(data stored in SCRATCH zone)

SWISSPROT: Q75CQ3_ASHGO

ID   Q75CQ3_ASHGO            Unreviewed;       586 AA.
AC   Q75CQ3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 99.
DE   SubName: Full=ACL134Cp {ECO:0000313|EMBL:AAS51094.1};
GN   ORFNames=AGOS_ACL134C {ECO:0000313|EMBL:AAS51094.1};
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:AAS51094.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51094.1, 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}.
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DR   EMBL; AE016816; AAS51094.1; -; Genomic_DNA.
DR   RefSeq; NP_983270.1; NM_208623.1.
DR   STRING; 33169.AAS51094; -.
DR   EnsemblFungi; AAS51094; AAS51094; AGOS_ACL134C.
DR   GeneID; 4619390; -.
DR   KEGG; ago:AGOS_ACL134C; -.
DR   HOGENOM; HOG000061334; -.
DR   InParanoid; Q75CQ3; -.
DR   KO; K01568; -.
DR   OMA; VGCPSTI; -.
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:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CQ3.
DR   SWISS-2DPAGE; Q75CQ3.
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          27..199
FT                   /note="TPP_enzyme_N"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          223..347
FT                   /note="TPP_enzyme_M"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          419..539
FT                   /note="TPP_enzyme_C"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   METAL           466
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   METAL           493
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   METAL           495
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         50
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         137
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         179
FT                   /note="Substrate; allosteric site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         499
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
SQ   SEQUENCE   586 AA;  64188 MW;  68D42F81B1AB2B18 CRC64;
     MVSGLSKKKT TAKQLSKLTI NTMSEITLGR YLFERLRQIE VQTIFGLPGD FNLSLLDKIY
     EVEGMRWAGN ANELNAAYAA DGYARLKGMS CLITTFGVGE LSALNGIAGS YAEHVGVLHV
     VGVPSISAQA KQLLLHHTLG NGDFTVFHRM SANISGTTAM ISDITSAPAE IDRCIRTCYI
     TQRPVYLGLP ANMVDLKVPA SLLETPIDLN LKPNDPEAEA EVVETVLEMI AAAKNPVILS
     DACASRHDVK AETMKLIDVT QFPAFVTPMG KGSIYEQHPR FGGVYVGTLS SPEVKEAVES
     ADLVLSVGAL LSDFNTGSFS YSYKTKNVVE FHSDHIKIRN ATFPGVQMKY VLRKLVDNVA
     EVIKSYVPVP VPSKPANNEE IDSATPLKQE WLWNQVGKFL REGDVVITET GTSAFGINQT
     HFPNNTYGIS QVLWGSIGFT TGACLGAAFA AEELDPNRRV ILFIGDGSLQ LTVQEISTMV
     RWGLKPYLFV LNNDGYTIER LIHGETAQYN DIQPWQHLNL LPTFGAKDYE AVRVSTTGEW
     DALTQDKAFN ENSKIRMIEV MLPVMDAPSN LVKQAELTAA TNAKQE
//

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