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Reviewed, UniProtKB/Swiss-Prot Q9I8S4 (DCOR2_XENLA)

Last modified January 19, 2010. Version 52. 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 2
      Short name=ODC 2
      Short name=xODC2
    EC=4.1.1.17
Gene names
Name: odc1-B
Synonyms: odc2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

L-ornithine = putrescine + CO2.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

Developmental stage

Expression is first detected at the animal pole at stage 9. During neurula stages it is found both in the extreme anterior and posterior part of the dorsal body axis. In tailbud stages the expression is further shifted to both the tail and head areas and gradually restricted to distinct tissues: forebrain, inner layer of epidermis of the head area, stomodeal-hypophyseal anlage, frontal gland, ear vesicle, branchial arches, the front tip of neural tube and proctodeum.

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 – 456456Ornithine decarboxylase 2
PRO_0000149897

Sites

Active site3571Proton donor; shared with dimeric partner By similarity

Amino acid modifications

Modified residue681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I8S4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 78A0BFBC6FED27FE

FASTA45650,637
        10         20         30         40         50         60 
MQGYIQESDF NLVEEGFLAR DLMEEIINEV SQTEDRDAFF VADLGDVVRK HLRFLKALPR 

        70         80         90        100        110        120 
VKPFYAVKCN SSKGVVKILA ELGAGFDCAS KTEIELVQDV GVAPERIIYA NPCKQISQIK 

       130        140        150        160        170        180 
YAAKNGVQMM TFDNEVELSK VSRSHPNARM VLRIATDDSK SSARLSVKFG APLKSCRRLL 

       190        200        210        220        230        240 
EMAKNLSVDV IGVSFHVGSG CTDSKAYTQA ISDARLVFEM ASEFGYKMWL LDIGGGFPGT 

       250        260        270        280        290        300 
EDSKIRFEEI AGVINPALDM YFPESSDVQI IAEPGRYYVA SAFSLAVNVI AKKEVEHSVS 

       310        320        330        340        350        360 
DDEENESSKS IMYYVNDGVY GSFNCLVFDH AHPKPILHKK PSPDQPLYTS SLWGPTCDGL 

       370        380        390        400        410        420 
DQIAERVQLP ELHVGDWLLF ENMGAYTIAA SSNFNGFQQS PVHYAMPRAA WKAVQLLQRG 

       430        440        450 
LQQTEEKENV CTPMSCGWEI SDSLCFTRTF AATSII 

« Hide

References

[1]"Tissue-specific expression of an ornithine decarboxylase paralogue, XODC2, in Xenopus laevis."
Cao Y., Zhao H., Hollemann T., Chen Y., Grunz H.
Mech. Dev. 102:243-246(2001) [PubMed: 11287202] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF217544 mRNA. Translation: AAF27628.2.
RefSeqNP_001079692.1.
UniGeneXl.8949

3D structure databases

SMRQ9I8S4. Positions 6-418.
ModBaseSearch...

Genome annotation databases

GeneID379379.
KEGGxla:379379.

Phylogenomic databases

HOVERGENQ9I8S4.

Enzyme and pathway databases

BRENDA4.1.1.17. 648.

Family and domain databases

InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR000183. 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 nameDCOR2_XENLA
AccessionPrimary (citable) accession number: Q9I8S4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2000
Last modified: January 19, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus 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