Skip Header

Contribute Send feedback
Read comments (?) or add your own

P27117 (DCOR_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 90. 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

Short name=ODC
EC=4.1.1.17
Gene names
Name:ODC1
Synonyms:ODC
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
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.

Subunit structure

Homodimer.

Sequence similarities

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

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
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 – 461461Ornithine decarboxylase
PRO_0000149889

Sites

Active site3601Proton 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
P27117 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 4E609B643E3B68FA

FASTA46151,346
        10         20         30         40         50         60 
MNSFSNEEFD CHFLDEGFTA KDILDQKINE VSYSDDKDAF YVADLGDILK KHLRWLKALP 

        70         80         90        100        110        120 
RVTPFYAVKC NDSRTIVKTL AAIGTGFDCA SKTEIQLVQS LGVPPERIIY ANPCKQVSQI 

       130        140        150        160        170        180 
KYAANNGVQM MTFDSEVELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL 

       190        200        210        220        230        240 
LERAKELDID VIGVSFHVGS GCTDPETFVQ AISDARCVFD MGAEVGFNMY LLDIGGGFPG 

       250        260        270        280        290        300 
SEDVKLKFEE ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKLVLKEQ 

       310        320        330        340        350        360 
TGSDDEEEST DRTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY YSSSIWGPTC 

       370        380        390        400        410        420 
DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPTIYYVMS GPTWQLMQQI 

       430        440        450        460 
RTQDFPPGVE EPDVGPLPVS CAWESGMKRH SAACASTRIN V 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a bovine ornithine decarboxylase cDNA and its use in the detection of restriction fragment length polymorphisms in Holsteins."
Yao J., Zadworny D., Kuhnlein U., Hayes J.F.
Genome 38:325-331(1995) [PubMed: 7774801] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Holstein.
Tissue: Liver.
[2]"Bovine ornithine decarboxylase gene: cloning, structure and polymorphisms."
Yao J., Zadworny D., Aggrey S.E., Kuhnlein U., Hayes J.F.
DNA Seq. 8:203-213(1998) [PubMed: 10520448] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M92441 mRNA. Translation: AAA92339.1.
U36394 Genomic DNA. Translation: AAA79849.1.
U18531 Genomic DNA. Translation: AAA86696.1.
BC146218 mRNA. Translation: AAI46219.1.
IPIIPI00698809.
RefSeqNP_776555.1. NM_174130.2.
UniGeneBt.7133.

3D structure databases

ProteinModelPortalP27117.
SMRP27117. Positions 7-421.
ModBaseSearch...

Protein-protein interaction databases

STRINGP27117.

Proteomic databases

PRIDEP27117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000005575; ENSBTAP00000005575; ENSBTAG00000004256.
GeneID281365.
KEGGbta:281365.

Organism-specific databases

CTD4953.

Phylogenomic databases

eggNOGmaNOG05169.
GeneTreeENSGT00390000011560.
HOVERGENHBG005456.
InParanoidP27117.
OMAAXITSVI.
OrthoDBEOG4ZGPC6.
PhylomeDBP27117.

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.
KOK01581.
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 nameDCOR_BOVIN
AccessionPrimary (citable) accession number: P27117
Secondary accession number(s): A6H7E8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 16, 2011
This is version 90 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