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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: -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)DescriptionActionsGraphical viewLength
Binding sitei28SubstrateBy similarity1
Binding sitei115SubstrateBy similarity1
Metal bindingi444MagnesiumBy similarity1
Metal bindingi471MagnesiumBy similarity1
Metal bindingi473Magnesium; via carbonyl oxygenBy similarity1
Binding sitei477SubstrateBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionDecarboxylase, Lyase
LigandMagnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BRENDAi4.1.1.1 2825

Protein family/group databases

MoonProtiQ12629

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000907651 – 563Pyruvate decarboxylaseAdd BLAST563

Proteomic databases

PRIDEiQ12629

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi284590.XP_454684.1

Structurei

Secondary structure

1563
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi6 – 16Combined sources11
Beta strandi21 – 24Combined sources4
Turni28 – 30Combined sources3
Helixi31 – 35Combined sources5
Helixi36 – 39Combined sources4
Helixi51 – 65Combined sources15
Beta strandi68 – 73Combined sources6
Helixi76 – 80Combined sources5
Helixi82 – 90Combined sources9
Beta strandi95 – 101Combined sources7
Helixi104 – 108Combined sources5
Helixi109 – 114Combined sources6
Beta strandi118 – 120Combined sources3
Helixi124 – 130Combined sources7
Beta strandi134 – 138Combined sources5
Turni142 – 144Combined sources3
Helixi145 – 159Combined sources15
Beta strandi163 – 168Combined sources6
Helixi169 – 172Combined sources4
Beta strandi174 – 177Combined sources4
Helixi178 – 182Combined sources5
Helixi194 – 210Combined sources17
Beta strandi212 – 218Combined sources7
Turni220 – 226Combined sources7
Helixi228 – 238Combined sources11
Beta strandi242 – 244Combined sources3
Turni246 – 250Combined sources5
Beta strandi259 – 262Combined sources4
Helixi265 – 267Combined sources3
Helixi270 – 277Combined sources8
Beta strandi280 – 286Combined sources7
Turni291 – 297Combined sources7
Beta strandi306 – 309Combined sources4
Beta strandi311 – 316Combined sources6
Beta strandi319 – 322Combined sources4
Helixi326 – 340Combined sources15
Turni341 – 343Combined sources3
Helixi367 – 377Combined sources11
Beta strandi383 – 386Combined sources4
Helixi390 – 394Combined sources5
Helixi395 – 397Combined sources3
Beta strandi405 – 407Combined sources3
Turni410 – 412Combined sources3
Helixi417 – 432Combined sources16
Beta strandi438 – 443Combined sources6
Helixi444 – 450Combined sources7
Helixi453 – 459Combined sources7
Beta strandi465 – 473Combined sources9
Helixi475 – 480Combined sources6
Helixi486 – 488Combined sources3
Helixi495 – 497Combined sources3
Helixi498 – 501Combined sources4
Beta strandi505 – 512Combined sources8
Helixi515 – 522Combined sources8
Helixi525 – 528Combined sources4
Beta strandi532 – 539Combined sources8
Helixi547 – 558Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ12629

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni390 – 476Thiamine pyrophosphate bindingAdd BLAST87

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiKOG1184 Eukaryota
COG3961 LUCA
HOGENOMiHOG000061334
InParanoidiQ12629
KOiK01568
OMAiEWIGNCN
OrthoDBiEOG092C29BL

Family and domain databases

InterProiView protein in InterPro
IPR029035 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
PfamiView protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit
PIRSFiPIRSF036565 Pyruvt_ip_decrb, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits
PROSITEiView protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti129S → C in CAA59953 (PubMed:8821934).Curated1
Sequence conflicti280D → H in CAA59953 (PubMed:8821934).Curated1
Sequence conflicti318 – 319SA → RP in CAA59953 (PubMed:8821934).Curated2
Sequence conflicti358A → D in CAA59953 (PubMed:8821934).Curated1
Sequence conflicti559T → S in CAA59953 (PubMed:8821934).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiPDC1_KLULA
AccessioniPrimary (citable) accession number: Q12629
Secondary accession number(s): Q6CN05
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2004
Last modified: May 23, 2018
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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