DCAM2_ARATH
ID DCAM2_ARATH Reviewed; 362 AA.
AC Q9S7T9;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme 2 {ECO:0000305};
DE Short=AdoMetDC2 {ECO:0000303|PubMed:11139406};
DE EC=4.1.1.50 {ECO:0000250|UniProtKB:Q96286};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 2 alpha chain {ECO:0000250|UniProtKB:P17707};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 2 beta chain {ECO:0000250|UniProtKB:P17707};
DE Flags: Precursor;
GN Name=SAMDC2 {ECO:0000303|PubMed:16699540}; OrderedLocusNames=At5g15950;
GN ORFNames=F1N13.90;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX 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. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY.
RX PubMed=16699540; DOI=10.1038/sj.cr.7310056;
RA Ge C., Cui X., Wang Y., Hu Y., Fu Z., Zhang D., Cheng Z., Li J.;
RT "BUD2, encoding an S-adenosylmethionine decarboxylase, is required for
RT Arabidopsis growth and development.";
RL Cell Res. 16:446-456(2006).
RN [6]
RP INDUCTION BY PLASMODIOPHORA BRASSICAE INFECTION.
RX PubMed=18305204; DOI=10.1104/pp.108.117432;
RA Jubault M., Hamon C., Gravot A., Lariagon C., Delourme R., Bouchereau A.,
RA Manzanares-Dauleux M.J.;
RT "Differential regulation of root arginine catabolism and polyamine
RT metabolism in clubroot-susceptible and partially resistant Arabidopsis
RT genotypes.";
RL Plant Physiol. 146:2008-2019(2008).
RN [7]
RP INDUCTION BY AUXIN.
RX PubMed=20386573; DOI=10.1038/cr.2010.51;
RA Cui X., Ge C., Wang R., Wang H., Chen W., Fu Z., Jiang X., Li J., Wang Y.;
RT "The BUD2 mutation affects plant architecture through altering cytokinin
RT and auxin responses in Arabidopsis.";
RL Cell Res. 20:576-586(2010).
CC -!- FUNCTION: Essential for biosynthesis of the polyamines spermidine and
CC spermine. Essential for polyamine homeostasis, and normal plant
CC embryogenesis, growth and development. {ECO:0000250|UniProtKB:Q96286}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
CC (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50;
CC Evidence={ECO:0000250|UniProtKB:Q96286};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000250|UniProtKB:P17707};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000250|UniProtKB:P17707};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1. {ECO:0000305}.
CC -!- INDUCTION: By auxin (PubMed:20386573) and infection by Plasmodiophora
CC brassicae (PubMed:18305204). {ECO:0000269|PubMed:18305204,
CC ECO:0000269|PubMed:20386573}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The post-translation
CC cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC in which the side chain hydroxyl group of the serine supplies its
CC oxygen atom to form the C-terminus of the beta chain, while the
CC remainder of the serine residue undergoes an oxidative deamination to
CC produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC alpha chain (By similarity). {ECO:0000250|UniProtKB:P17707}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; AJ252212; CAB64672.1; -; Genomic_DNA.
DR EMBL; AJ251915; CAB63805.1; -; mRNA.
DR EMBL; AL391145; CAC01794.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92227.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92228.1; -; Genomic_DNA.
DR EMBL; AF436825; AAL32007.1; -; mRNA.
DR EMBL; AY066030; AAL47397.1; -; mRNA.
DR PIR; T51378; T51378.
DR RefSeq; NP_001031888.1; NM_001036811.1.
DR RefSeq; NP_197099.1; NM_121600.3.
DR AlphaFoldDB; Q9S7T9; -.
DR SMR; Q9S7T9; -.
DR BioGRID; 16728; 1.
DR STRING; 3702.AT5G15950.2; -.
DR PaxDb; Q9S7T9; -.
DR PRIDE; Q9S7T9; -.
DR EnsemblPlants; AT5G15950.1; AT5G15950.1; AT5G15950.
DR EnsemblPlants; AT5G15950.2; AT5G15950.2; AT5G15950.
DR GeneID; 831452; -.
DR Gramene; AT5G15950.1; AT5G15950.1; AT5G15950.
DR Gramene; AT5G15950.2; AT5G15950.2; AT5G15950.
DR KEGG; ath:AT5G15950; -.
DR Araport; AT5G15950; -.
DR TAIR; locus:2146132; AT5G15950.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_2_1_1; -.
DR InParanoid; Q9S7T9; -.
DR OMA; LPKSHVD; -.
DR OrthoDB; 932490at2759; -.
DR PhylomeDB; Q9S7T9; -.
DR BioCyc; ARA:AT5G15950-MON; -.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:Q9S7T9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7T9; baseline and differential.
DR Genevisible; Q9S7T9; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006597; P:spermine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001985; S-AdoMet_decarboxylase.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR PANTHER; PTHR11570; PTHR11570; 1.
DR Pfam; PF01536; SAM_decarbox; 1.
DR PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR SUPFAM; SSF56276; SSF56276; 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; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..68
FT /note="S-adenosylmethionine decarboxylase 2 beta chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000029989"
FT CHAIN 69..362
FT /note="S-adenosylmethionine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000029990"
FT ACT_SITE 9
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 12
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 69
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 83
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 232
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 245
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT SITE 68..69
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT MOD_RES 69
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
SQ SEQUENCE 362 AA; 40010 MW; 49FFC5DF5AFA59B5 CRC64;
MAMSAIGFEG YEKRLEVTFF EPGLFLDTQG KGLRALAKSQ IDEILQPAEC TIVSSLSNDQ
LDSYVLSESS LFIFPYKIVI KTCGTTKLLL SIEPLLRLAG ELSLDVKAVR YTRGSFLCPG
GQPFPHRNFS EEVSVLDGHF AKLGLSSVAY LMGNDDETKK WHVYSASSAN SNNKNNVYTL
EMCMTGLDKD KASVFYKNES SSAGSMTDNS GIRKILPQSQ ICDFEFEPCG YSMNSIEGDA
ISTIHVTPED GFSYASFEAV GYDFTTMDLS HLVSKVLTCF KPKQFSVAVH STVAQKSYDS
GLSVDLDDYG CKESTMESLG EERGTVMYQR FEKLGRYCGS PRSTLKCEWS SNSSCNSEDE
KE
