(data stored in SCRATCH zone)

SWISSPROT: C5DC94_LACTC

ID   C5DC94_LACTC            Unreviewed;       593 AA.
AC   C5DC94;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 51.
DE   SubName: Full=KLTH0B01188p {ECO:0000313|EMBL:CAR21405.1};
GN   OrderedLocusNames=KLTH0B01188g {ECO:0000313|EMBL:CAR21405.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21405.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21405.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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; CU928166; CAR21405.1; -; Genomic_DNA.
DR   RefSeq; XP_002551843.1; XM_002551797.1.
DR   STRING; 381046.XP_002551843.1; -.
DR   EnsemblFungi; CAR21405; CAR21405; KLTH0B01188g.
DR   GeneID; 8290669; -.
DR   KEGG; lth:KLTH0B01188g; -.
DR   HOGENOM; HOG000061334; -.
DR   InParanoid; C5DC94; -.
DR   KO; K01568; -.
DR   OMA; VGCPSTI; -.
DR   OrthoDB; 560466at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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; 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; C5DC94.
DR   SWISS-2DPAGE; C5DC94.
KW   Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          34..206
FT                   /note="TPP_enzyme_N"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          230..353
FT                   /note="TPP_enzyme_M"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          425..534
FT                   /note="TPP_enzyme_C"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   METAL           500
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   METAL           502
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         57
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         144
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         186
FT                   /note="Substrate; allosteric site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         506
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
SQ   SEQUENCE   593 AA;  65284 MW;  DB95803C643A7F43 CRC64;
     MSDLILYCDF YKTRNLNSNR VSQNKPEITM SEITLGRYVF ERLKQVDVTT VFGLPGDFNL
     RLLDEIYEVE GMRWAGNCNE LNASYAADAY ARIKGMSCLI TTFGVGELSA LNGIAGSYAE
     HVGVLHIVGV PSVSAQAKQL LLHHTLGNGD FTVFHRMSAN ISETTAMITD LATAPSEIDR
     CIRTTYIRQR PVYLGLPSNF VDQMVPASLL DTPIDLALKP NDQQAEEEVI STLLEMIKDA
     KNPVILADAC ASRHDVKAET KKLIDITQFP SFVTPMGKGS IDEKHPRFGG VYVGTLSSPA
     VKEAVESADL VLSVGALLSD FNTGSFSYSY KTKNVVEFHS DHIKIRNATF PGVQMKFVLQ
     SLLNKVGAVV KDYKPVPVPE LPAPNAAVDP STPLKQQWLW NQVGQFLQEG DIVLTETGTS
     AFGINQTHFP NNTYGISQVL WGSIGYATGA CLGAVMAAEE LDKSKRVILF TGEGSLQLTA
     QEISTMVRWN LKPYLFVLNN KGYTIEKLIH GPTAEYNEIQ NWNHLDLLPT FGAKDYEAIR
     VSTTGEWNKL AEDKDFNKNS KIRLIELMLP VMDAPESLVK QAQLTAATNA KSA
//

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