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Database: UniProt
Entry: H5XC03_9PSEU
LinkDB: H5XC03_9PSEU
Original site: H5XC03_9PSEU 
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
//
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