DCAM1_ARATH
ID DCAM1_ARATH Reviewed; 366 AA.
AC Q96286; B9DFT1; Q96531; Q9M893;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme 1 {ECO:0000305};
DE Short=AdoMetDC1 {ECO:0000303|PubMed:11139406};
DE EC=4.1.1.50 {ECO:0000269|PubMed:10578049};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 1 alpha chain {ECO:0000250|UniProtKB:P17707};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 1 beta chain {ECO:0000250|UniProtKB:P17707};
DE Flags: Precursor;
GN Name=SAMDC1 {ECO:0000303|PubMed:16699540};
GN Synonyms=SAMDC {ECO:0000303|PubMed:11139406}; OrderedLocusNames=At3g02470;
GN ORFNames=F16B3.10;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Carrasco P., Marco F.;
RT "Arabidopsis S-adenosylmethionine decarboxylase.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP CYS-50; LYS-81; CYS-83 AND CYS-230.
RX PubMed=10578049; DOI=10.1093/oxfordjournals.jbchem.a022568;
RA Park S.J., Cho Y.D.;
RT "Identification of functionally important residues of Arabidopsis thaliana
RT S-adenosylmethionine decarboxylase.";
RL J. Biochem. 126:996-1003(1999).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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 [9]
RP INDUCTION.
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:0000269|PubMed:16699540}.
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:0000269|PubMed:10578049};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.1 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:10578049};
CC pH dependence:
CC Optimum pH is 6.8-7.2. {ECO:0000269|PubMed:10578049};
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: Down-regulated by auxin. {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. {ECO:0000250|UniProtKB:P17707}.
CC -!- DISRUPTION PHENOTYPE: Reduction in the length of stem internodes.
CC Increased thickness of veins in leaves and inflorescence stems. Altered
CC morphology of xylem vessel elements. The double mutants of bud2-1 and
CC samdc1-1 are embryonic lethal. {ECO:0000269|PubMed:16699540}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y07765; CAA69073.1; -; Genomic_DNA.
DR EMBL; U63633; AAB17665.1; -; mRNA.
DR EMBL; AC021640; AAF32454.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73812.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73813.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73814.1; -; Genomic_DNA.
DR EMBL; AF428468; AAL16237.1; -; mRNA.
DR EMBL; AY042824; AAK68764.1; -; mRNA.
DR EMBL; AY081446; AAM10008.1; -; mRNA.
DR EMBL; AK316891; BAH19598.1; -; mRNA.
DR RefSeq; NP_001078093.1; NM_001084624.1.
DR RefSeq; NP_001154585.1; NM_001161113.1.
DR RefSeq; NP_186896.1; NM_111114.2.
DR AlphaFoldDB; Q96286; -.
DR SMR; Q96286; -.
DR BioGRID; 6547; 2.
DR IntAct; Q96286; 1.
DR STRING; 3702.AT3G02470.1; -.
DR PaxDb; Q96286; -.
DR PRIDE; Q96286; -.
DR ProteomicsDB; 224680; -.
DR EnsemblPlants; AT3G02470.1; AT3G02470.1; AT3G02470.
DR EnsemblPlants; AT3G02470.3; AT3G02470.3; AT3G02470.
DR EnsemblPlants; AT3G02470.4; AT3G02470.4; AT3G02470.
DR GeneID; 821214; -.
DR Gramene; AT3G02470.1; AT3G02470.1; AT3G02470.
DR Gramene; AT3G02470.3; AT3G02470.3; AT3G02470.
DR Gramene; AT3G02470.4; AT3G02470.4; AT3G02470.
DR KEGG; ath:AT3G02470; -.
DR Araport; AT3G02470; -.
DR TAIR; locus:2076834; AT3G02470.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_2_1_1; -.
DR InParanoid; Q96286; -.
DR OMA; AIGFEGC; -.
DR OrthoDB; 932490at2759; -.
DR PhylomeDB; Q96286; -.
DR BRENDA; 4.1.1.50; 399.
DR SABIO-RK; Q96286; -.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:Q96286; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96286; baseline and differential.
DR Genevisible; Q96286; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:TAIR.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; TAS:TAIR.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006597; P:spermine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019079; P:viral genome replication; IMP:TAIR.
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 1: Evidence at protein 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 1 beta chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000029987"
FT CHAIN 69..366
FT /note="S-adenosylmethionine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000029988"
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 233
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 246
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 250
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"
FT MUTAGEN 50
FT /note="C->A: Slightly reduces activity."
FT /evidence="ECO:0000269|PubMed:10578049"
FT MUTAGEN 81
FT /note="K->A: Reduces activity 2-fold. Increases substrate
FT specificity for lysine 6-fold."
FT /evidence="ECO:0000269|PubMed:10578049"
FT MUTAGEN 83
FT /note="C->A: Reduces activity 10-fold."
FT /evidence="ECO:0000269|PubMed:10578049"
FT MUTAGEN 230
FT /note="C->A: Slightly reduces activity."
FT /evidence="ECO:0000269|PubMed:10578049"
FT CONFLICT 123
FT /note="P -> L (in Ref. 1; CAA69073)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Y -> T (in Ref. 2; AAB17665)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="I -> N (in Ref. 2; AAB17665)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="I -> N (in Ref. 2; AAB17665)"
FT /evidence="ECO:0000305"
SQ 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
