ID E9CXL9_COCPS Unreviewed; 536 AA.
AC E9CXL9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
GN ORFNames=CPSG_02539 {ECO:0000313|EMBL:EFW20696.1};
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN [1] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
RN [2] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; GL636488; EFW20696.1; -; Genomic_DNA.
DR AlphaFoldDB; E9CXL9; -.
DR STRING; 443226.E9CXL9; -.
DR VEuPathDB; FungiDB:CPSG_02539; -.
DR VEuPathDB; FungiDB:D8B26_002975; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR OMA; YIFLPLD; -.
DR Proteomes; UP000002497; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; 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|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW Pyruvate {ECO:0000313|EMBL:EFW20696.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002497};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 209..338
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 410..467
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 536 AA; 59731 MW; 68A44280838C23A7 CRC64;
MTKESQIPVG EYLFRRLHQL GLRHILGVPG DFNLNLLDHI YNVPDMRWVG TCNELNAAYA
ADGYARTRGI PGAVITTYGV GELSAINGIA GAYSEYVPVI HIVGNTSRDM QRNHVKIHHT
LWMDEWDHTT YQKMSEPVRK DSAFLTDPAT APEQIDRVIE TCVKTRLPVY LFVPIDVPDL
MTDSSRLSIP LDLEVRNEGR EAHEDEVVSE IVRAIDQASS PGVLIDVLVQ RHVLVGDAKE
LIEQINAPFY ITPMGKSIVN ESDPRFAGLY GGIVSNPSSA QSQIEGHDII LHVGPFPVSA
NTGGFSTNLP GDKVIKLHPS YCSVGNRVWD GLDFRPVVKK LVQRLNKQPL TRKASSVPKC
QPYKETAHVD DSCVDGLDHK RFWDRLSRYI QPNDFVIAEV GTSQFGSLDL KLPDNCQYFS
QLYYSCIGFT VPALLGVLLA RKETGAEGRV ILLVGDGSLQ MTVQEFGNDH TGGAEGRPSL
WANNARYSIE RSHPRSPCSS ITIFRRNGTT RRCCRSSELR MLPPTWPRPT RSLARF
//
