ID H5XC03_9PSEU Unreviewed; 409 AA.
AC H5XC03;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Pyruvate dehydrogenase E1 component, alpha subunit {ECO:0000313|EMBL:EHR53807.1};
GN ORFNames=SacmaDRAFT_5693 {ECO:0000313|EMBL:EHR53807.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR53807.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR53807.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR53807.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CM001439; EHR53807.1; -; Genomic_DNA.
DR RefSeq; WP_009157181.1; NZ_CM001439.1.
DR AlphaFoldDB; H5XC03; -.
DR STRING; 882083.SacmaDRAFT_5693; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000004926; 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:EHR53807.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004926}.
FT DOMAIN 74..356
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 45362 MW; 38A89F43C3648F8C CRC64;
MSSPEQWTRP EPGAGPAATA AQPSPEQVIA GLRATAEGGA ELTQLLTPEG ERQPSRFDPY
LADIDDAALR GLYRDMVLVR RADRECNAMQ RQGQLGIWVP LLGQEAAQVG SGRALKPQDM
AFPSYREHGV AYTRGVDFRE LLGIFRCTDH SAWDFREHGF HPYTIVIGNQ VLNATGYAMG
QKFEGKVGNT DPDGKPSGTD EATIVYFGDG ATSQGDVHEG FVWAAVYDAP VVFFCQNNQW
AISEPTERQS RLPLYQRARG YGFPGIRVDG NDVLACLAVT RWALDECRHG NGPVLIEAFT
YRMDAHTTTD DPTRYRLSDE IEVWKHKDPI ERVRVHLART GGADQEFFDQ VQADADAFAA
ELRDYCFNMP DPPPERIFSE VYAEPSAALD AQREEYLAYL SGFADGGEQ
//