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P40807 (DCOR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine decarboxylase 1
Short name=ODC
EC=4.1.1.17
Gene names
Name:Odc1
ORF Names:CG8721
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Developmental stage

Expressed in adults. Ref.1

Sequence similarities

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

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG12116Q9W3F11EBI-149186,EBI-193758

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Ornithine decarboxylase 1
PRO_0000149899

Sites

Active site3431Proton donor; shared with dimeric partner By similarity

Amino acid modifications

Modified residue621N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict44 – 452KL → NV in CAA47167. Ref.1
Sequence conflict44 – 452KL → NV in CAA47165. Ref.1
Sequence conflict2421K → Q in CAA47165. Ref.1
Sequence conflict3251L → Q in CAA47165. Ref.1
Sequence conflict3481K → Q in CAA47165. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40807 [UniParc].

Last modified April 12, 2005. Version 3.
Checksum: 5D2F348D1467E39B

FASTA39444,195
        10         20         30         40         50         60 
MAAATPEIQF YERELNIRRV IEECDLQRLD QALNICDLSS VERKLRLWQK LLPRIKPFYA 

        70         80         90        100        110        120 
VKCNDDPMVV RLLAQLGAGF DCASKNEVKL VLGFDVSPER IIFANPCRPV SHLEYAKEHQ 

       130        140        150        160        170        180 
VSNGTVDNEF EVYKLHTHYP NSNLIVRFKS EAKEAQCPLG DKFGCDADVD AAALMLLAKS 

       190        200        210        220        230        240 
LELKVTGTSF HVGSGCSELQ AYDRAIKKAK NLFKFGALLG YDMDFLDIGG GFPGSDDVKF 

       250        260        270        280        290        300 
EKIAESVNTS VQRHFPDERV HIIAEPGRFF VAAACTLVCK IHAKREIRNE AGKLDTVMYY 

       310        320        330        340        350        360 
LNDGVYGSFN CILYDHQVVI AEHYLDNAES LPHLKSLIWG PSCDALDKIS EDLHLPNLNR 

       370        380        390 
GDLLGFRNMG AYTMPIASAF NGFEVPKTLY FQAI

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the Drosophila ornithine decarboxylase locus: evidence for the presence of two transcribed ODC genes in the Drosophila genome."
Rom E., Kahana C.
DNA Cell Biol. 12:499-508(1993) [PubMed: 8329117] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE.
Strain: Canton-S.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X66601 Genomic DNA. Translation: CAA47167.1.
X66599 mRNA. Translation: CAA47165.1.
AE013599 Genomic DNA. Translation: AAF59150.1.
AY094710 mRNA. Translation: AAM11063.1.
RefSeqNP_477052.2. NM_057704.3.
UniGeneDm.3665.

3D structure databases

ProteinModelPortalP40807.
SMRP40807. Positions 7-393.
ModBaseSearch...

Protein-protein interaction databases

IntActP40807. 1 interaction.
MINTMINT-824263.
STRINGP40807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088863; FBpp0087939; FBgn0013307.
GeneID35766.
KEGGdme:Dmel_CG8721.
NMPDRfig|7227.3.peg.3797.

Organism-specific databases

CTD4953.
FlyBaseFBgn0013307. Odc1.

Phylogenomic databases

eggNOGinNOG06353.
GeneTreeEMGT00050000011331.
InParanoidP40807.
OMAMNCILFD.
OrthoDBEOG4R7SS8.
PhylomeDBP40807.

Gene expression databases

ArrayExpressP40807.
BgeeP40807.
GermOnlineCG8721. Drosophila melanogaster.

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...

Other

NextBio795118.

Entry information

Entry nameDCOR1_DROME
AccessionPrimary (citable) accession number: P40807
Secondary accession number(s): Q9V352
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 12, 2005
Last modified: January 25, 2012
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents