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Protein

Ornithine decarboxylase

Gene

spe1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

L-ornithine = putrescine + CO2.By similarity

Cofactori

pyridoxal 5'-phosphateBy similarity

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.By similarity

Pathwayi: putrescine biosynthesis via L-ornithine pathway

This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine.
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
Sitei226Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediatesBy similarity1
Binding sitei229Pyridoxal phosphateBy similarity1
Binding sitei266Pyridoxal phosphate; via amino nitrogenBy similarity1
Active sitei377Proton donor; shared with dimeric partnerBy similarity1
Binding sitei378Substrate; shared with dimeric partnerBy similarity1
Binding sitei407Pyridoxal phosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-SPO-351143. Agmatine biosynthesis.
R-SPO-351202. Metabolism of polyamines.
UniPathwayiUPA00535; UER00288.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase (EC:4.1.1.17)
Short name:
ODC
Gene namesi
Name:spe1
ORF Names:SPAC144.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC144.04c.
PomBaseiSPAC144.04c. spe1.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001499081 – 432Ornithine decarboxylaseAdd BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

MaxQBiQ9UQW9.
PRIDEiQ9UQW9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi279301. 11 interactors.
MINTiMINT-4706818.

Structurei

3D structure databases

ProteinModelPortaliQ9UQW9.
SMRiQ9UQW9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni296 – 299Pyridoxal phosphate bindingBy similarity4
Regioni341 – 342Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000274133.
InParanoidiQ9UQW9.
KOiK01581.
OMAiVFCRILC.
OrthoDBiEOG092C2Q2K.
PhylomeDBiQ9UQW9.

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.
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.

Sequencei

Sequence statusi: Complete.

Q9UQW9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAIMEKNML VSESLRTTEL LGHVKPIDSV VTWSSPGSSR QAIGEAFKNT
60 70 80 90 100
IEEIERAAVR GEPADSDAFF VADLNGVYRQ LLRWHAKLPR VQPFYAVKCN
110 120 130 140 150
PDPKVLALLN KFGTGFDCAS KGELEQILGL GVSPDRIVYA NPCKAITYVR
160 170 180 190 200
YAASKGINLM TFDNADELYK VKQHHPNSRL LLRISTDDSN SLCRLSLKFG
210 220 230 240 250
ASLDDTGKLL DIAKSLELNV VGVSFHVGSG SYDPSAFLDA IQRSRQVFDQ
260 270 280 290 300
GLERGFNFDL LDIGGGFMND SFDGVADLIR SALDTYFDPS IRVISEPGRF
310 320 330 340 350
FVSSSFTLAV NVIAKRKLDD EEKVMYYVND GVYGSLNCIL FDHQHPVARV
360 370 380 390 400
LKCGSRFVYN DLVGTGQHRC FIWGPTCDSL DVIANDAHLP YELNVGDWIY
410 420 430
FEDAGAYTVA AASCFNGFKT SRIVYLDTDI LD
Length:432
Mass (Da):47,843
Last modified:May 1, 2000 - v1
Checksum:iF91BD81073970AC9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti116F → L in BAA13839 (PubMed:9501991).Curated1
Sequence conflicti393L → P in BAA13839 (PubMed:9501991).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243276 mRNA. Translation: CAB45689.1.
CU329670 Genomic DNA. Translation: CAB59684.1.
D89177 mRNA. Translation: BAA13839.1.
PIRiT37671.
RefSeqiNP_594665.1. NM_001020094.2.

Genome annotation databases

EnsemblFungiiSPAC144.04c.1; SPAC144.04c.1:pep; SPAC144.04c.
GeneIDi2542855.
KEGGispo:SPAC144.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243276 mRNA. Translation: CAB45689.1.
CU329670 Genomic DNA. Translation: CAB59684.1.
D89177 mRNA. Translation: BAA13839.1.
PIRiT37671.
RefSeqiNP_594665.1. NM_001020094.2.

3D structure databases

ProteinModelPortaliQ9UQW9.
SMRiQ9UQW9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279301. 11 interactors.
MINTiMINT-4706818.

Proteomic databases

MaxQBiQ9UQW9.
PRIDEiQ9UQW9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC144.04c.1; SPAC144.04c.1:pep; SPAC144.04c.
GeneIDi2542855.
KEGGispo:SPAC144.04c.

Organism-specific databases

EuPathDBiFungiDB:SPAC144.04c.
PomBaseiSPAC144.04c. spe1.

Phylogenomic databases

HOGENOMiHOG000274133.
InParanoidiQ9UQW9.
KOiK01581.
OMAiVFCRILC.
OrthoDBiEOG092C2Q2K.
PhylomeDBiQ9UQW9.

Enzyme and pathway databases

UniPathwayiUPA00535; UER00288.
ReactomeiR-SPO-351143. Agmatine biosynthesis.
R-SPO-351202. Metabolism of polyamines.

Miscellaneous databases

PROiQ9UQW9.

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.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiDCOR_SCHPO
AccessioniPrimary (citable) accession number: Q9UQW9
Secondary accession number(s): P78829
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: March 15, 2017
This is version 120 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.