UniProtKB - O76240 (DCAMC_TRYCR)
Protein
S-adenosylmethionine decarboxylase proenzyme
Gene
N/A
Organism
Trypanosoma cruzi
Status
Functioni
Probably in association with catalytically inactive AdoMetDC prozyme, catalyzes the decarboxylation of S-adenosyl-L-methionine which is essential for the biosynthesis of the polyamine spermidine (PubMed:9677309, PubMed:10413038). Required for growth and survival during the bloodstream life cycle stage (By similarity).By similarity2 Publications
Catalytic activityi
- EC:4.1.1.502 Publications
Cofactori
pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.
Activity regulationi
Allosterically activated by AdoMetDC prozyme (By similarity). Activated by putrescine (PubMed:9677309, PubMed:10413038). Inhibited by spermine and methylglyoxal-bis(guanylhydrazone) (MGBG) and slightly by spermidine (PubMed:9677309). Inhibited by 5'-([(Z)-4-amino-2-butenyl]methylamino)-5'-deoxyadenosine (MDL 73811) (PubMed:10413038).By similarity2 Publications
Kineticsi
- KM=0.21 mM for S-adenosyl-L-methionine (at pH 7.5)1 Publication
- KM=0.051 mM for S-adenosyl-L-methionine (in presence of putrescine)1 Publication
: S-adenosylmethioninamine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine.2 PublicationsProteins known to be involved in this subpathway in this organism are:
- Adenosylmethionine decarboxylase (C3747_104g30), Putative S-adenosylmethionine decarboxylase proenzyme (C3747_28g20), Putative S-adenosylmethionine decarboxylase proenzyme (C3747_104g29), S-adenosylmethionine decarboxylase proenzyme (C4B63_18g214), S-adenosylmethionine decarboxylase proenzyme (C3747_28g21), Putative S-adenosylmethionine decarboxylase proenzyme (C4B63_18g213), S-adenosylmethionine decarboxylase proenzyme
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine, the pathway S-adenosylmethioninamine biosynthesis and in Amine and polyamine biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 28 | SubstrateBy similarity | 1 | |
Active sitei | 29 | By similarity | 1 | |
Active sitei | 32 | By similarity | 1 | |
Binding sitei | 85 | SubstrateBy similarity | 1 | |
Active sitei | 86 | Schiff-base intermediate with substrate; via pyruvic acidBy similarity | 1 | |
Active sitei | 100 | Proton donor; for catalytic activityBy similarity | 1 | |
Active sitei | 250 | Proton acceptor; for processing activityBy similarity | 1 | |
Active sitei | 263 | Proton acceptor; for processing activityBy similarity | 1 | |
Binding sitei | 267 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- adenosylmethionine decarboxylase activity Source: UniProtKB-EC
GO - Biological processi
- S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
- spermidine biosynthetic process Source: UniProtKB-KW
- spermine biosynthetic process Source: InterPro
Keywordsi
Molecular function | Decarboxylase, Lyase |
Biological process | Polyamine biosynthesis, Spermidine biosynthesis |
Ligand | Pyruvate, S-adenosyl-L-methionine, Schiff base |
Enzyme and pathway databases
BRENDAi | 4.1.1.50, 6524 |
SABIO-RKi | O76240 |
UniPathwayi | UPA00331;UER00451 |
Names & Taxonomyi
Protein namesi | Recommended name: S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.502 Publications)Short name: AdoMetDC Short name: SAMDC Cleaved into the following 2 chains: |
Organismi | Trypanosoma cruzi |
Taxonomic identifieri | 5693 [NCBI] |
Taxonomic lineagei | Eukaryota › Discoba › Euglenozoa › Kinetoplastea › Metakinetoplastina › Trypanosomatida › Trypanosomatidae › Trypanosoma › Schizotrypanum |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000029985 | 1 – 85 | S-adenosylmethionine decarboxylase beta chainBy similarityAdd BLAST | 85 | |
ChainiPRO_0000029986 | 86 – 370 | S-adenosylmethionine decarboxylase alpha chainBy similarityAdd BLAST | 285 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 86 | Pyruvic acid (Ser); by autocatalysisBy similarity | 1 |
Post-translational modificationi
Is synthesized initially as an inactive proenzyme (PubMed:9677309, PubMed:10413038). Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification (By similarity). Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme (By similarity). The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to the alpha chain (By similarity).By similarity2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 85 – 86 | Cleavage (non-hydrolytic); by autolysisBy similarity | 2 |
Keywords - PTMi
Autocatalytic cleavage, ZymogenInteractioni
Subunit structurei
Forms a heterodimer with catalytically inactive AdoMetDC prozyme; heterodimerization is required to activate AdoMetDC.
