DCAM_SCHPO
ID DCAM_SCHPO Reviewed; 378 AA.
AC Q9P7E3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 145.
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=spe2; ORFNames=SPBP4H10.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11283013; DOI=10.1074/jbc.m010643200;
RA Chattopadhyay M.K., Murakami Y., Matsufuji S.;
RT "Antizyme regulates the degradation of ornithine decarboxylase in fission
RT yeast Schizosaccharomyces pombe. Study in the spe2 knockout strains.";
RL J. Biol. Chem. 276:21235-21241(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(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; Evidence={ECO:0000250};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250};
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}.
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DR EMBL; AB045111; BAB12576.1; -; Genomic_DNA.
DR EMBL; AB045110; BAB12575.1; -; mRNA.
DR EMBL; CU329671; CAB83163.1; -; Genomic_DNA.
DR RefSeq; NP_596179.1; NM_001022098.2.
DR AlphaFoldDB; Q9P7E3; -.
DR SMR; Q9P7E3; -.
DR BioGRID; 277849; 3.
DR STRING; 4896.SPBP4H10.05c.1; -.
DR iPTMnet; Q9P7E3; -.
DR MaxQB; Q9P7E3; -.
DR PaxDb; Q9P7E3; -.
DR EnsemblFungi; SPBP4H10.05c.1; SPBP4H10.05c.1:pep; SPBP4H10.05c.
DR GeneID; 2541338; -.
DR KEGG; spo:SPBP4H10.05c; -.
DR PomBase; SPBP4H10.05c; spe2.
DR VEuPathDB; FungiDB:SPBP4H10.05c; -.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_0_1_1; -.
DR InParanoid; Q9P7E3; -.
DR OMA; LEIWFEE; -.
DR PhylomeDB; Q9P7E3; -.
DR Reactome; R-SPO-351202; Metabolism of polyamines.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:Q9P7E3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; ISO:PomBase.
DR GO; GO:0015940; P:pantothenate biosynthetic process; ISO:PomBase.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:PomBase.
DR GO; GO:0006597; P:spermine biosynthetic process; IMP:PomBase.
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..84
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030031"
FT CHAIN 85..378
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030032"
FT ACT_SITE 21
FT /evidence="ECO:0000250"
FT ACT_SITE 24
FT /evidence="ECO:0000250"
FT ACT_SITE 85
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 99
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 84..85
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT MOD_RES 85
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 42712 MW; 10AEA8B3DAF62894 CRC64;
MSPTLVVDQE NSEEFNTSSF EGPEKLLELW FSAPIKTNLS AGEKANLGLK AVSRNDWDDM
LAQAQCKVLS VVNSEEIDAY LLSESSMFVF AHKIILKTCG TTTLLASLPR LLEIASSVGF
DRPLRIFYSR KNFLYPERQL APHTSWEEEV RYLQLFFPSG CSYVVGPTNK NHWHLFSDLA
DDYSLLEDSL DPEDETLEVL MTDMSPERSL QFYAPSLDVV RSARGDDYVR EKNNLSGGHI
LGSYVADESG VRDLCSTSDK KAVLDAFQFE PIGFSSNMIY KDRYATIHVT PQEHCSYASF
ETNVSQFQFG RSISETIEKT VKTFGANKFC LTLFQAKGAS QEKHFSAKLK SFSSYKREEF
IVYDFPGYDL IFASFTAV
