DCAMC_TRYCR
ID DCAMC_TRYCR Reviewed; 370 AA.
AC O76240; Q9UAD2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50 {ECO:0000269|PubMed:10413038, ECO:0000269|PubMed:9677309};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE Flags: Precursor;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND PROTEOLYTIC
RP CLEAVAGE.
RC STRAIN=CL Brener;
RX PubMed=9677309; DOI=10.1042/bj3330527;
RA Persson K., Aaslund L., Grahn B., Hanke J., Heby O.;
RT "Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase:
RT characterization of the gene and the encoded enzyme.";
RL Biochem. J. 333:527-537(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=10413038; DOI=10.1016/s0166-6851(98)00181-9;
RA Kinch L.N., Scott J.R., Ullman B., Phillips M.A.;
RT "Cloning and kinetic characterization of the Trypanosoma cruzi S-
RT adenosylmethionine decarboxylase.";
RL Mol. Biochem. Parasitol. 101:1-11(1999).
CC -!- FUNCTION: Probably in association with catalytically inactive AdoMetDC
CC prozyme, catalyzes the decarboxylation of S-adenosyl-L-methionine which
CC is essential for the biosynthesis of the polyamine spermidine
CC (PubMed:9677309, PubMed:10413038). Required for growth and survival
CC during the bloodstream life cycle stage (By similarity).
CC {ECO:0000250|UniProtKB:P50244, ECO:0000269|PubMed:10413038,
CC ECO:0000269|PubMed:9677309}.
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:10413038, ECO:0000269|PubMed:9677309};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Note=Binds 1 pyruvoyl group covalently per subunit.;
CC -!- ACTIVITY REGULATION: Allosterically activated by AdoMetDC prozyme (By
CC similarity). Activated by putrescine (PubMed:9677309, PubMed:10413038).
CC Inhibited by spermine and methylglyoxal-bis(guanylhydrazone) (MGBG) and
CC slightly by spermidine (PubMed:9677309). Inhibited by 5'-([(Z)-4-amino-
CC 2-butenyl]methylamino)-5'-deoxyadenosine (MDL 73811) (PubMed:10413038).
CC {ECO:0000250|UniProtKB:P50244, ECO:0000269|PubMed:10413038,
CC ECO:0000269|PubMed:9677309}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 mM for S-adenosyl-L-methionine (at pH 7.5)
CC {ECO:0000269|PubMed:9677309};
CC KM=0.051 mM for S-adenosyl-L-methionine (in presence of putrescine)
CC {ECO:0000269|PubMed:10413038};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1. {ECO:0000269|PubMed:10413038, ECO:0000269|PubMed:9677309}.
CC -!- SUBUNIT: Forms a heterodimer with catalytically inactive AdoMetDC
CC prozyme; heterodimerization is required to activate AdoMetDC.
CC {ECO:0000250|UniProtKB:P50244}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme (PubMed:9677309,
CC PubMed:10413038). Formation of the active enzyme involves a self-
CC maturation process in which the active site pyruvoyl group is generated
CC from an internal serine residue via an autocatalytic post-translational
CC modification (By similarity). Two non-identical subunits are generated
CC from the proenzyme in this reaction, and the pyruvate is formed at the
CC N-terminus of the alpha chain, which is derived from the carboxyl end
CC of the proenzyme (By similarity). The post-translation cleavage follows
CC an unusual pathway, termed non-hydrolytic serinolysis, in which the
CC side chain hydroxyl group of the serine supplies its oxygen atom to
CC form the C-terminus of the beta chain, while the remainder of the
CC serine residue undergoes an oxidative deamination to the alpha chain
CC (By similarity). {ECO:0000250|UniProtKB:P17707,
CC ECO:0000269|PubMed:10413038, ECO:0000269|PubMed:9677309}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; AF032907; AAC33263.1; -; Genomic_DNA.
DR EMBL; AF075243; AAC26796.1; -; mRNA.
DR AlphaFoldDB; O76240; -.
DR SMR; O76240; -.
DR VEuPathDB; TriTrypDB:BCY84_01143; -.
DR VEuPathDB; TriTrypDB:C3747_28g21; -.
DR VEuPathDB; TriTrypDB:C4B63_18g214; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_2060; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0027780; -.
DR VEuPathDB; TriTrypDB:TcCL_NonESM02979; -.
DR VEuPathDB; TriTrypDB:TcCLB.504257.30; -.
DR VEuPathDB; TriTrypDB:TcCLB.509167.120; -.
DR VEuPathDB; TriTrypDB:TCDM_02116; -.
DR VEuPathDB; TriTrypDB:TcG_00999; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_003342; -.
DR VEuPathDB; TriTrypDB:TcYC6_0098450; -.
DR OMA; LEIWFEE; -.
DR BRENDA; 4.1.1.50; 6524.
DR SABIO-RK; O76240; -.
DR UniPathway; UPA00331; UER00451.
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 PROSITE; PS01336; ADOMETDC; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW Zymogen.
FT CHAIN 1..85
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000029985"
FT CHAIN 86..370
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000029986"
FT ACT_SITE 29
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 32
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 86
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 100
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 250
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 263
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT SITE 85..86
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT MOD_RES 86
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT CONFLICT 42
FT /note="I -> T (in Ref. 2; AAC26796)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="E -> G (in Ref. 2; AAC26796)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="D -> N (in Ref. 2; AAC26796)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="T -> A (in Ref. 2; AAC26796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 42154 MW; DF218AC3348067F5 CRC64;
MLSNKDPLSL MAMWGSVKGY DPNQGASFEG PEKRLEVIMR IIDETHSEGL HALGDEVWKG
VVGSLNAQIV SKESNEYIRS YVLTESSLFV MRDRIILITC GTTTLLNAVP FVLDAVSDVR
GEVEWVSFMH KNYSFPWEQK GPHLSMAEEF NTLRTYFPSG KPFIFGPVDS DHYFLFVYDD
VIRPCETEND TQLSMTMYGL DRTQTKHWFS DRFISTGTET AAIRKATKLD KVADDSWKLH
DLQFEPCGYS INTIRGAEYQ TIHITPEDHC SFASYETNTP AVNYSERINT VLGVFAPIRF
SVIVFIDPDS DVGRLYQKGQ NVGVEAEYYP KYELQNRTVN EFAPGYVVMK MNYARRAEVT
EKDSTDSVEE
