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Protein

Ornithine decarboxylase 1

Gene

Odc1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

L-ornithine = putrescine + CO2.

Cofactori

Pathwayi: putrescine biosynthesis via L-ornithine pathway

This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine.
Proteins known to be involved in this subpathway in this organism are:
  1. Ornithine decarboxylase 2 (Odc2), Ornithine decarboxylase 1 (Odc1)
This subpathway is part of the pathway putrescine biosynthesis via L-ornithine pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from L-ornithine, the pathway putrescine biosynthesis via L-ornithine pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei343 – 3431Proton donor; shared with dimeric partnerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-351143. Agmatine biosynthesis.
R-DME-351202. Metabolism of polyamines.
UniPathwayiUPA00535; UER00288.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase 1 (EC:4.1.1.17)
Short name:
ODC
Gene namesi
Name:Odc1
ORF Names:CG8721
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0013307. Odc1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Ornithine decarboxylase 1PRO_0000149899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP40807.

Expressioni

Developmental stagei

Expressed in adults.1 Publication

Gene expression databases

BgeeiP40807.
GenevisibleiP40807. DM.

Interactioni

Protein-protein interaction databases

BioGridi61627. 1 interaction.
IntActiP40807. 1 interaction.
MINTiMINT-824263.
STRINGi7227.FBpp0087939.

Structurei

3D structure databases

ProteinModelPortaliP40807.
SMRiP40807. Positions 32-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0622. Eukaryota.
COG0019. LUCA.
GeneTreeiENSGT00390000011560.
InParanoidiP40807.
KOiK01581.
OMAiVFCRILC.
OrthoDBiEOG73Z2T6.
PhylomeDBiP40807.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. 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.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATPEIQF YERELNIRRV IEECDLQRLD QALNICDLSS VERKLRLWQK
60 70 80 90 100
LLPRIKPFYA VKCNDDPMVV RLLAQLGAGF DCASKNEVKL VLGFDVSPER
110 120 130 140 150
IIFANPCRPV SHLEYAKEHQ VSNGTVDNEF EVYKLHTHYP NSNLIVRFKS
160 170 180 190 200
EAKEAQCPLG DKFGCDADVD AAALMLLAKS LELKVTGTSF HVGSGCSELQ
210 220 230 240 250
AYDRAIKKAK NLFKFGALLG YDMDFLDIGG GFPGSDDVKF EKIAESVNTS
260 270 280 290 300
VQRHFPDERV HIIAEPGRFF VAAACTLVCK IHAKREIRNE AGKLDTVMYY
310 320 330 340 350
LNDGVYGSFN CILYDHQVVI AEHYLDNAES LPHLKSLIWG PSCDALDKIS
360 370 380 390
EDLHLPNLNR GDLLGFRNMG AYTMPIASAF NGFEVPKTLY FQAI
Length:394
Mass (Da):44,195
Last modified:April 12, 2005 - v3
Checksum:i5D2F348D1467E39B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 452KL → NV in CAA47167 (PubMed:8329117).Curated
Sequence conflicti44 – 452KL → NV in CAA47165 (PubMed:8329117).Curated
Sequence conflicti242 – 2421K → Q in CAA47165 (PubMed:8329117).Curated
Sequence conflicti325 – 3251L → Q in CAA47165 (PubMed:8329117).Curated
Sequence conflicti348 – 3481K → Q in CAA47165 (PubMed:8329117).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66601 Genomic DNA. Translation: CAA47167.1.
X66599 mRNA. Translation: CAA47165.1.
AE013599 Genomic DNA. Translation: AAF59150.1.
AY094710 mRNA. Translation: AAM11063.1.
RefSeqiNP_477052.2. NM_057704.5.
UniGeneiDm.3665.

Genome annotation databases

EnsemblMetazoaiFBtr0088863; FBpp0087939; FBgn0013307.
GeneIDi35766.
KEGGidme:Dmel_CG8721.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66601 Genomic DNA. Translation: CAA47167.1.
X66599 mRNA. Translation: CAA47165.1.
AE013599 Genomic DNA. Translation: AAF59150.1.
AY094710 mRNA. Translation: AAM11063.1.
RefSeqiNP_477052.2. NM_057704.5.
UniGeneiDm.3665.

3D structure databases

ProteinModelPortaliP40807.
SMRiP40807. Positions 32-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61627. 1 interaction.
IntActiP40807. 1 interaction.
MINTiMINT-824263.
STRINGi7227.FBpp0087939.

Proteomic databases

PaxDbiP40807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088863; FBpp0087939; FBgn0013307.
GeneIDi35766.
KEGGidme:Dmel_CG8721.

Organism-specific databases

CTDi4953.
FlyBaseiFBgn0013307. Odc1.

Phylogenomic databases

eggNOGiKOG0622. Eukaryota.
COG0019. LUCA.
GeneTreeiENSGT00390000011560.
InParanoidiP40807.
KOiK01581.
OMAiVFCRILC.
OrthoDBiEOG73Z2T6.
PhylomeDBiP40807.

Enzyme and pathway databases

UniPathwayiUPA00535; UER00288.
ReactomeiR-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-351143. Agmatine biosynthesis.
R-DME-351202. Metabolism of polyamines.

Miscellaneous databases

GenomeRNAii35766.
NextBioi795118.
PROiP40807.

Gene expression databases

BgeeiP40807.
GenevisibleiP40807. DM.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. 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.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Testis.

Entry informationi

Entry nameiDCOR1_DROME
AccessioniPrimary (citable) accession number: P40807
Secondary accession number(s): Q9V352
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 12, 2005
Last modified: May 11, 2016
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.