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Database: UniProt
Entry: A0A178AGR1_9PLEO
LinkDB: A0A178AGR1_9PLEO
Original site: A0A178AGR1_9PLEO 
ID   A0A178AGR1_9PLEO        Unreviewed;       402 AA.
AC   A0A178AGR1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) {ECO:0000256|ARBA:ARBA00012277};
DE            EC=1.2.4.4 {ECO:0000256|ARBA:ARBA00012277};
GN   ORFNames=IQ06DRAFT_351332 {ECO:0000313|EMBL:OAK96733.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK96733.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK96733.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK96733.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 +
CC         N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase];
CC         Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036680};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13458;
CC         Evidence={ECO:0000256|ARBA:ARBA00036680};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; KV441719; OAK96733.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AGR1; -.
DR   STRING; 765868.A0A178AGR1; -.
DR   InParanoid; A0A178AGR1; -.
DR   OrthoDB; 364at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT   DOMAIN          80..256
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   402 AA;  44050 MW;  7FD285084488C89C CRC64;
     MASKTPSIRA LSRSIRPRAQ LRPRCQHQAQ CKQYSAAAAG ARLNGSVEYD TTPILNHTSK
     ASLANPELPP EIRKGQTKRI NLYTAVNEAM RHALQADERV LVFGEDIQFG GVFRCTMNLA
     ADFGTERVFN TPLSEQGLIG FAVGAAAEGM RPIAEIQFAD YVFPAFDQIH NEVAKYRYRS
     GSTGVNCGGL VIRMPSGSVG HGALYHTQSP EALFTHTPGL RVVIPRSPVQ AKGLLLSAIR
     CNDPVIFMEP KILYRAAVEQ VPVDAYHLPL DKAEVLKTGK DVTIISYGTP LYTCSAAITA
     AEKDFGCSVE LIDLRTIYPW DRETVLNSVK KTGRAIVVHE SMMNAGVGAE VAATIQEKAF
     LRLEAPVKRV AGWATHTGLM FEQFIIPDVT RVYDAIKQTI DY
//
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