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Reviewed, UniProtKB/Swiss-Prot O22616 (DCOR_SOLLC)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ornithine decarboxylase
      Short name=ODC
    EC=4.1.1.17
Alternative name(s):
    LeODC
Gene names
Name: ODC
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

L-ornithine = putrescine + CO2.

Cofactor

Pyridoxal phosphate.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.

Tissue specificity

High expression in roots, shoot tips and whole flowers at anthesis. Lower expression in stems and the lowest in adult leaves. Ref.2

Developmental stage

Transient induction at 8 days post-anthesis. ODC activity seems to be related to active cell division. Ref.2

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
Gene Ontology (GO)
   Biological processpolyamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionornithine decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Ornithine decarboxylase
PRO_0000239255

Sites

Active site3761Proton donor; shared with dimeric partner By similarity

Amino acid modifications

Modified residue941N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O22616-1 [UniParc].

Last modified March 1, 2001. Version 2.
Checksum: B126D4FECEAE305D

FASTA43146,647
        10         20         30         40         50         60 
MAGQTVIVSG LNPAAILQST IGGAPVAAAA ENGHTRKVVP LSKDALQDFM VSIITQKLQD 

        70         80         90        100        110        120 
DKQPFYVLDL GEVVSLMEQW NSALPNIRPF YAVKCNPEPS FLSMLSAMGS NFDCASRAEI 

       130        140        150        160        170        180 
EYVLSHGISP DRIVFANPCK PESDIIFAEK IGVNLTTYDS EDEVYKIRKH HPKCELLLRI 

       190        200        210        220        230        240 
KPMTDGNARC PMGPKYGALP EEIEPLLRTA QAARLTVSGV SFHIGSGDAD SNAYLGAIAA 

       250        260        270        280        290        300 
AKQVFETAAQ LGMPKMTVLD IGGGFTSGHQ FTTAAPAVKS ALETHFHDFP ELTIIAEPGR 

       310        320        330        340        350        360 
FFAETAFTLA TTIIGKRVRG ELKEYWINDG LYGSMNCVLY DHATVTATPL ACMSNRNNLN 

       370        380        390        400        410        420 
CGGSKTFPST VFGPTCDALD TVLRDYQLPE LQVNDWLIFP NMGAYTKAAG SNFNGFNTSA 

       430 
IVTHLAYAYP N 

« Hide

References

[1]Kwak S.H., Lee S.H.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Pink ball.
Tissue: Root.
[2]"Expression of ornithine decarboxylase is transiently increased by pollination, 2,4-dichlorophenoxyacetic acid, and gibberellic acid in tomato ovaries."
Alabadi D., Carbonell J.
Plant Physiol. 118:323-328(1998) [PubMed: 9733552] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Strain: cv. Rutgers.
Tissue: Ovary.

Cross-references

Sequence databases

AF029349 mRNA. Translation: AAB82301.2.
AF030292 mRNA. Translation: AAC61845.1.
UniGeneLes.3525

3D structure databases

HSSPHSSP built from PDB template 1NJJ based on UniProtKB Q9TZZ6.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.17. 281054.

Family and domain databases

InterProIPR000183. De-COase2.
IPR002433. Orn_de-COase.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCOR_SOLLC
AccessionPrimary (citable) accession number: O22616
Secondary accession number(s): O82420
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents