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S-adenosylmethionine decarboxylase proenzyme 1 (AdoMetDC1) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase 1 alpha chain; S-adenosylmethionine decarboxylase 1 beta chain]

 DCAM1_ARATH             Reviewed;         366 AA.
Q96286; B9DFT1; Q96531; Q9M893;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 2.
22-NOV-2017, entry version 138.
RecName: Full=S-adenosylmethionine decarboxylase proenzyme 1 {ECO:0000305};
Short=AdoMetDC1 {ECO:0000303|PubMed:11139406};
EC=4.1.1.50 {ECO:0000269|PubMed:10578049};
Contains:
RecName: Full=S-adenosylmethionine decarboxylase 1 alpha chain {ECO:0000250|UniProtKB:P17707};
Contains:
RecName: Full=S-adenosylmethionine decarboxylase 1 beta chain {ECO:0000250|UniProtKB:P17707};
Flags: Precursor;
Name=SAMDC1 {ECO:0000303|PubMed:16699540};
Synonyms=SAMDC {ECO:0000303|PubMed:11139406};
OrderedLocusNames=At3g02470; ORFNames=F16B3.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11139406; DOI=10.1042/0264-6021:3530403;
Franceschetti M., Hanfrey C., Scaramagli S., Torrigiani P., Bagni N.,
Michael A.J.;
"Characterization of monocot and dicot plant S-adenosyl-L-methionine
decarboxylase gene families including identification in the mRNA of a
highly conserved pair of upstream overlapping open reading frames.";
Biochem. J. 353:403-409(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Carrasco P., Marco F.;
"Arabidopsis S-adenosylmethionine decarboxylase.";
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[7]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
CYS-50; LYS-81; CYS-83 AND CYS-230.
PubMed=10578049; DOI=10.1093/oxfordjournals.jbchem.a022568;
Park S.J., Cho Y.D.;
"Identification of functionally important residues of Arabidopsis
thaliana S-adenosylmethionine decarboxylase.";
J. Biochem. 126:996-1003(1999).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND GENE FAMILY.
PubMed=16699540; DOI=10.1038/sj.cr.7310056;
Ge C., Cui X., Wang Y., Hu Y., Fu Z., Zhang D., Cheng Z., Li J.;
"BUD2, encoding an S-adenosylmethionine decarboxylase, is required for
Arabidopsis growth and development.";
Cell Res. 16:446-456(2006).
[9]
INDUCTION.
PubMed=20386573; DOI=10.1038/cr.2010.51;
Cui X., Ge C., Wang R., Wang H., Chen W., Fu Z., Jiang X., Li J.,
Wang Y.;
"The BUD2 mutation affects plant architecture through altering
cytokinin and auxin responses in Arabidopsis.";
Cell Res. 20:576-586(2010).
-!- FUNCTION: Essential for biosynthesis of the polyamines spermidine
and spermine. Essential for polyamine homeostasis, and normal
plant embryogenesis, growth and development.
{ECO:0000269|PubMed:16699540}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3-
(methylthio)propylamine + CO(2). {ECO:0000269|PubMed:10578049}.
-!- COFACTOR:
Name=pyruvate; Xref=ChEBI:CHEBI:15361;
Evidence={ECO:0000250|UniProtKB:P17707};
Note=Binds 1 pyruvoyl group covalently per subunit.
{ECO:0000250|UniProtKB:P17707};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=23.1 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:10578049};
pH dependence:
Optimum pH is 6.8-7.2. {ECO:0000269|PubMed:10578049};
-!- PATHWAY: Amine and polyamine biosynthesis; S-
adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
S-adenosyl-L-methionine: step 1/1. {ECO:0000305}.
-!- INDUCTION: Down-regulated by auxin. {ECO:0000269|PubMed:20386573}.
