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Database: UniProt
Entry: L1KLD7_9ACTN
LinkDB: L1KLD7_9ACTN
Original site: L1KLD7_9ACTN 
ID   L1KLD7_9ACTN            Unreviewed;       408 AA.
AC   L1KLD7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Pyruvate dehydrogenase E1 component, alpha subunit {ECO:0000313|EMBL:EKX61636.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:EKX61636.1};
GN   Name=pdhA_1 {ECO:0000313|EMBL:EKX61636.1};
GN   ORFNames=STRIP9103_04880 {ECO:0000313|EMBL:EKX61636.1};
OS   Streptomyces ipomoeae 91-03.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX61636.1, ECO:0000313|Proteomes:UP000010411};
RN   [1] {ECO:0000313|EMBL:EKX61636.1, ECO:0000313|Proteomes:UP000010411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-03 {ECO:0000313|EMBL:EKX61636.1,
RC   ECO:0000313|Proteomes:UP000010411};
RA   Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL   Submitted (NOV-2012) 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:EKX61636.1}.
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DR   EMBL; AEJC01000576; EKX61636.1; -; Genomic_DNA.
DR   RefSeq; WP_009333720.1; NZ_AEJC01000576.1.
DR   AlphaFoldDB; L1KLD7; -.
DR   PATRIC; fig|698759.3.peg.7653; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000010411; Unassembled WGS sequence.
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:EKX61636.1}; Pyruvate {ECO:0000313|EMBL:EKX61636.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010411}.
FT   DOMAIN          83..350
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  44553 MW;  F83B90B941E497E6 CRC64;
     MTVESTAARK PRRSAAGKTG TTGGKAAGTT GTKRTTAKKT AGAEPELVQL LTPEGKRVKN
     AGTAPYDAYV ADITPDELRG LYRDMVLTRR FDAEATSLQR QGELGLWASL LGQEAAQIGS
     GRATREDDYV FPTYREHGVA WCRGVDPTNL LGMFRGVNNG GWDPNSNNFH LYTIVIGSQA
     LHATGYAMGV AKDGADSAVV AYFGDGASSQ GDVAEAFTFS AVYNAPVVFF CQNNQWAISE
     PTERQTRVPL YQRAQGFGFP GVRVDGNDVL ACLAVTKWAL ERARRGEGPT LVEAYTYRMG
     AHTTSDDPTR YRHDEERVAW EAKDPIARLR SHLESETDTN EGFFAELEAE SEALGRRVRE
     VVRAMPDPDH FAVFENVYAD GHALVDEERA QFAAYQASFA DVDVEEGK
//
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