DCAM4_ARATH
ID DCAM4_ARATH Reviewed; 347 AA.
AC Q3E9D5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme 4 {ECO:0000305};
DE Short=AdoMetDC4 {ECO:0000305};
DE EC=4.1.1.50 {ECO:0000269|PubMed:16699540};
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 AltName: Full=Protein BUSHY AND DWARF 2 {ECO:0000303|PubMed:16699540};
DE Flags: Precursor;
GN Name=SAMDC4 {ECO:0000303|PubMed:16699540};
GN Synonyms=BUD2 {ECO:0000303|PubMed:16699540};
GN OrderedLocusNames=At5g18930 {ECO:0000312|Araport:AT5G18930};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
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 INDUCTION BY AUXIN, AND DISRUPTION PHENOTYPE.
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:16699540};
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 -!- INTERACTION:
CC Q3E9D5; P11035: NIA2; NbExp=5; IntAct=EBI-25512418, EBI-4451150;
CC Q3E9D5; P29448: TRX1; NbExp=3; IntAct=EBI-25512418, EBI-8519814;
CC Q3E9D5; Q38879: TRX2; NbExp=3; IntAct=EBI-25512418, EBI-727983;
CC Q3E9D5; Q9C9Y6: TRX9; NbExp=3; IntAct=EBI-25512418, EBI-4466064;
CC -!- INDUCTION: 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 (By similarity). {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. Altered homeostasis of polyamines.
CC Hyposensitivity to auxin and hypersensitivity to cytokinin. The double
CC mutants of bud2-1 and samdc1-1 are embryonic lethal.
CC {ECO:0000269|PubMed:16699540, ECO:0000269|PubMed:20386573}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; DQ217414; ABB20589.1; -; mRNA.
DR EMBL; AC068655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92629.1; -; Genomic_DNA.
DR RefSeq; NP_197394.1; NM_121898.3.
DR AlphaFoldDB; Q3E9D5; -.
DR SMR; Q3E9D5; -.
DR BioGRID; 17287; 4.
DR IntAct; Q3E9D5; 4.
DR STRING; 3702.AT5G18930.1; -.
DR PaxDb; Q3E9D5; -.
DR PRIDE; Q3E9D5; -.
DR ProteomicsDB; 222196; -.
DR EnsemblPlants; AT5G18930.1; AT5G18930.1; AT5G18930.
DR GeneID; 832011; -.
DR Gramene; AT5G18930.1; AT5G18930.1; AT5G18930.
DR KEGG; ath:AT5G18930; -.
DR Araport; AT5G18930; -.
DR TAIR; locus:2144985; AT5G18930.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_1_0_1; -.
DR InParanoid; Q3E9D5; -.
DR OMA; LEIWFEE; -.
DR OrthoDB; 932490at2759; -.
DR PhylomeDB; Q3E9D5; -.
DR BioCyc; ARA:AT5G18930-MON; -.
DR BRENDA; 4.1.1.50; 399.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:Q3E9D5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E9D5; baseline and differential.
DR Genevisible; Q3E9D5; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
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 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 Decarboxylase; Lyase; Polyamine biosynthesis; Pyruvate; Reference proteome;
KW S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT CHAIN 1..66
FT /note="S-adenosylmethionine decarboxylase 1 beta chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000430962"
FT CHAIN 67..347
FT /note="S-adenosylmethionine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT /id="PRO_0000430963"
FT ACT_SITE 7
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 10
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 67
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 81
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 237
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 250
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT SITE 66..67
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT MOD_RES 67
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
SQ SEQUENCE 347 AA; 39039 MW; CFC991E8A37817C7 CRC64;
MAVSGFEGFE KRLELRFFDD DKPITKNPMG LRLIDFESLD QVLNEVQCTV VSAVANRSFD
AYVLSESSLF VYPTKIIIKT CGTTQLLKSI RPLIHLARNL GLTLRACRYS RGSFIFPKAQ
PFPYTSFKDE VIVVEESLPK SLCYRKASVM TPSNNPSRAW HVFTASADVE SDEHVVVVEV
CMTELDRVNA RSFFKRKGDE KNNSDSAGKE MTRLSGIDNI NANAYICDFA FDPCGYSMNG
VDGDRYSTIH VTPEDGFSYA SFECGLSLYD NGHEDISEVL SRAIDVFRPS DVSIATTYGG
EDYNHEVTKR VERVLAKKLD LKCRSRLMDE FPGSGTVVYQ SFTPRRK
