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Protein

Pyruvate decarboxylase

Gene

cfp

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 5 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:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331SubstrateBy similarity
Binding sitei120 – 1201SubstrateBy similarity
Metal bindingi444 – 4441MagnesiumBy similarity
Metal bindingi471 – 4711MagnesiumBy similarity
Metal bindingi473 – 4731Magnesium; via carbonyl oxygenBy similarity
Binding sitei477 – 4771SubstrateBy similarity

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. magnesium ion binding Source: InterPro
  3. pyruvate decarboxylase activity Source: UniProtKB-EC
  4. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. pyruvate metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

UniPathwayiUPA00231.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate decarboxylase (EC:4.1.1.1)
Alternative name(s):
8-10 nm cytoplasmic filament-associated protein
P59NC
Gene namesi
Name:cfp
Synonyms:pdc-1
ORF Names:NCU02193
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 7, Linkage Group VII

Subcellular locationi

Cytoplasm
Note: Cytoplasmic filaments.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature form1 PublicationPRO_0000035653
Chaini3 – 570568Pyruvate decarboxylasePRO_0000035654Add
BLAST

Interactioni

Subunit structurei

Homopolymer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-7533403,EBI-7533403

Protein-protein interaction databases

MINTiMINT-8291074.

Structurei

3D structure databases

ProteinModelPortaliP33287.
SMRiP33287. Positions 9-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni394 – 47683Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiCOG3961.
HOGENOMiHOG000061335.
InParanoidiP33287.
KOiK01568.
OMAiYSIPACL.
OrthoDBiEOG7K6Q3N.

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]
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33287-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVAQQQGKFT VGDYLAERLA QVGVRHHFVV PGDYNLILLD KLQAHPDLKE
60 70 80 90 100
VGCANELNCS LAAEGYARAN GISACVVTYS VGALSAFNGT GSAYAENLPL
110 120 130 140 150
VLISGSPNTN DPSQYHILHH TLGHPDYTYQ YEMAKKITCC AVAIPRAIDA
160 170 180 190 200
PRLIDRALRA AILARKPCYI EIPTNLAGAT CVRPGPISAI TDPITSDKSA
210 220 230 240 250
LEAAAKCAAE YLDGKLKPVI LVGPKAGRAG SEKELIEFAE AMGCAVALQP
260 270 280 290 300
AAKGMFPEDH KQFVGIFWGQ VSSDAADAMV HWADAMICVG AVFNDYSTVG
310 320 330 340 350
WTAVPNIPLM TVDMDHVTFP GAHFSRVRMC EFLSHLATQV TFNDSTMIEY
360 370 380 390 400
KRLKPDPPHV HTAEREEPLS RKEISRQVQE MLTDKTSLFV DTGDSWFNGI
410 420 430 440 450
QLKLPPGAKF EIEMQWGHIG WSIPAAFGYA LRHPDRHTIV LVGDGSFQVT
460 470 480 490 500
AQEVSQMVRF KVPITIMLIN NRGYTIEVEI HDGSYNKIKN WDYAMLVEAF
510 520 530 540 550
NSTDGHAKGL LANTAGELAD AIKVAESHKE GPTLIECTID QDDCSKELIT
560 570
WGHYVAAANA RPPRNMSVQE
Length:570
Mass (Da):62,263
Last modified:February 1, 1994 - v1
Checksum:iDF48B86C24EDAACF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09125 mRNA. Translation: AAA33567.1.
U65927 Genomic DNA. Translation: AAB17969.1.
CM002242 Genomic DNA. Translation: ESA42032.1.
S40298 mRNA. Translation: AAB22524.2.
PIRiJN0782.
RefSeqiXP_959587.1. XM_954494.2.
UniGeneiNcr.14819.

Genome annotation databases

EnsemblFungiiEFNCRT00000003234; EFNCRP00000003234; EFNCRG00000003230.
GeneIDi3875734.
KEGGincr:NCU02193.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09125 mRNA. Translation: AAA33567.1.
U65927 Genomic DNA. Translation: AAB17969.1.
CM002242 Genomic DNA. Translation: ESA42032.1.
S40298 mRNA. Translation: AAB22524.2.
PIRiJN0782.
RefSeqiXP_959587.1. XM_954494.2.
UniGeneiNcr.14819.

3D structure databases

ProteinModelPortaliP33287.
SMRiP33287. Positions 9-565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8291074.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000003234; EFNCRP00000003234; EFNCRG00000003230.
GeneIDi3875734.
KEGGincr:NCU02193.

Phylogenomic databases

eggNOGiCOG3961.
HOGENOMiHOG000061335.
InParanoidiP33287.
KOiK01568.
OMAiYSIPACL.
OrthoDBiEOG7K6Q3N.

Enzyme and pathway databases

UniPathwayiUPA00231.

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]
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 59-kDa polypeptide constituent of 8-10-nm cytoplasmic filaments in Neurospora crassa is a pyruvate decarboxylase."
    Alvarez M.E., Rosa A.L., Temporini E.D., Wolstenholme A., Panzetta G., Patrito L., Maccioni H.J.F.
    Gene 130:253-258(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-25.
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  2. Temporini E.D., Alvarez M.E., Mautino M., Kawaguchi T., Kinghorn J., Rosa A.L.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Mycelium.
  3. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  4. "Molecular cloning of a gene (cfp) encoding the cytoplasmic filament protein P59Nc and its genetic relationship to the snowflake locus of Neurospora crassa."
    Haedo S.D., Temporini E.D., Alvarez M.E., Maccioni H.J., Rosa A.L.
    Genetics 131:575-580(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-25.

Entry informationi

Entry nameiPDC_NEUCR
AccessioniPrimary (citable) accession number: P33287
Secondary accession number(s): Q7RV97, V5IKN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 7, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.