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Protein

Ornithine decarboxylase

Gene

SPE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.1 Publication

Miscellaneous

Present with 688 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

L-ornithine = putrescine + CO2.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Inhibited by antizyme (AZ) OAZ1 in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome.1 Publication

Pathwayi: putrescine biosynthesis via L-ornithine pathway

This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Ornithine decarboxylase (SPE1)
This subpathway is part of the pathway putrescine biosynthesis via L-ornithine pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from L-ornithine, the pathway putrescine biosynthesis via L-ornithine pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei244Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediatesBy similarity1
Binding sitei247Pyridoxal phosphateBy similarity1
Binding sitei286Pyridoxal phosphate; via amino nitrogenBy similarity1
Active sitei411Proton donor; shared with dimeric partnerBy similarity1
Binding sitei412Substrate; shared with dimeric partnerBy similarity1
Binding sitei441Pyridoxal phosphateBy similarity1

GO - Molecular functioni

  • ornithine decarboxylase activity Source: SGD

GO - Biological processi

  • pantothenate biosynthetic process Source: SGD
  • putrescine biosynthetic process Source: SGD
  • putrescine biosynthetic process from ornithine Source: GO_Central

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:YKL184W-MONOMER.
YEAST:YKL184W-MONOMER.
ReactomeiR-SCE-351143. Agmatine biosynthesis.
R-SCE-351202. Metabolism of polyamines.
UniPathwayiUPA00535; UER00288.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase (EC:4.1.1.171 Publication)
Short name:
ODC
Gene namesi
Name:SPE11 Publication
Synonyms:ORD1
Ordered Locus Names:YKL184WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL184W.
SGDiS000001667. SPE1.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001499091 – 466Ornithine decarboxylaseAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PRIDEiP08432.

Interactioni

Subunit structurei

Homodimer (PubMed:2669750). Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi33938. 432 interactors.
IntActiP08432. 6 interactors.
MINTiMINT-4493221.
STRINGi4932.YKL184W.

Structurei

3D structure databases

ProteinModelPortaliP08432.
SMRiP08432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni318 – 321Pyridoxal phosphate bindingBy similarity4
Regioni362 – 363Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000011560.
HOGENOMiHOG000274133.
InParanoidiP08432.
KOiK01581.
OMAiNDKFSSG.
OrthoDBiEOG092C2Q2K.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiView protein in InterPro
IPR009006. Ala_racemase/Decarboxylase_C.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
IPR029066. PLP-binding_barrel.
PfamiView protein in Pfam
PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiView protein in PROSITE
PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P08432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTQVGNAL SSSTTTLVDL SNSTVTQKKQ YYKDGETLHN LLLELKNNQD
60 70 80 90 100
LELLPHEQAH PKIFQALKAR IGRINNETCD PGEENSFFIC DLGEVKRLFN
110 120 130 140 150
NWVKELPRIK PFYAVKCNPD TKVLSLLAEL GVNFDCASKV EIDRVLSMNI
160 170 180 190 200
SPDRIVYANP CKVASFIRYA ASKNVMKSTF DNVEELHKIK KFHPESQLLL
210 220 230 240 250
RIATDDSTAQ CRLSTKYGCE MENVDVLLKA IKELGLNLAG VSFHVGSGAS
260 270 280 290 300
DFTSLYKAVR DARTVFDKAA NEYGLPPLKI LDVGGGFQFE SFKESTAVLR
310 320 330 340 350
LALEEFFPVG CGVDIIAEPG RYFVATAFTL ASHVIAKRKL SENEAMIYTN
360 370 380 390 400
DGVYGNMNCI LFDHQEPHPR TLYHNLEFHY DDFESTTAVL DSINKTRSEY
410 420 430 440 450
PYKVSIWGPT CDGLDCIAKE YYMKHDVIVG DWFYFPALGA YTSSAATQFN
460
GFEQTADIVY IDSELD
Length:466
Mass (Da):52,285
Last modified:August 1, 1988 - v1
Checksum:i2EBD7EE8CFAA67CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02777 Genomic DNA. Translation: AAA34829.1.
X74151 Genomic DNA. Translation: CAA52254.1.
Z28184 Genomic DNA. Translation: CAA82027.1.
BK006944 Genomic DNA. Translation: DAA08982.1.
PIRiA28437. DCBYO.
RefSeqiNP_012737.1. NM_001179750.1.

Genome annotation databases

EnsemblFungiiYKL184W; YKL184W; YKL184W.
GeneIDi853651.
KEGGisce:YKL184W.

Similar proteinsi

Entry informationi

Entry nameiDCOR_YEAST
AccessioniPrimary (citable) accession number: P08432
Secondary accession number(s): D6VX16
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 27, 2017
This is version 145 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names