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P27120 (DCOR1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine decarboxylase 1

Short name=ODC 1
Short name=xODC1
EC=4.1.1.17
Gene names
Name:odc1-a
Synonyms:odc, odc1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

L-ornithine = putrescine + CO2.

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Regulated post-translationally by polyamines.

Pathway

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

Developmental stage

Levels increase in the embryos 1.5-2 hours after fertilization and reach a maximum at 6 hours post-fertilization, then decrease to a very low level in early gastrulating embryos (12 hours post-fertilization). Ref.2

Sequence similarities

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

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   PTMPhosphoprotein
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 – 460460Ornithine decarboxylase 1
PRO_0000149896

Sites

Active site3611Proton donor; shared with dimeric partner By similarity

Amino acid modifications

Modified residue691N6-(pyridoxal phosphate)lysine By similarity
Modified residue3031Phosphoserine; by CK2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27120 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: CC6F87FD165877EE

FASTA46050,830
        10         20         30         40         50         60 
MNSFSNDDFD FSFLEEGFSA RDIVEQKINE VSLSDDKDAF YVADFGDIVK KHVRWFKALP 

        70         80         90        100        110        120 
RVTPFYAVKC NDGKAIVKTL SILGAGFDCA SKTEIQLVQS IGVSPERIIY ANPCKQVSQI 

       130        140        150        160        170        180 
KYAASCGVEK MTFDSEVELM KVARNHPNAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL 

       190        200        210        220        230        240 
LERAKELNVD IIGVSFHVGS GCTDPQTYVQ AVSDARCVFD MGAELGFNMH LLDIGGGFPG 

       250        260        270        280        290        300 
SEDVKLKFEE ITSVINPALD KYFPADSGVK IIAEPGRYYV ASSFTLAVNI IAKKVMVNEQ 

       310        320        330        340        350        360 
SGSDDEEDAA NDKTLMYYVN DGVYGSFNCI LFDHAHVKPV LTKKPKPDEK FYSSSIWGPT 

       370        380        390        400        410        420 
CDGLDRIVER FELPELQVGD WMLFENMGAY TVAAASTFNG FQRPTLYYVM SRPHWQLMHD 

       430        440        450        460 
IKEHGILPEV PDLSALHVSC AQESGMELAP AVCTAASINV 

« Hide

References

[1]"Post-transcriptional regulation of ornithine decarboxylase in Xenopus laevis oocytes."
Bassez T., Paris J., Omilli F., Dorel C., Osborne H.B.
Development 110:955-962(1990) [PubMed: 2088731] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Oocyte.
[2]"Expression and post-transcriptional regulation of ornithine decarboxylase during early Xenopus development."
Osborne H.B., Duval C., Ghoda L., Omilli F., Bassez T., Coffino P.
Eur. J. Biochem. 202:575-581(1991) [PubMed: 1761057] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56316 mRNA. Translation: CAA39760.1.
PIRA43563.
UniGeneXl.4223.

3D structure databases

ProteinModelPortalP27120.
SMRP27120. Positions 7-422.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-856383. odc1.

Phylogenomic databases

HOVERGENHBG005456.

Family and domain databases

InterProIPR009006. 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.
[Graphical view]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit.
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCOR1_XENLA
AccessionPrimary (citable) accession number: P27120
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 31, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families