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
//