQR
AQGYGFPGVR VDGNDVLAVL AVTKWALERA RSGEGPTLVE AYTYRMGAHT TSDDPTRYRG
DEERLSWEAK DPILRLRRYL EASNHTDEGF FAELEEESEA LGKRVREAVR AMPDPDHFAI
FENVYADGHA LVDEERAQFA AYQASFADGE GA
//
