GenomeNet

Database: UniProt
Entry: A0A101N7A8_9ACTN
LinkDB: A0A101N7A8_9ACTN
Original site: A0A101N7A8_9ACTN 
ID   A0A101N7A8_9ACTN        Unreviewed;       325 AA.
AC   A0A101N7A8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:KUM87855.1};
GN   ORFNames=AQI94_15105 {ECO:0000313|EMBL:KUM87855.1};
OS   Streptomyces pseudovenezuelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM87855.1, ECO:0000313|Proteomes:UP000053039};
RN   [1] {ECO:0000313|EMBL:KUM87855.1, ECO:0000313|Proteomes:UP000053039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM87855.1,
RC   ECO:0000313|Proteomes:UP000053039};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT   strain for the species Streptomyces pseudovenezuelae.";
RL   Submitted (OCT-2015) 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:KUM87855.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMWM01000013; KUM87855.1; -; Genomic_DNA.
DR   RefSeq; WP_031057868.1; NZ_KQ948146.1.
DR   AlphaFoldDB; A0A101N7A8; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000053039; 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:KUM87855.1}.
FT   DOMAIN          12..308
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   325 AA;  34700 MW;  800499FFB102FB89 CRC64;
     MDTGELLALY EQMALIRRTE KAAHDLFLQG LVKGTTHLAA GHEAIAVGAS AALRDDDYVF
     ATYRGHHHAL ARGATPEECL AELMSRATGL CGAKGGSMHL TKAATNMLGS YAIVGAHLPM
     AVGAAWSAKL RGTGQLAVAF FGDGATNIGA FHEALNLAAV WKLPVLFVCE NNLYMEYTPI
     ADVTAVPRPA ADRASAYGIP GEVVDGNDVV SVLETVARLA RRARAGEGPA LLEAETYRHF
     GHSRTDPATY RPAEEVERWL KHDPLDIARG RLVEAGVPEE TVAEADDRAR TVVQRAVEAA
     RNAPSPDPRE AFTDVWADGG AAWRT
//
DBGET integrated database retrieval system