(data stored in SCRATCH zone)

SWISSPROT: B8BX10_THAPS

ID   B8BX10_THAPS            Unreviewed;       349 AA.
AC   B8BX10;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-DEC-2019, entry version 55.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   ORFNames=THAPSDRAFT_32983 {ECO:0000313|EMBL:EED94123.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae;
OC   Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED94123.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED94123.1,
RC   ECO:0000313|Proteomes:UP000001449};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED94123.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED94123.1,
RC   ECO:0000313|Proteomes:UP000001449};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-
CC         lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residue
CC         acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine +
CC         CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-
CC         COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
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DR   EMBL; CM000640; EED94123.1; -; Genomic_DNA.
DR   RefSeq; XP_002288687.1; XM_002288651.1.
DR   STRING; 35128.Thaps32983; -.
DR   EnsemblProtists; EED94123; EED94123; THAPSDRAFT_32983.
DR   GeneID; 7442486; -.
DR   KEGG; tps:THAPSDRAFT_32983; -.
DR   eggNOG; KOG0524; Eukaryota.
DR   eggNOG; COG0022; LUCA.
DR   HOGENOM; HOG000281450; -.
DR   InParanoid; B8BX10; -.
DR   Proteomes; UP000001449; Chromosome 3.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR027110; PDHB.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR11624; PTHR11624; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   4: Predicted;
DR   PRODOM; B8BX10.
DR   SWISS-2DPAGE; B8BX10.
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN          20..194
FT                   /note="Transket_pyr"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   349 AA;  37156 MW;  6D7B6D4AD10712C8 CRC64;
     MKGITEHIEE LIAKAKAGEI TISEAANLAI HEEMLRDPTT TMQAEDLQAG SSYGIPGMTQ
     QTYGSMRASD EIISEGHFIG KGIGEAMNGY RPIIELMNTN FGIYGVKIAS AGNTYLQSGG
     QFKLPITILG AGGTAPDQAL GAEHSQPLHA YIMGIPGLKI GAAASPEAAY GLTKTMIRDD
     GPCFLIFPVK MMKDTKGTVD LGKCLPLKAA LLHEASAESI NSGKAVTVLT YLHGVKESTN
     TIKELNEKGL DIELIELRSL KPLDMDTIRK SLERTNKLII LDESTRSGGV GASVSSAIAE
     EMFNLLDAPV MRLSMDDAPV PYASAMEKVV VKRGADLVDG VLKMCDGKV
//

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