ID DCAM_ORYSJ Reviewed; 398 AA. AC Q0JC10; A2ZZV4; O24215; O81269; Q56CX9; Q7XU78; Q7XUL0; Q9SC65; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme; DE Short=AdoMetDC; DE Short=SAMDC; DE EC=4.1.1.50; DE Contains: DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain; DE Contains: DE RecName: Full=S-adenosylmethionine decarboxylase beta chain; DE Flags: Precursor; GN Name=SAMDC; OrderedLocusNames=Os04g0498600, LOC_Os04g42090; GN ORFNames=OSJNBa0029H02.4, OSJNBa0067K08.23, OsJ_004076; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Nipponbare; RX MEDLINE=21066059; PubMed=11139406; DOI=10.1042/0264-6021:3530403; RA Franceschetti M., Hanfrey C., Scaramagli S., Torrigiani P., Bagni N., RA Michael A.J.; RT "Characterization of monocot and dicot plant S-adenosyl-L-methionine RT decarboxylase gene families including identification in the mRNA of a RT highly conserved pair of upstream overlapping open reading frames."; RL Biochem. J. 353:403-409(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX MEDLINE=22337377; PubMed=12447439; DOI=10.1038/nature01183; RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., RA Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., RA Weng Q., Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., RA Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., RA Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., RA Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., RA Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., RA Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., RA Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., RA Han B.; RT "Sequence and analysis of rice chromosome 4."; RL Nature 420:316-320(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=17210932; DOI=10.1101/gr.5509507; RG The rice annotation project (RAP); RT "Curated genome annotation of Oryza sativa ssp. japonica and RT comparative genome analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5- CC adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2). CC -!- COFACTOR: Pyruvoyl group. CC -!- PATHWAY: Amine and polyamine biosynthesis; S- CC adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from CC S-adenosyl-L-methionine: step 1/1. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation CC of the active enzyme involves a self-maturation process in which CC the active site pyruvoyl group is generated from an internal CC serine residue via an autocatalytic post-translational CC modification. Two non-identical subunits are generated from the CC proenzyme in this reaction, and the pyruvate is formed at the N- CC terminus of the alpha chain, which is derived from the carboxyl CC end of the proenzyme. The post-translation cleavage follows an CC unusual pathway, termed non-hydrolytic serinolysis, in which the CC side chain hydroxyl group of the serine supplies its oxygen atom CC to form the C-terminus of the beta chain, while the remainder of CC the serine residue undergoes an oxidative deamination to produce CC ammonia and the pyruvoyl group blocking the N-terminus of the CC alpha chain (By similarity). CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. CC -!- SEQUENCE CAUTION: CC Sequence=CAD41510.3; Type=Erroneous gene model prediction; CC Sequence=EAZ14251.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y07766; CAA69074.2; -; mRNA. DR EMBL; AL606594; CAD41510.3; ALT_SEQ; Genomic_DNA. DR EMBL; AL606627; CAD41242.2; -; Genomic_DNA. DR EMBL; AP008210; BAF15127.1; -; Genomic_DNA. DR EMBL; CM000138; EAZ14251.1; ALT_SEQ; Genomic_DNA. DR PIR; T04099; T04099. DR RefSeq; NP_001053213.1; -. DR UniGene; Os.38386; -. DR UniGene; Os.4786; -. DR UniGene; Os.52749; -. DR HSSP; P17707; 1I72. DR GeneID; 4336294; -. DR KEGG; osa:4336294; -. DR Gramene; O24215; -. DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:EC. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro. DR InterPro; IPR001985; S-AdoMet_decarboxylase. DR InterPro; IPR018167; S-AdoMet_decarboxylase_sg. DR InterPro; IPR016067; S-AdoMet_deCO2ase_core. DR InterPro; IPR018166; S-AdoMet_deCO2ase_CS. DR Gene3D; G3DSA:3.60.90.10; SAM_decarbox; 1. DR PANTHER; PTHR11570; SAM_decarbox; 1. DR Pfam; PF01536; SAM_decarbox; 1. DR PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1. DR ProDom; PD002379; SAM_decarbox; 1. DR TIGRFAMs; TIGR00535; SAM_DCase; 1. DR PROSITE; PS01336; ADOMETDC; 1. PE 2: Evidence at transcript level; KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis; KW Pyruvate; S-adenosyl-L-methionine; Schiff base; KW Spermidine biosynthesis; Zymogen. FT CHAIN 1 77 S-adenosylmethionine decarboxylase beta FT chain (By similarity). FT /FTId=PRO_0000030017. FT CHAIN 78 398 S-adenosylmethionine decarboxylase alpha FT chain (By similarity). FT /FTId=PRO_0000030018. FT ACT_SITE 18 18 By similarity. FT ACT_SITE 21 21 By similarity. FT ACT_SITE 78 78 Schiff-base intermediate with substrate; FT via pyruvic acid (By similarity). FT ACT_SITE 92 92 Proton donor; for catalytic activity (By FT similarity). FT ACT_SITE 243 243 Proton acceptor; for processing activity FT (By similarity). FT ACT_SITE 256 256 Proton acceptor; for processing activity FT (By similarity). FT SITE 77 78 Cleavage (non-hydrolytic); by autolysis FT (By similarity). FT MOD_RES 78 78 Pyruvic acid (Ser); by autocatalysis (By FT similarity). SQ SEQUENCE 398 AA; 43283 MW; BC24F359962F8655 CRC64; MGVLSAADPP PVSAIGFEGY EKRLEITFSE APVFADPDGR GLRALSRAQI DSVLDLARCT IVSELSNKDF DSYVLSESSL FIYSDKIVIK TCGTTKLLLT IPRILELAEG LSMPLAAVKY SRGMFIFPSA QPAPHRSFSE EVAVLNRYFG HLKSGGNAYV IGDPAKPGQK WHIYYATQHP EQPMVTLEMC MTGLDKEKAS VFFKTSADGH TSCAKEMTKL SGISDIIPEM EICDFDFEPC GYSMNAIHGS AFSTIHVTPE DGFSYASYEV VGFDASTLAY GDLVKRVLRC FGPSEFSVAV TIFGGHGHAG TWAKELNADA YKCNNMVEQE LPCGGLLIYQ SFDATEDVPV AVGSPKSVLH CFEAENMVNP APVKEGKLGN LLPWGEDALE ENDGVFDE //