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Protein

Pyruvate decarboxylase

Gene

PDC1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A 2-oxo acid = an aldehyde + CO2.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281SubstrateBy similarity
Binding sitei115 – 1151SubstrateBy similarity
Metal bindingi444 – 4441MagnesiumBy similarity
Metal bindingi471 – 4711MagnesiumBy similarity
Metal bindingi473 – 4731Magnesium; via carbonyl oxygenBy similarity
Binding sitei477 – 4771SubstrateBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BRENDAi4.1.1.1. 2825.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate decarboxylase (EC:4.1.1.1)
Gene namesi
Name:PDC1
Ordered Locus Names:KLLA0E16357g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
Proteomesi
  • UP000000598 Componenti: Chromosome E

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 563563Pyruvate decarboxylasePRO_0000090765Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi284590.XP_454684.1.

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi6 – 1611Combined sources
Beta strandi21 – 244Combined sources
Turni28 – 303Combined sources
Helixi31 – 355Combined sources
Helixi36 – 394Combined sources
Helixi51 – 6515Combined sources
Beta strandi68 – 736Combined sources
Helixi76 – 805Combined sources
Helixi82 – 909Combined sources
Beta strandi95 – 1017Combined sources
Helixi104 – 1085Combined sources
Helixi109 – 1146Combined sources
Beta strandi118 – 1203Combined sources
Helixi124 – 1307Combined sources
Beta strandi134 – 1385Combined sources
Turni142 – 1443Combined sources
Helixi145 – 15915Combined sources
Beta strandi163 – 1686Combined sources
Helixi169 – 1724Combined sources
Beta strandi174 – 1774Combined sources
Helixi178 – 1825Combined sources
Helixi194 – 21017Combined sources
Beta strandi212 – 2187Combined sources
Turni220 – 2267Combined sources
Helixi228 – 23811Combined sources
Beta strandi242 – 2443Combined sources
Turni246 – 2505Combined sources
Beta strandi259 – 2624Combined sources
Helixi265 – 2673Combined sources
Helixi270 – 2778Combined sources
Beta strandi280 – 2867Combined sources
Turni291 – 2977Combined sources
Beta strandi306 – 3094Combined sources
Beta strandi311 – 3166Combined sources
Beta strandi319 – 3224Combined sources
Helixi326 – 34015Combined sources
Turni341 – 3433Combined sources
Helixi367 – 37711Combined sources
Beta strandi383 – 3864Combined sources
Helixi390 – 3945Combined sources
Helixi395 – 3973Combined sources
Beta strandi405 – 4073Combined sources
Turni410 – 4123Combined sources
Helixi417 – 43216Combined sources
Beta strandi438 – 4436Combined sources
Helixi444 – 4507Combined sources
Helixi453 – 4597Combined sources
Beta strandi465 – 4739Combined sources
Helixi475 – 4806Combined sources
Helixi486 – 4883Combined sources
Helixi495 – 4973Combined sources
Helixi498 – 5014Combined sources
Beta strandi505 – 5128Combined sources
Helixi515 – 5228Combined sources
Helixi525 – 5284Combined sources
Beta strandi532 – 5398Combined sources
Helixi547 – 55812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VJYX-ray2.30A/B/C/D1-563[»]
2VK4X-ray1.95A/B/C/D1-563[»]
ProteinModelPortaliQ12629.
SMRiQ12629. Positions 2-554.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12629.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 47687Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiKOG1184. Eukaryota.
COG3961. LUCA.
HOGENOMiHOG000061334.
InParanoidiQ12629.
KOiK01568.
OMAiPNNTYGI.
OrthoDBiEOG779P6S.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PANTHERiPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEITLGRYL FERLKQVEVQ TIFGLPGDFN LSLLDNIYEV PGMRWAGNAN
60 70 80 90 100
ELNAAYAADG YARLKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG
110 120 130 140 150
VPSVSSQAKQ LLLHHTLGNG DFTVFHRMSS NISETTAMIT DINTAPAEID
160 170 180 190 200
RCIRTTYVSQ RPVYLGLPAN LVDLTVPASL LDTPIDLSLK PNDPEAEEEV
210 220 230 240 250
IENVLQLIKE AKNPVILADA CCSRHDAKAE TKKLIDLTQF PAFVTPMGKG
260 270 280 290 300
SIDEKHPRFG GVYVGTLSSP AVKEAVESAD LVLSVGALLS DFNTGSFSYS
310 320 330 340 350
YKTKNIVEFH SDYTKIRSAT FPGVQMKFAL QKLLTKVADA AKGYKPVPVP
360 370 380 390 400
SEPEHNEAVA DSTPLKQEWV WTQVGEFLRE GDVVITETGT SAFGINQTHF
410 420 430 440 450
PNNTYGISQV LWGSIGFTTG ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT
460 470 480 490 500
VQEISTMIRW GLKPYLFVLN NDGYTIERLI HGETAQYNCI QNWQHLELLP
510 520 530 540 550
TFGAKDYEAV RVSTTGEWNK LTTDEKFQDN TRIRLIEVML PTMDAPSNLV
560
KQAQLTAATN AKN
Length:563
Mass (Da):61,658
Last modified:September 27, 2004 - v2
Checksum:iB6A4691DC081626C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291S → C in CAA59953 (PubMed:8821934).Curated
Sequence conflicti280 – 2801D → H in CAA59953 (PubMed:8821934).Curated
Sequence conflicti318 – 3192SA → RP in CAA59953 (PubMed:8821934).Curated
Sequence conflicti358 – 3581A → D in CAA59953 (PubMed:8821934).Curated
Sequence conflicti559 – 5591T → S in CAA59953 (PubMed:8821934).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85968 Genomic DNA. Translation: CAA59953.1.
CR382125 Genomic DNA. Translation: CAG99771.1.
PIRiS70684.
RefSeqiXP_454684.1. XM_454684.1.

Genome annotation databases

EnsemblFungiiCAG99771; CAG99771; KLLA0_E16303g.
GeneIDi2894295.
KEGGikla:KLLA0E16303g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85968 Genomic DNA. Translation: CAA59953.1.
CR382125 Genomic DNA. Translation: CAG99771.1.
PIRiS70684.
RefSeqiXP_454684.1. XM_454684.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VJYX-ray2.30A/B/C/D1-563[»]
2VK4X-ray1.95A/B/C/D1-563[»]
ProteinModelPortaliQ12629.
SMRiQ12629. Positions 2-554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284590.XP_454684.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG99771; CAG99771; KLLA0_E16303g.
GeneIDi2894295.
KEGGikla:KLLA0E16303g.

Phylogenomic databases

eggNOGiKOG1184. Eukaryota.
COG3961. LUCA.
HOGENOMiHOG000061334.
InParanoidiQ12629.
KOiK01568.
OMAiPNNTYGI.
OrthoDBiEOG779P6S.

Enzyme and pathway databases

BRENDAi4.1.1.1. 2825.

Miscellaneous databases

EvolutionaryTraceiQ12629.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PANTHERiPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 'petite-negative' yeast Kluyveromyces lactis has a single gene expressing pyruvate decarboxylase activity."
    Bianchi M.M., Tizzani L., Destruelle M., Frontall L., Wesolowski-Louvel M.
    Mol. Microbiol. 19:27-36(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Entry informationi

Entry nameiPDC1_KLULA
AccessioniPrimary (citable) accession number: Q12629
Secondary accession number(s): Q6CN05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2004
Last modified: November 11, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.