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 01-MAY-2013, entry version 95.
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;
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 -!- INTERACTION:
CC Q9W3F1:CG12116; NbExp=1; IntAct=EBI-178569, EBI-193758;
CC Q9VL02:nmd; NbExp=1; IntAct=EBI-178569, EBI-146380;
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 ProteinModelPortal; P40808; -.
DR SMR; P40808; 35-385.
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; HIGSAIR; -.
DR OrthoDB; EOG473N6V; -.
DR PhylomeDB; P40808; -.
DR UniPathway; UPA00535; UER00288.
DR GenomeRNAi; 35767; -.
DR NextBio; 795123; -.
DR Bgee; P40808; -.
DR GermOnline; CG8719; Drosophila melanogaster.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IEA:EC.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.40.37.10; -; 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 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; Racem_decarbox_C; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
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
//
