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PDC1_CANGA
ID   PDC1_CANGA              Reviewed;         564 AA.
AC   Q6FJA3; Q8J134;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Pyruvate decarboxylase;
DE            EC=4.1.1.1 {ECO:0000269|PubMed:15625313};
GN   Name=PDC1; Synonyms=PDC; OrderedLocusNames=CAGL0M07920g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=JCM 3699 / NBRC 0005;
RX   PubMed=15625313; DOI=10.1093/jb/mvh141;
RA   Wang Q., He P., Lu D., Shen A., Jiang N.;
RT   "Purification, characterization, cloning and expression of pyruvate
RT   decarboxylase from Torulopsis glabrata IFO005.";
RL   J. Biochem. 136:447-455(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC         Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC         Evidence={ECO:0000269|PubMed:15625313};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526; Evidence={ECO:0000250|UniProtKB:P06169};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P06169};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P06169};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000250|UniProtKB:P06169};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AF545432; AAN77243.1; -; Genomic_DNA.
DR   EMBL; CR380959; CAG62667.1; -; Genomic_DNA.
DR   RefSeq; XP_449691.1; XM_449691.1.
DR   AlphaFoldDB; Q6FJA3; -.
DR   SMR; Q6FJA3; -.
DR   STRING; 5478.XP_449691.1; -.
DR   PRIDE; Q6FJA3; -.
DR   EnsemblFungi; CAG62667; CAG62667; CAGL0M07920g.
DR   GeneID; 2891742; -.
DR   KEGG; cgr:CAGL0M07920g; -.
DR   CGD; CAL0137069; PDC.
DR   VEuPathDB; FungiDB:CAGL0M07920g; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   InParanoid; Q6FJA3; -.
DR   OMA; EQRYNDI; -.
DR   BRENDA; 4.1.1.1; 1113.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IDA:CGD.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IDA:CGD.
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   PANTHER; PTHR43452; PTHR43452; 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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..564
FT                   /note="Pyruvate decarboxylase"
FT                   /id="PRO_0000090762"
FT   BINDING         28
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         115
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         390
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         413..415
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         445..446
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         471..476
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         477
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   CONFLICT        559
FT                   /note="I -> T (in Ref. 1; AAN77243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        564
FT                   /note="Missing (in Ref. 1; AAN77243)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  61906 MW;  A0F08DE36A96D2AA CRC64;
     MSEITLGRYL FERLNQVDVK TIFGLPGDFN LSLLDKIYEV EGMRWAGNAN ELNAAYAADG
     YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSISSQAKQ LLLHHTLGNG
     DFTVFHRMSA NISETTAMVT DIATAPAEID RCIRTTYITQ RPVYLGLPAN LVDLKVPAKL
     LETPIDLSLK PNDPEAETEV VDTVLELIKA AKNPVILADA CASRHDVKAE TKKLIDATQF
     PSFVTPMGKG SIDEQHPRFG GVYVGTLSRP EVKEAVESAD LILSVGALLS DFNTGSFSYS
     YKTKNIVEFH SDYIKIRNAT FPGVQMKFAL QKLLNAVPEA IKGYKPVPVP ARVPENKSCD
     PATPLKQEWM WNQVSKFLQE GDVVITETGT SAFGINQTPF PNNAYGISQV LWGSIGFTTG
     ACLGAAFAAE EIDPKKRVIL FIGDGSLQLT VQEISTMIRW GLKPYLFVLN NDGYTIERLI
     HGEKAGYNDI QNWDHLALLP TFGAKDYENH RVATTGEWDK LTQDKEFNKN SKIRMIEVML
     PVMDAPTSLI EQAKLTASIN AKQE
 
 
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