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Protein

Ornithine decarboxylase

Gene

spe1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

L-ornithine = putrescine + CO2.

Cofactori

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei377 – 3771Proton donor; shared with dimeric partnerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyridoxal 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

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Ornithine decarboxylasePRO_0000149908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiQ9UQW9.

Interactioni

Protein-protein interaction databases

BioGridi279301. 11 interactions.
MINTiMINT-4706818.

Structurei

3D structure databases

ProteinModelPortaliQ9UQW9.
SMRiQ9UQW9. Positions 66-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000274133.
InParanoidiQ9UQW9.
KOiK01581.
OMAiVFCRILC.
OrthoDBiEOG7V76GV.
PhylomeDBiQ9UQW9.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. 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.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161F → L in BAA13839 (PubMed:9501991).Curated
Sequence conflicti393 – 3931L → P in BAA13839 (PubMed:9501991).Curated

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. Positions 66-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279301. 11 interactions.
MINTiMINT-4706818.

Proteomic databases

MaxQBiQ9UQW9.

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.
OrthoDBiEOG7V76GV.
PhylomeDBiQ9UQW9.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20803896.
PROiQ9UQW9.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. 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.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterisation of a cDNA for ornithine decarboxylase from Schizosaccharomyces pombe."
    Franceschetti M., Illingworth C., Mayer M.J., Michael A.J.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-432.
    Strain: PR745.

Entry informationi

Entry nameiDCOR_SCHPO
AccessioniPrimary (citable) accession number: Q9UQW9
Secondary accession number(s): P78829
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 113 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, 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.