By similarityFamily & Domainsi
Sequence similaritiesi
Belongs to the eukaryotic AdoMetDC family.Curated
Family and domain databases
InterProi | View protein in InterPro IPR001985, S-AdoMet_decarboxylase IPR016067, S-AdoMet_deCO2ase_core IPR018166, S-AdoMet_deCO2ase_CS |
PANTHERi | PTHR11570, PTHR11570, 1 hit |
Pfami | View protein in Pfam PF01536, SAM_decarbox, 1 hit |
PIRSFi | PIRSF001355, S-AdenosylMet_decarboxylase, 1 hit |
SUPFAMi | SSF56276, SSF56276, 1 hit |
PROSITEi | View protein in PROSITE PS01336, ADOMETDC, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O76240-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLSNKDPLSL MAMWGSVKGY DPNQGASFEG PEKRLEVIMR IIDETHSEGL
60 70 80 90 100
HALGDEVWKG VVGSLNAQIV SKESNEYIRS YVLTESSLFV MRDRIILITC
110 120 130 140 150
GTTTLLNAVP FVLDAVSDVR GEVEWVSFMH KNYSFPWEQK GPHLSMAEEF
160 170 180 190 200
NTLRTYFPSG KPFIFGPVDS DHYFLFVYDD VIRPCETEND TQLSMTMYGL
210 220 230 240 250
DRTQTKHWFS DRFISTGTET AAIRKATKLD KVADDSWKLH DLQFEPCGYS
260 270 280 290 300
INTIRGAEYQ TIHITPEDHC SFASYETNTP AVNYSERINT VLGVFAPIRF
310 320 330 340 350
SVIVFIDPDS DVGRLYQKGQ NVGVEAEYYP KYELQNRTVN EFAPGYVVMK
360 370
MNYARRAEVT EKDSTDSVEE
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 42 | I → T in AAC26796 (PubMed:10413038).Curated | 1 | |
Sequence conflicti | 56 | E → G in AAC26796 (PubMed:10413038).Curated | 1 | |
Sequence conflicti | 230 | D → N in AAC26796 (PubMed:10413038).Curated | 1 | |
Sequence conflicti | 360 | T → A in AAC26796 (PubMed:10413038).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF032907 Genomic DNA Translation: AAC33263.1 AF075243 mRNA Translation: AAC26796.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF032907 Genomic DNA Translation: AAC33263.1 AF075243 mRNA Translation: AAC26796.1 |
3D structure databases
SMRi | O76240 |
ModBasei | Search... |
Enzyme and pathway databases
UniPathwayi | UPA00331;UER00451 |
BRENDAi | 4.1.1.50, 6524 |
SABIO-RKi | O76240 |
Family and domain databases
InterProi | View protein in InterPro IPR001985, S-AdoMet_decarboxylase IPR016067, S-AdoMet_deCO2ase_core IPR018166, S-AdoMet_deCO2ase_CS |
PANTHERi | PTHR11570, PTHR11570, 1 hit |
Pfami | View protein in Pfam PF01536, SAM_decarbox, 1 hit |
PIRSFi | PIRSF001355, S-AdenosylMet_decarboxylase, 1 hit |
SUPFAMi | SSF56276, SSF56276, 1 hit |
PROSITEi | View protein in PROSITE PS01336, ADOMETDC, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DCAMC_TRYCR | |
Accessioni | O76240Primary (citable) accession number: O76240 Secondary accession number(s): Q9UAD2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1999 |
Last sequence update: | November 1, 1998 | |
Last modified: | August 12, 2020 | |
This is version 90 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families