DCAM_DICDI
ID DCAM_DICDI Reviewed; 379 AA.
AC Q8T1E3; B0M0Q1; Q553L2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 25-MAY-2022, entry version 116.
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=amd1; ORFNames=DDB_G0275567;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: S-adenosylmethionine decarboxylase is essential for the
CC biosynthesis of spermine and spermidine. The alpha subunit contains the
CC active site (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000250}.
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; AAFI02000013; EAL69534.2; -; Genomic_DNA.
DR RefSeq; XP_643401.2; XM_638309.2.
DR AlphaFoldDB; Q8T1E3; -.
DR SMR; Q8T1E3; -.
DR STRING; 44689.DDB0237590; -.
DR PaxDb; Q8T1E3; -.
DR EnsemblProtists; EAL69534; EAL69534; DDB_G0275567.
DR GeneID; 8619987; -.
DR KEGG; ddi:DDB_G0275567; -.
DR dictyBase; DDB_G0275567; amd1.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_1_0_1; -.
DR InParanoid; Q8T1E3; -.
DR OMA; LEIWFEE; -.
DR PhylomeDB; Q8T1E3; -.
DR Reactome; R-DDI-351202; Metabolism of polyamines.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:Q8T1E3; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; ISS:dictyBase.
DR GO; GO:0009446; P:putrescine biosynthetic process; IMP:dictyBase.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:dictyBase.
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 3: Inferred from homology;
KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..95
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000327446"
FT CHAIN 96..379
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000327447"
FT ACT_SITE 30
FT /evidence="ECO:0000250"
FT ACT_SITE 33
FT /evidence="ECO:0000250"
FT ACT_SITE 96
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 267
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 95..96
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 42569 MW; F4CDB13DC46A4F2A CRC64;
MPILSTEIFN EADAGFVYQS NSNDYSDGFE GPEKKLDIRF GPISKGSVKS IAGSPSKVGL
RTIDKEKWQT VLDSARCTII SQTSNDHMDS YVLSESSLFV YPRRAMIKTC GTTTLLHLIA
KMVQVGKECG LEVEMVVFSR KNLNQPSKQV FPHCSFSDEV NFLNKIFDGQ AYVMGDVNKD
HWNLYIADFR KNPTLQRTEQ TFEVMMHDLD ETVMKQFFKR EGVSAWDTTV NSGIADLLPG
SMIDDFQFDP CGYSMNGLLN EFYWTIHITP ESHCSYVSFD TNVALADYNQ LLAKVLNVFK
PGRFTAALYA EDGAPCGDPY TAFDVNVPSY AIQNKTVHGF DGGYDVVVSN YQQLDKKVNF
SNDDLIQSIE STNIDLIQV
