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Database: UniProt
Entry: P40808
LinkDB: P40808
Original site: P40808 
ID   DCOR2_DROME             Reviewed;         393 AA.
AC   P40808; Q9V353;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   05-JUL-2017, entry version 131.
DE   RecName: Full=Ornithine decarboxylase 2;
DE            Short=ODC;
DE            EC=4.1.1.17;
DE   AltName: Full=dODC2;
GN   Name=Odc2; ORFNames=CG8719;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RX   PubMed=8329117; DOI=10.1089/dna.1993.12.499;
RA   Rom E., Kahana C.;
RT   "Isolation and characterization of the Drosophila ornithine
RT   decarboxylase locus: evidence for the presence of two transcribed ODC
RT   genes in the Drosophila genome.";
RL   DNA Cell Biol. 12:499-508(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC   -!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine
CC       biosynthesis that converts ornithine into putrescine, which is the
CC       precursor for the polyamines, spermidine and spermine. Polyamines
CC       are essential for cell proliferation and are implicated in
CC       cellular processes, ranging from DNA replication to apoptosis.
CC       {ECO:0000250|UniProtKB:P11926}.
CC   -!- CATALYTIC ACTIVITY: L-ornithine = putrescine + CO(2).
CC       {ECO:0000250|UniProtKB:P11926}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P11926};
CC   -!- ENZYME REGULATION: Inhibited by antizyme (AZ) in response to
CC       polyamine levels. AZ inhibits the assembly of the functional
CC       homodimer by binding to ODC monomers and targeting them for
CC       ubiquitin-independent proteolytic destruction by the 26S
CC       proteasome. {ECO:0000250|UniProtKB:P11926}.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis
CC       via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC   -!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the
CC       active sites are constructed of residues from both monomers.
CC       {ECO:0000250|UniProtKB:P11926}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. {ECO:0000305}.
DR   EMBL; X66600; CAA47166.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF59149.2; -; Genomic_DNA.
DR   RefSeq; NP_477053.2; NM_057705.4.
DR   ProteinModelPortal; P40808; -.
DR   SMR; P40808; -.
DR   BioGrid; 61628; 2.
DR   IntAct; P40808; 2.
DR   MINT; MINT-929037; -.
DR   STRING; 7227.FBpp0087940; -.
DR   PaxDb; P40808; -.
DR   PRIDE; P40808; -.
DR   EnsemblMetazoa; FBtr0088864; FBpp0087940; FBgn0013308.
DR   GeneID; 35767; -.
DR   KEGG; dme:Dmel_CG8719; -.
DR   CTD; 35767; -.
DR   FlyBase; FBgn0013308; Odc2.
DR   eggNOG; KOG0622; Eukaryota.
DR   eggNOG; COG0019; LUCA.
DR   InParanoid; P40808; -.
DR   KO; K01581; -.
DR   OMA; WIEIGHI; -.
DR   OrthoDB; EOG091G0AJV; -.
DR   PhylomeDB; P40808; -.
DR   Reactome; R-DME-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-DME-351143; Agmatine biosynthesis.
DR   Reactome; R-DME-351202; Metabolism of polyamines.
DR   UniPathway; UPA00535; UER00288.
DR   GenomeRNAi; 35767; -.
DR   PRO; PR:P40808; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0013308; -.
DR   ExpressionAtlas; P40808; differential.
DR   Genevisible; P40808; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR002433; Orn_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   PRINTS; PR01182; ORNDCRBXLASE.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    393       Ornithine decarboxylase 2.
FT                                /FTId=PRO_0000149900.
FT   REGION      265    268       Pyridoxal phosphate binding.
FT                                {ECO:0000250|UniProtKB:P11926}.
FT   REGION      314    315       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P07805}.
FT   ACT_SITE    343    343       Proton donor; shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P11926}.
FT   BINDING     194    194       Pyridoxal phosphate.
FT                                {ECO:0000250|UniProtKB:P11926}.
FT   BINDING     231    231       Pyridoxal phosphate; via amino nitrogen.
FT                                {ECO:0000250|UniProtKB:P11926}.
FT   BINDING     344    344       Substrate; shared with dimeric partner.
FT                                {ECO:0000250|UniProtKB:P07805}.
FT   BINDING     371    371       Pyridoxal phosphate.
FT                                {ECO:0000250|UniProtKB:P11926}.
FT   SITE        191    191       Stacks against the aromatic ring of
FT                                pyridoxal phosphate and stabilizes
FT                                reaction intermediates.
FT                                {ECO:0000250|UniProtKB:P00860}.
FT   MOD_RES      62     62       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250|UniProtKB:P11926}.
FT   CONFLICT     94     94       L -> F (in Ref. 1; CAA47166).
FT                                {ECO:0000305}.
FT   CONFLICT    143    143       N -> S (in Ref. 1; CAA47166).
FT                                {ECO:0000305}.
FT   CONFLICT    241    241       E -> K (in Ref. 1; CAA47166).
FT                                {ECO:0000305}.
FT   CONFLICT    346    346       M -> L (in Ref. 1; CAA47166).
FT                                {ECO:0000305}.
SQ   SEQUENCE   393 AA;  44153 MW;  9D21DF650D0FD228 CRC64;
     MVNGDLRIQY YDEELNIRKV IEQADLEHLD QALNICDLSS LERKLRLWHK LMPRIEPHYA
     VKCNDDPVVV KFLADLGTGF DCASKNELKL VLGLGVSPER IIFAHPCRPA SHLRYAKEQQ
     VVNGTVDNEY EIYKLRKHYP DSNLIVRFKS EAKKALCPLG DKYGCDAEAD AAALMLLAKA
     LGLKVTGTSF HVGSGCSEVE AYDRAIEKAE NIFKVGEMIG HKMELLDVGG GFPGIDDEMF
     EEIAQSVNTS VELRFPDKRI RIISEPGRFF VEAAYTLICK VHAKREVRSK DGKLDTMMYY
     LNDGIFGAFA GMFYYPEEVA PELYLDEAES LPKLKSVIWG PSCDAMDKIS DLLLPNLNPG
     DLLGFRNMGA YTMPIASPFN GFDVPETRFF KAK
//
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