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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   09-JUL-2014, entry version 105.
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; Endopterygota; 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   -!- CATALYTIC ACTIVITY: L-ornithine = putrescine + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis
CC       via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family.
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DR   EMBL; X66600; CAA47166.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF59149.2; -; Genomic_DNA.
DR   RefSeq; NP_477053.2; NM_057705.3.
DR   UniGene; Dm.5265; -.
DR   ProteinModelPortal; P40808; -.
DR   SMR; P40808; 35-385.
DR   BioGrid; 61628; 2.
DR   IntAct; P40808; 2.
DR   MINT; MINT-929037; -.
DR   EnsemblMetazoa; FBtr0088864; FBpp0087940; FBgn0013308.
DR   GeneID; 35767; -.
DR   KEGG; dme:Dmel_CG8719; -.
DR   CTD; 35767; -.
DR   FlyBase; FBgn0013308; Odc2.
DR   eggNOG; COG0019; -.
DR   GeneTree; ENSGT00390000011560; -.
DR   InParanoid; P40808; -.
DR   KO; K01581; -.
DR   OMA; PIVVKEF; -.
DR   OrthoDB; EOG73Z2T6; -.
DR   PhylomeDB; P40808; -.
DR   UniPathway; UPA00535; UER00288.
DR   GenomeRNAi; 35767; -.
DR   NextBio; 795123; -.
DR   Bgee; P40808; -.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IEA:UniProtKB-UniPathway.
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   ACT_SITE    343    343       Proton donor; shared with dimeric partner
FT                                (By similarity).
FT   MOD_RES      62     62       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   CONFLICT     94     94       L -> F (in Ref. 1; CAA47166).
FT   CONFLICT    143    143       N -> S (in Ref. 1; CAA47166).
FT   CONFLICT    241    241       E -> K (in Ref. 1; CAA47166).
FT   CONFLICT    346    346       M -> L (in Ref. 1; CAA47166).
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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