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Database: UniProt
Entry: H6R2P8_NOCCG
LinkDB: H6R2P8_NOCCG
Original site: H6R2P8_NOCCG 
ID   H6R2P8_NOCCG            Unreviewed;       372 AA.
AC   H6R2P8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Pyruvate dehydrogenase E1 COMPONENT (ALPHA SUBUNIT) PDHA (PYRUVATE DECARBOXYLASE) (PYRUVATE DEHYDROGENASE) (PYRUVIC DEHYDROGENASE) {ECO:0000313|EMBL:CCF61898.1};
GN   Name=pdhA {ECO:0000313|EMBL:CCF61898.1};
GN   OrderedLocusNames=NOCYR_1090 {ECO:0000313|EMBL:CCF61898.1};
OS   Nocardia cyriacigeorgica (strain GUH-2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF61898.1, ECO:0000313|Proteomes:UP000008190};
RN   [1] {ECO:0000313|EMBL:CCF61898.1, ECO:0000313|Proteomes:UP000008190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUH-2 {ECO:0000313|EMBL:CCF61898.1,
RC   ECO:0000313|Proteomes:UP000008190};
RX   PubMed=22461543; DOI=10.1128/JB.00161-12;
RA   Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA   Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA   Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA   Richard Y., Cournoyer B., Blaha D.;
RT   "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT   cyriacigeorgica GUH-2.";
RL   J. Bacteriol. 194:2098-2099(2012).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FO082843; CCF61898.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6R2P8; -.
DR   STRING; 1127134.NOCYR_1090; -.
DR   KEGG; ncy:NOCYR_1090; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_1_0_11; -.
DR   Proteomes; UP000008190; 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:CCF61898.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008190}.
FT   DOMAIN          51..318
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   372 AA;  40796 MW;  9535B4718ABBCC23 CRC64;
     MQEAVKEMLG KPSYPVQLIQ PDGRRVLDRE HAAVVADIGP DKLRDLYEDL VVTRRIDTEA
     TALQRQGQLG LWAPLLGQEA AQVGSARALH PDDYVFCSYR EAAVAYCRGV DPAQLTRMWR
     GVAHSCWDPD VIKTTNPAIV VGAQGLHATG YAYAAHLEGA DIATIAYFGD GATSQGDIAE
     ALGFAASWSA PVVFFCQNNH WAISEPVRLQ SATPIAQRAL GYGIPSVQVD GNDVLAVLAV
     TRQALARAHA GGGPSFIEAI TYRMGPHTTA DDPTRYRSDA ETEEWKKRDP IDRVHRLLGR
     ENLLDEQFEQ RVRDRADEIA SVVRTATITM PDPDPMELFE HVYSTEHPLI AEQRRAYAQH
     LAAHASTEGV PS
//
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