-!- PTM: Is synthesized initially as an inactive proenzyme. Formation
of the active enzyme involves a self-maturation process in which
the active site pyruvoyl group is generated from an internal
serine residue via an autocatalytic post-translational
modification. Two non-identical subunits are generated from the
proenzyme in this reaction, and the pyruvate is formed at the N-
terminus of the alpha chain, which is derived from the carboxyl
end of the proenzyme. The post-translation cleavage follows an
unusual pathway, termed non-hydrolytic serinolysis, in which the
side chain hydroxyl group of the serine supplies its oxygen atom
to form the C-terminus of the beta chain, while the remainder of
the serine residue undergoes an oxidative deamination to produce
ammonia and the pyruvoyl group blocking the N-terminus of the
alpha chain. {ECO:0000250|UniProtKB:P17707}.
-!- DISRUPTION PHENOTYPE: Reduction in the length of stem internodes.
Increased thickness of veins in leaves and inflorescence stems.
Altered morphology of xylem vessel elements. The double mutants of
bud2-1 and samdc1-1 are embryonic lethal.
{ECO:0000269|PubMed:16699540}.
-!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y07765; CAA69073.1; -; Genomic_DNA.
EMBL; U63633; AAB17665.1; -; mRNA.
EMBL; AC021640; AAF32454.1; -; Genomic_DNA.
EMBL; CP002686; AEE73812.1; -; Genomic_DNA.
EMBL; CP002686; AEE73813.1; -; Genomic_DNA.
EMBL; CP002686; AEE73814.1; -; Genomic_DNA.
EMBL; AF428468; AAL16237.1; -; mRNA.
EMBL; AY042824; AAK68764.1; -; mRNA.
EMBL; AY081446; AAM10008.1; -; mRNA.
EMBL; AK316891; BAH19598.1; -; mRNA.
RefSeq; NP_001078093.1; NM_001084624.1.
RefSeq; NP_001154585.1; NM_001161113.1.
RefSeq; NP_186896.1; NM_111114.2.
UniGene; At.25574; -.
UniGene; At.69373; -.
UniGene; At.72938; -.
ProteinModelPortal; Q96286; -.
SMR; Q96286; -.
BioGrid; 6547; 2.
IntAct; Q96286; 1.
STRING; 3702.AT3G02470.1; -.
PaxDb; Q96286; -.
EnsemblPlants; AT3G02470.1; AT3G02470.1; AT3G02470.
EnsemblPlants; AT3G02470.3; AT3G02470.3; AT3G02470.
EnsemblPlants; AT3G02470.4; AT3G02470.4; AT3G02470.
GeneID; 821214; -.
Gramene; AT3G02470.1; AT3G02470.1; AT3G02470.
Gramene; AT3G02470.3; AT3G02470.3; AT3G02470.
Gramene; AT3G02470.4; AT3G02470.4; AT3G02470.
KEGG; ath:AT3G02470; -.
Araport; AT3G02470; -.
TAIR; locus:2076834; AT3G02470.
eggNOG; KOG0788; Eukaryota.
eggNOG; ENOG410XRN0; LUCA.
HOGENOM; HOG000159915; -.
InParanoid; Q96286; -.
KO; K01611; -.
OMA; AVYGLEM; -.
OrthoDB; EOG09360IDC; -.
PhylomeDB; Q96286; -.
BRENDA; 4.1.1.50; 399.
Reactome; R-ATH-351202; Metabolism of polyamines.
SABIO-RK; Q96286; -.
UniPathway; UPA00331; UER00451.
PRO; PR:Q96286; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q96286; baseline and differential.
Genevisible; Q96286; AT.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:TAIR.
GO; GO:0016458; P:gene silencing; IMP:TAIR.
GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
GO; GO:0006596; P:polyamine biosynthetic process; TAS:TAIR.
GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008295; P:spermidine biosynthetic process; IMP:UniProtKB.
GO; GO:0006597; P:spermine biosynthetic process; IMP:UniProtKB.
GO; GO:0019079; P:viral genome replication; IMP:TAIR.
Gene3D; 3.60.90.10; -; 1.
InterPro; IPR001985; S-AdoMet_decarboxylase.
