DCAM3_ARATH
ID DCAM3_ARATH Reviewed; 349 AA.
AC Q9LSU6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme 3 {ECO:0000305};
DE Short=AdoMetDC3 {ECO:0000305};
DE EC=4.1.1.50 {ECO:0000250|UniProtKB:Q96286};
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};
GN Name=SAMDC3 {ECO:0000303|PubMed:16699540};
GN OrderedLocusNames=At3g25570 {ECO:0000312|Araport:AT3G25570};
GN ORFNames=MWL2.23 {ECO:0000312|EMBL:BAB01327.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
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 -!- 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 -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; AB025639; BAB01327.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77029.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77030.1; -; Genomic_DNA.
DR EMBL; BT012654; AAT06473.1; -; mRNA.
DR RefSeq; NP_001189972.1; NM_001203043.1.
DR RefSeq; NP_189184.1; NM_113454.3.
DR AlphaFoldDB; Q9LSU6; -.
DR SMR; Q9LSU6; -.
DR STRING; 3702.AT3G25570.2; -.
DR PaxDb; Q9LSU6; -.
DR PRIDE; Q9LSU6; -.
DR ProteomicsDB; 224585; -.
DR EnsemblPlants; AT3G25570.1; AT3G25570.1; AT3G25570.
DR EnsemblPlants; AT3G25570.2; AT3G25570.2; AT3G25570.
DR GeneID; 822144; -.
DR Gramene; AT3G25570.1; AT3G25570.1; AT3G25570.
DR Gramene; AT3G25570.2; AT3G25570.2; AT3G25570.
DR KEGG; ath:AT3G25570; -.
DR Araport; AT3G25570; -.
DR TAIR; locus:2094473; AT3G25570.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_2_1_1; -.
DR InParanoid; Q9LSU6; -.
DR OMA; CYQRKNE; -.
DR OrthoDB; 932490at2759; -.
DR PhylomeDB; Q9LSU6; -.
DR BioCyc; ARA:AT3G25570-MON; -.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:Q9LSU6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSU6; baseline and differential.
DR Genevisible; Q9LSU6; 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 Decarboxylase; Lyase; Polyamine biosynthesis; Pyruvate; Reference proteome;
KW S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT CHAIN 1..68
FT /note="S-adenosylmethionine decarboxylase 1 beta chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000430960"
FT CHAIN 69..349
FT /note="S-adenosylmethionine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000430961"
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 235
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 248
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 252
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 349 AA; 38290 MW; 77F78A658A7B666E CRC64;
MAVSATGFEG FEKRLEISFF ETTDFLDPQG KSLRSLTKSQ LDEILTPAEC TIVSSLTNSF
VDSYVLSESS LFVYPYKIII KTCGTTKLLL SIPHILRLAD SLCLTVKSVR YTRGSFIFPG
AQSYPHRSFS EEVALLDDYF GKLNAGSKAF VMGGSDNNPQ RWHVYSASST EESAVCDKPV
YTLEMCMTGL DNIKASVFFK TNSVSASEMT ISSGIRNILP GSEICDFNFE PCGYSMNSIE
GDAVSTIHVT PEDGFSYASF ETVGYDLKAL NFKELVDRVL VCFGPEEFSV AVHANLGTEV
LASDCVADVN GYFSQERELE ELGLGGSVLY QRFVKTVECC SPKSTLGFC
