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Reviewed, UniProtKB/Swiss-Prot Q92445 (DCOR_PARBR)

Last modified January 20, 2009. Version 39. 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
Gene names
Name: ODC
OrganismParacoccidioides brasiliensis
Taxonomic identifier121759 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides

Protein attributes

Sequence length79 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

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

Chain‹1 – ›79›79Ornithine decarboxylase
PRO_0000149907

Experimental info

Non-terminal residue11
Non-terminal residue791

Sequences

Sequence LengthMass (Da)Tools
Q92445-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 3F81351DC5C84F9B

FASTA798,579
        10         20         30         40         50         60 
GVSFHVGSGA EDPKSFVKAV EDSRFVFDQA AEVGFDLKVL DVGGGFSEDT FERFAATLSD 

        70 
ALDEYFPPHI RIIAEPGRI 

« Hide

References

[1]"Ornithine decarboxylase in Paracoccidioides brasiliensis."
San-Blas G., Sorais F., San-Blas F., Ruiz-Herrera J.
Arch. Microbiol. 165:311-316(1996) [PubMed: 8661922] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 32071 / IVIC Pb73 / C81.

Cross-references

Sequence databases

X97265 Genomic DNA. Translation: CAA65920.1.

3D structure databases

HSSPHSSP built from PDB template 7ODC based on UniProtKB P00860.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.17. 274879.

Family and domain databases

InterProIPR000183. De-COase2.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
[Graphical view]
PROSITEPS00878. ODR_DC_2_1. Partial match.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCOR_PARBR
AccessionPrimary (citable) accession number: Q92445
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 20, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal 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