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Database: UniProt
Entry: E1ZS11_CHLVA
LinkDB: E1ZS11_CHLVA
Original site: E1ZS11_CHLVA 
ID   E1ZS11_CHLVA            Unreviewed;       331 AA.
AC   E1ZS11;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Dehydrogenase E1 component domain-containing protein {ECO:0000259|Pfam:PF00676};
GN   ORFNames=CHLNCDRAFT_141042 {ECO:0000313|EMBL:EFN51425.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN51425.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN51425.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; GL433864; EFN51425.1; -; Genomic_DNA.
DR   RefSeq; XP_005843527.1; XM_005843465.1.
DR   AlphaFoldDB; E1ZS11; -.
DR   SMR; E1ZS11; -.
DR   STRING; 554065.E1ZS11; -.
DR   GeneID; 17350852; -.
DR   KEGG; cvr:CHLNCDRAFT_141042; -.
DR   eggNOG; KOG0225; Eukaryota.
DR   InParanoid; E1ZS11; -.
DR   OMA; SKRDPIM; -.
DR   OrthoDB; 166915at2759; -.
DR   Proteomes; UP000008141; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000008141}.
FT   DOMAIN          77..329
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          303..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  35750 MW;  05B9D5B5BC94E194 CRC64;
     MLAAVSSIAA GAARQAVGGS LACLASTLHR RGFAASATVD GDTLTVEVNP FKTHRIDPPP
     TTVTATKDEL LAYFKQLYRL RRMEISADML YKAKAIRGFC HLYDGQEAVI VGLEAALDHN
     DSIITSYRNH ATHVARGGTV SEVIGELMGR TTGASKGKGG SMHMYRREAN FFGGQGIVGA
     QVPLGTGLAL AHQYNGTGGV AVAMYGDGAA NQGQIFESFN MAALWDLPCI FVCENNHYGM
     GTAEWRAAKS PAFYTRGDYM PGMKCDGMDV LAVKQAFAYA KQHAVANGPI ILEMDTYRYH
     GHSMSDPGST YRTRDEISSI RQQRDPVEHV R
//
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