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Database: UniProt
Entry: C5DZH1_ZYGRC
LinkDB: C5DZH1_ZYGRC
Original site: C5DZH1_ZYGRC 
ID   C5DZH1_ZYGRC            Unreviewed;       613 AA.
AC   C5DZH1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=ZYRO0G04378p {ECO:0000313|EMBL:CAR29255.1};
GN   OrderedLocusNames=ZYRO0G04378g {ECO:0000313|EMBL:CAR29255.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR29255.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CU928179; CAR29255.1; -; Genomic_DNA.
DR   RefSeq; XP_002498188.1; XM_002498143.1.
DR   AlphaFoldDB; C5DZH1; -.
DR   SMR; C5DZH1; -.
DR   STRING; 559307.C5DZH1; -.
DR   GeneID; 8205982; -.
DR   KEGG; zro:ZYRO0G04378g; -.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   InParanoid; C5DZH1; -.
DR   Proteomes; UP000008536; Chromosome G.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02005; TPP_PDC_IPDC; 1.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR012110; PDC/IPDC-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047214; TPP_PDC_IPDC.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF3; TRANSAMINATED AMINO ACID DECARBOXYLASE; 1.
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; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          19..123
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          228..365
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          424..583
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         40
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         130
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         181
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         494
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         521
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         523
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         527
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
SQ   SEQUENCE   613 AA;  68883 MW;  24FB552F44BF6606 CRC64;
     MGPVSYESQD IRTKRIPFGE YLFKKLVQSG SKSIFGVPGD YNLPLLEHLY DDSVKDIGCR
     WIACCNELNA AYAADGYSRY TNKLATLITT YGVGELSAIN GVAGSSAENV KVLHIVGVVK
     SDAPECNYHH LIPQLQHSNF IGPNRKICYD MVKDRVACSA EYLEDIETAP EKVDKVITEI
     YKHSKPGYLF VPADFADKLV DTTCLNNEIN LCNSIERTPS EKLDSIVDGV LQWIYQSQTP
     AILADGNVDR FGLISQLNQF IERTQMVNFT TIMGKSIIDE TNPRYQGLYA GKSCTDLVRS
     KFLSCDLILH FGVEKNEVNY CAQGFPYGPQ AKVIEFHQSY IRLFDTLNGD EQLFENVNFV
     DVLTALHQRI DISKLNLQYD KAIFTTYEPS QLNLPEEDTS DVTQIYLQKK FPEILAPGDI
     LVSDTGSFQF GVRDYKLPTQ SKFMAQSTWL SIGMGLPAAL GVGIGMQDYP RIHICDQSKV
     PAGYKPKLVL GVGDGAAQMT VQELTTMLRY HVDINVFVWN NNGYTIERAI MGENSDYNDI
     MPWRWTKLFE AFGDFDGKYS NSSLVKTRQE LDQKIEDINK GGKGIELVEV KLGVMDYPAQ
     LQMMLSNMKN AKK
//
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