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Database: UniProt
Entry: H5X540_9PSEU
LinkDB: H5X540_9PSEU
Original site: H5X540_9PSEU 
ID   H5X540_9PSEU            Unreviewed;       331 AA.
AC   H5X540;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component alpha subunit {ECO:0000313|EMBL:EHR53372.1};
GN   ORFNames=SacmaDRAFT_5211 {ECO:0000313|EMBL:EHR53372.1};
OS   Saccharomonospora marina XMU15.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR53372.1, ECO:0000313|Proteomes:UP000004926};
RN   [1] {ECO:0000313|EMBL:EHR53372.1, ECO:0000313|Proteomes:UP000004926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XMU15 {ECO:0000313|EMBL:EHR53372.1,
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; EHR53372.1; -; Genomic_DNA.
DR   RefSeq; WP_009156748.1; NZ_CM001439.1.
DR   AlphaFoldDB; H5X540; -.
DR   STRING; 882083.SacmaDRAFT_5211; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_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; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 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:EHR53372.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004926}.
FT   DOMAIN          24..320
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   331 AA;  34768 MW;  AE0E749C099B8843 CRC64;
     MTDTLSTAAT PELDENALLA AYRTMRTIRA FEERLHEEFA TGEIPGFVHL YAGEEASATG
     VCSHLDERDS IASTHRGHGH CIAKGVDVLA MMAEIYGRST GSCHGKGGSM HIADLAKGML
     GANGIVGGGP PLICGAALAA KQQRSGGVGV AFFGDGASNQ GTTLEALNLA SVWELPAIFV
     AENNGYAEAT ASTWSVAADN IADRAAGFGM PGVIVDGFDF FAVYEAAGEA ISRAREGGGP
     TLLEIKFTRY FGHFEGDQQS YRASEVAEAR AKLDCLKRFR ARVAETGQLE PARLNAVDAE
     VSALIDTAVR EAKAAPKPTA ADLETDVYVS Y
//
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