DCAM_CAEEL
ID DCAM_CAEEL Reviewed; 368 AA.
AC O02655;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50 {ECO:0000269|PubMed:9841864, ECO:0000305|PubMed:19762559};
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=smd-1 {ECO:0000312|WormBase:F47G4.7};
GN Synonyms=samdc {ECO:0000312|WormBase:F47G4.7};
GN ORFNames=F47G4.7 {ECO:0000312|WormBase:F47G4.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CATALYTIC ACTIVITY, PATHWAY, AND
RP SUBUNIT.
RX PubMed=9841864; DOI=10.1042/bj3360545;
RA Da'dara A.A., Walter R.D.;
RT "Molecular and biochemical characterization of S-adenosylmethionine
RT decarboxylase from the free-living nematode Caenorhabditis elegans.";
RL Biochem. J. 336:545-550(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19762559; DOI=10.1096/fj.09-135889;
RA Heinick A., Urban K., Roth S., Spies D., Nunes F., Phanstiel O. IV,
RA Liebau E., Lueersen K.;
RT "Caenorhabditis elegans P5B-type ATPase CATP-5 operates in polyamine
RT transport and is crucial for norspermidine-mediated suppression of RNA
RT interference.";
RL FASEB J. 24:206-217(2010).
CC -!- FUNCTION: Essential for biosynthesis of the polyamines spermidine and
CC spermine. Polyamines are essential for cell proliferation and are
CC implicated in cellular processes, ranging from DNA replication to
CC apoptosis. {ECO:0000269|PubMed:19762559}.
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:9841864, ECO:0000305|PubMed:19762559};
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:0000269|PubMed:9841864}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000269|PubMed:9841864}.
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. {ECO:0000250|UniProtKB:P17707}.
CC -!- DISRUPTION PHENOTYPE: Reduced body size as compared to wild-type with
CC the production of fewer progeny. Reduced spermidine levels, but
CC increased putrescine accumulation. Double knockout with the polyamine
CC transporter catp-5 results in a reduced brood size, delayed
CC postembryonic development, and a more marked reduction in spermidine
CC levels and a more marked increase in putrescine accumulation as
CC compared to the single mutants. {ECO:0000269|PubMed:19762559}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; Y12500; CAA73102.1; -; Genomic_DNA.
DR EMBL; Y12499; CAA73101.1; -; mRNA.
DR EMBL; BX284601; CAB16315.1; -; Genomic_DNA.
DR EMBL; AL023853; CAB16315.1; JOINED; Genomic_DNA.
DR PIR; T22361; T22361.
DR RefSeq; NP_493448.1; NM_061047.5.
DR AlphaFoldDB; O02655; -.
DR SMR; O02655; -.
DR BioGRID; 38658; 1.
DR IntAct; O02655; 2.
DR STRING; 6239.F47G4.7.1; -.
DR EPD; O02655; -.
DR PaxDb; O02655; -.
DR PeptideAtlas; O02655; -.
DR EnsemblMetazoa; F47G4.7.1; F47G4.7.1; WBGene00004875.
DR EnsemblMetazoa; F47G4.7.2; F47G4.7.2; WBGene00004875.
DR EnsemblMetazoa; F47G4.7.3; F47G4.7.3; WBGene00004875.
DR GeneID; 173269; -.
DR UCSC; F47G4.7.1; c. elegans.
DR CTD; 173269; -.
DR WormBase; F47G4.7; CE18705; WBGene00004875; smd-1.
DR eggNOG; KOG0788; Eukaryota.
DR GeneTree; ENSGT00390000011776; -.
DR HOGENOM; CLU_023050_1_0_1; -.
DR InParanoid; O02655; -.
DR OMA; LEIWFEE; -.
DR OrthoDB; 932490at2759; -.
DR PhylomeDB; O02655; -.
DR BRENDA; 4.1.1.50; 1045.
DR Reactome; R-CEL-351202; Metabolism of polyamines.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:O02655; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004875; Expressed in larva and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:WormBase.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:WormBase.
DR GO; GO:0006597; P:spermine biosynthetic process; IDA:WormBase.
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 Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..82
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000029975"
FT CHAIN 83..368
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000029976"
FT ACT_SITE 26
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 29
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 83
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 97
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 246
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 261
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT SITE 82..83
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT MOD_RES 83
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
SQ SEQUENCE 368 AA; 42143 MW; 72CED2D16BC46E5E CRC64;
MSATSATNFA VQTHPVKAPD EEYFFEGAEK LLELWFCSST QNETRSLRII PREEIDAMLD
IARCKILHSK HNESIDSYVL SESSLFISDN RVILKTCGTT RLLAALPVIM QLAGAYAGLD
QVQSVYYSRK NFLRPDLQPS LHKNFDAEVE YLDSFFVDGH AYCLGSLKQD RWYLYTFHRE
VEFPAHKQPD HTLEILMSDL DEEVLHKFTK DYAVDGNDCF MRAGIDKIIP AGADVHDELF
DPCGYSMNAY MNDTDQYATI HVTPEKAFSF ASFETNQDLV CLYSQTRKVL QCFRPNKILM
TVFANDISEK GKDAQQQLWD RELPGYRRTN VQFVRLETET LVYAHFVRKA STGQDSSSSD
EDDGERSD
