(data stored in SCRATCH zone)

SWISSPROT: Q75BR0_ASHGO

ID   Q75BR0_ASHGO            Unreviewed;       629 AA.
AC   Q75BR0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 93.
DE   SubName: Full=ACR211Wp {ECO:0000313|EMBL:AAS51437.2};
GN   ORFNames=AGOS_ACR211W {ECO:0000313|EMBL:AAS51437.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51437.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51437.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016816; AAS51437.2; -; Genomic_DNA.
DR   RefSeq; NP_983613.2; NM_208966.2.
DR   STRING; 33169.AAS51437; -.
DR   EnsemblFungi; AAS51437; AAS51437; AGOS_ACR211W.
DR   GeneID; 4619745; -.
DR   KEGG; ago:AGOS_ACR211W; -.
DR   HOGENOM; HOG000061334; -.
DR   InParanoid; Q75BR0; -.
DR   KO; K12732; -.
DR   OMA; YLSIGMA; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050177; F:phenylpyruvate decarboxylase activity; IEA:EnsemblFungi.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IEA:EnsemblFungi.
DR   GO; GO:0000950; P:branched-chain amino acid catabolic process to alcohol via Ehrlich pathway; IEA:EnsemblFungi.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0000951; P:methionine catabolic process to 3-methylthiopropanol; IEA:EnsemblFungi.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:EnsemblFungi.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR012110; TPP_enzyme.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q75BR0.
DR   SWISS-2DPAGE; Q75BR0.
KW   Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          32..220
FT                   /note="TPP_enzyme_N"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          251..368
FT                   /note="TPP_enzyme_M"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          439..587
FT                   /note="TPP_enzyme_C"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           508
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   METAL           535
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   METAL           537
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   629 AA;  70237 MW;  3DF8684719234B95 CRC64;
     MKPIGLTGMG LQSAGDSGEE LKSGWMPAEM PLGEYMFRRL MSAGTKTVFG VPGDFNMGLL
     EHMYGEAVCA EGLQWIGTCN ELNAAYAADG YSRYCNKIGC VVTTLGVGEL SALNGVAGAF
     AEHVKVLHIV GVSMRAAQTH PELHGNVHHL VPRLRNSNFE APNHKVYSEM VSGRVSCCCE
     FLEDLETACD QIDHVIREIW RHGKPGYLFV PADMPNMKVS SRNLVQAPTI MLESAVLERT
     NLAACDRIGI EILQHLYQSS TPAILCDGLC DRFGLTGDVR RLVELTGMWN FSTIMGKSIL
     DETQPHYKGV YYGAGSKERN ALLQECDLIL YLGPVKDEVN TWKYTFQFNP QSMIIELHPE
     YVSLTRNGEQ TILNSGHLLP VLRSILAHLN VANLSFNYPT AKKRVPREHQ YAADEPITQG
     MLQHMIPECL NPGDVMVVDT GTFQFSVFDM KFPTDLKCIS QSFYLSIGMA LPAALGVACA
     MREFPRLHLG PKLANEGYTP RLVLCEGDGA AQMTIQELST FIRYELPVEV LLWNNDGYTV
     ERVIKGPTRS YNDIMSWDWT KLLRVFGDFD GTRSESVRVK DFNSLIEHLS SWKSDKKRSK
     IRLMEVILDK MDISATLKEL AKQFQHNAA
//

If you have problems or comments...

PBIL Back to PBIL home page