DCAM_SOLTU
ID DCAM_SOLTU Reviewed; 360 AA.
AC Q04694;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50;
DE AltName: Full=Induced stolen tip protein TUB13;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE Flags: Precursor;
GN Name=SAMDC; Synonyms=TUB13;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Record; TISSUE=Stolon tip;
RX PubMed=1450379; DOI=10.1007/bf00046449;
RA Taylor M.A., Mad Arif S.A., Kumar A., Davies H.V., Scobie L.A.,
RA Pearce S.R., Flavell A.J.;
RT "Expression and sequence analysis of cDNAs induced during the early stages
RT of tuberisation in different organs of the potato plant (Solanum tuberosum
RT L.).";
RL Plant Mol. Biol. 20:641-651(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Desiree;
RX PubMed=7948879; DOI=10.1007/bf00039543;
RA Mad Arif S.A., Taylor M.A., George L.A., Butler A.R., Burch L.R.,
RA Davies H.V., Stark M.J., Kumar A.;
RT "Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of
RT potato.";
RL Plant Mol. Biol. 26:327-338(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND PYRUVATE FORMATION AT SER-73.
RX PubMed=12463749; DOI=10.1021/bi026710u;
RA Bennett E.M., Ekstrom J.L., Pegg A.E., Ealick S.E.;
RT "Monomeric S-adenosylmethionine decarboxylase from plants provides an
RT alternative to putrescine stimulation.";
RL Biochemistry 41:14509-14517(2002).
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 -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Note=Binds 1 pyruvoyl group covalently per subunit.;
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1.
CC -!- TISSUE SPECIFICITY: Stolon, also expressed in leaves, stems and roots.
CC {ECO:0000269|PubMed:1450379}.
CC -!- DEVELOPMENTAL STAGE: Transcribed in the stolon tip during the early
CC stages of tuberization. Maximum expression was in non-swelling stolon
CC tips from stage b, and level declined as the tuber increased in size.
CC {ECO:0000269|PubMed:1450379}.
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}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; Z11680; CAA77742.1; -; mRNA.
DR EMBL; S74514; AAB32507.1; -; Genomic_DNA.
DR PIR; S52662; S52662.
DR RefSeq; NP_001306788.1; NM_001319859.1.
DR PDB; 1MHM; X-ray; 2.30 A; A=73-360, B=1-72.
DR PDBsum; 1MHM; -.
DR AlphaFoldDB; Q04694; -.
DR SMR; Q04694; -.
DR STRING; 4113.PGSC0003DMT400019451; -.
DR GeneID; 102601725; -.
DR KEGG; sot:102601725; -.
DR eggNOG; KOG0788; Eukaryota.
DR InParanoid; Q04694; -.
DR BRENDA; 4.1.1.50; 5757.
DR UniPathway; UPA00331; UER00451.
DR EvolutionaryTrace; Q04694; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q04694; baseline.
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 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Decarboxylase; Lyase;
KW Polyamine biosynthesis; Pyruvate; Reference proteome;
KW S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT CHAIN 1..72
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000030023"
FT CHAIN 73..360
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000030024"
FT ACT_SITE 13
FT ACT_SITE 16
FT ACT_SITE 73
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 87
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 249
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 72..73
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT MOD_RES 73
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12463749"
FT CONFLICT 174
FT /note="S -> P (in Ref. 2; AAB32507)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="T -> S (in Ref. 2; AAB32507)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="V -> I (in Ref. 2; AAB32507)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="I -> T (in Ref. 2; AAB32507)"
FT /evidence="ECO:0000305"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1MHM"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:1MHM"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1MHM"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:1MHM"
SQ SEQUENCE 360 AA; 39726 MW; EE8165FA54814B46 CRC64;
MEMDLPVSAI GFEGFEKRLE ISFVEPGLFA DPNGKGLRSL SKAQLDEILG PAECTIVDNL
SNDYVDSYVL SESSLFVYSY KIIIKTCGTT KLLLAIPPIL RLAETLSLKV QDVRYTRGSF
IFPGAQSFPH RHFSEEVAVL DGYFGKLAAG SKAVIMGSPD KTQKWHVYSA SAGSVQSNDP
VYTLEMCMTG LDREKASVFY KTEESSAAHM TVRSGIRKIL PKSEICDFEF EPCGYSMNSI
EGAAVSTIHI TPEDGFTYAS FESVGYNPKT MELGPLVERV LACFEPAEFS VALHADVATK
LLERICSVDV KGYSLAEWSP EEFGEGGSIV YQKFTRTPYC ESPKSVLKGC WKEEEKEGKE
