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Database: UniProt
Entry: C3JHY3_RHOER
LinkDB: C3JHY3_RHOER
Original site: C3JHY3_RHOER 
ID   C3JHY3_RHOER            Unreviewed;       362 AA.
AC   C3JHY3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Pyruvate dehydrogenase E1 component, alpha subunit {ECO:0000313|EMBL:EEN88834.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:EEN88834.1};
GN   Name=pdhA {ECO:0000313|EMBL:EEN88834.1};
GN   ORFNames=RHOER0001_0369 {ECO:0000313|EMBL:EEN88834.1};
OS   Rhodococcus erythropolis SK121.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN88834.1, ECO:0000313|Proteomes:UP000005836};
RN   [1] {ECO:0000313|EMBL:EEN88834.1, ECO:0000313|Proteomes:UP000005836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK121 {ECO:0000313|EMBL:EEN88834.1,
RC   ECO:0000313|Proteomes:UP000005836};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-2009) 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:EEN88834.1}.
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DR   EMBL; ACNO01000014; EEN88834.1; -; Genomic_DNA.
DR   RefSeq; WP_003941309.1; NZ_ACNO01000014.1.
DR   AlphaFoldDB; C3JHY3; -.
DR   Proteomes; UP000005836; 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:EEN88834.1}; Pyruvate {ECO:0000313|EMBL:EEN88834.1}.
FT   DOMAIN          44..310
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   362 AA;  39214 MW;  E5C6AEE2E38DD25E CRC64;
     MVDNLDYPVQ LIQPNGARVC RPEFDRLITD IGPDELLSLY RDLVVSRRID TEAVALQRQG
     EIGLWAPMLG QEAAQVGSAR ALAPGDFAFT SYREHAVAYC RGVPPELLTT MWRGISHSGW
     DPEQFSVTNP AIVVGSQGLH ATGYALGAHL DGAEIATIAY FGDGATSQGD IAEAMGFAAS
     FRVGVVFFCQ NNQWAISEPV SLQSRTPISH RAIGYGIPAI RVDGNDVLAV LAVTRSALNR
     AREGSGPTFI EAITCRMGPH TTSDDPSRYR TDTDMSEWRS RDPLERMRLL LGRRDLLGEN
     ELSTIAAAAD DIAAGLRRAT IALADPPPSA LFDHVYAEAH PLIDAEREEH RAYLGSLEGA
     SS
//
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