InterPro; IPR016067; S-AdoMet_deCO2ase_core.
InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
PANTHER; PTHR11570; PTHR11570; 1.
Pfam; PF01536; SAM_decarbox; 1.
PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
SUPFAM; SSF56276; SSF56276; 1.
TIGRFAMs; TIGR00535; SAM_DCase; 1.
PROSITE; PS01336; ADOMETDC; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Complete proteome; Decarboxylase; Lyase;
Polyamine biosynthesis; Pyruvate; Reference proteome;
S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
Zymogen.
CHAIN 1 68 S-adenosylmethionine decarboxylase 1 beta
chain. {ECO:0000250|UniProtKB:P17707}.
/FTId=PRO_0000029987.
CHAIN 69 366 S-adenosylmethionine decarboxylase 1
alpha chain.
{ECO:0000250|UniProtKB:P17707}.
/FTId=PRO_0000029988.
ACT_SITE 9 9 {ECO:0000250|UniProtKB:P17707}.
ACT_SITE 12 12 {ECO:0000250|UniProtKB:P17707}.
ACT_SITE 69 69 Schiff-base intermediate with substrate;
via pyruvic acid.
{ECO:0000250|UniProtKB:P17707}.
ACT_SITE 83 83 Proton donor; for catalytic activity.
{ECO:0000250|UniProtKB:P17707}.
ACT_SITE 233 233 Proton acceptor; for processing activity.
{ECO:0000250|UniProtKB:P17707}.
ACT_SITE 246 246 Proton acceptor; for processing activity.
{ECO:0000250|UniProtKB:P17707}.
BINDING 68 68 Substrate.
{ECO:0000250|UniProtKB:P17707}.
BINDING 250 250 Substrate.
{ECO:0000250|UniProtKB:P17707}.
SITE 68 69 Cleavage (non-hydrolytic); by autolysis.
{ECO:0000250|UniProtKB:P17707}.
MOD_RES 69 69 Pyruvic acid (Ser); by autocatalysis.
{ECO:0000250|UniProtKB:P17707}.
MUTAGEN 50 50 C->A: Slightly reduces activity.
{ECO:0000269|PubMed:10578049}.
MUTAGEN 81 81 K->A: Reduces activity 2-fold. Increases
substrate specificity for lysine 6-fold.
{ECO:0000269|PubMed:10578049}.
MUTAGEN 83 83 C->A: Reduces activity 10-fold.
{ECO:0000269|PubMed:10578049}.
MUTAGEN 230 230 C->A: Slightly reduces activity.
{ECO:0000269|PubMed:10578049}.
CONFLICT 123 123 P -> L (in Ref. 1; CAA69073).
{ECO:0000305}.
CONFLICT 150 150 Y -> T (in Ref. 2; AAB17665).
{ECO:0000305}.
CONFLICT 216 216 I -> N (in Ref. 2; AAB17665).
{ECO:0000305}.
CONFLICT 245 245 I -> N (in Ref. 2; AAB17665).
{ECO:0000305}.
SEQUENCE 366 AA; 40403 MW; 7E416C3E42BA804E CRC64;
MALSAIGFEG YEKRLEVTFF EPSIFQDSKG LGLRALTKSQ LDEILTPAAC TIVSSLSNDQ
LDSYVLSESS FFVYPYKVII KTCGTTKLLL SIPPLLKLAG ELSLSVKSVK YTRGSFLCPG
GQPFPHRSFS EEVSVLDGHF TQLGLNSVAY LMGNDDETKK WHVYAASAQD SSNCNNNVYT
LEMCMTGLDR EKAAVFYKDE ADKTGSMTDN SGIRKILPKS EICDFEFEPC GYSMNSIEGD
AISTIHVTPE DGFSYASFEA VGYDFNTLDL SQLVTRVLSC FEPKQFSVAV HSSVGANSYK
PEITVDLEDY GCRERTFESL GEESGTVMYQ TFEKLGKYCG SPRSTLKCEW SSNNSCSSED
EKDEGI


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