DCAM_ORYSI
ID DCAM_ORYSI Reviewed; 398 AA.
AC A2XV58; O24215; O81269; Q56CX9; Q7XU78; Q7XUL0; Q9SC65;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50;
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; ORFNames=OsI_015951;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX AGRICOLA=IND22302496; DOI=10.1007/s001220051352;
RA Li Z.Y., Chen S.Y.;
RT "Differential accumulation of S-adenosylmethionine decarboxylase transcript
RT in rice seedlings in response to salt and drought stresses.";
RL Theor. Appl. Genet. 100:782-788(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Pokkali; TISSUE=Root;
RA Laha S., Majumder G., Sengupta D.N.;
RT "cDNA of S-adenosylmethionine decarboxylase from Oryza sativa var.
RT pokkali.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAY94718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF067194; AAC79990.1; -; mRNA.
DR EMBL; AJ252213; CAB64671.1; -; Genomic_DNA.
DR EMBL; AY966487; AAX76987.1; -; mRNA.
DR EMBL; CM000129; EAY94718.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2XV58; -.
DR SMR; A2XV58; -.
DR STRING; 39946.A2XV58; -.
DR HOGENOM; CLU_023050_2_0_1; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
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 Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..77
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000302051"
FT CHAIN 78..398
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000302052"
FT ACT_SITE 18
FT /evidence="ECO:0000250"
FT ACT_SITE 21
FT /evidence="ECO:0000250"
FT ACT_SITE 78
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 243
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 77..78
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 78
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="V -> D (in Ref. 3; AAX76987)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="K -> R (in Ref. 2; CAB64671)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="N -> Y (in Ref. 3; AAX76987)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="F -> L (in Ref. 3; AAX76987)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> T (in Ref. 3; AAX76987)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="G -> R (in Ref. 3; AAX76987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 43309 MW; 1324EDA871B2AF39 CRC64;
MGVLSAADPP PVSAIGFEGY EKRLEITFSE APVFADPDGR GLRALSRAQI DSVLDLARCT
IVSELSNKDF DSYVLSESSL FIYSDKIVIK TCGTTKLLLT IPRILELAEG LSMPLAAVKY
SRGMFIFPSA QPAPHRSFSE EVAVLNRYFG HLKSGGNAYV IGDPAKPGQK WHIYYATQHP
EQPMVTLEMC MTGLDKEKAS VFFKTSADGH TSCAKEMTKL SGISDIIPEM EICDFDFEPC
GYSMNAIHGL AFSTIHVTPE DGFSYASYEV VGFDASTLAY GDLVKRVLRC FGPSEFSVAV
TIFGGHGHAG TWAKELNADA YKCNNMVEQE LPCGGLLIYQ SFDATEDVPV AVGSPKSVLH
CFEAENMVNP APVKEGKLGN LLPWGEDALE ENDGVFDE
