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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

spe2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.

Cofactori

pyruvateBy similarityNote: Binds 1 pyruvoyl group covalently per subunit.By similarity

Pathwayi: S-adenosylmethioninamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine.
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine decarboxylase proenzyme (spe2)
This subpathway is part of the pathway S-adenosylmethioninamine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei21 – 211By similarity
Active sitei24 – 241By similarity
Active sitei85 – 851Schiff-base intermediate with substrate; via pyruvic acidBy similarity
Active sitei99 – 991Proton donor; for catalytic activityBy similarity
Active sitei275 – 2751Proton acceptor; for processing activityBy similarity
Active sitei288 – 2881Proton acceptor; for processing activityBy similarity

GO - Molecular functioni

GO - Biological processi

  • pantothenate biosynthetic process Source: PomBase
  • S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
  • spermidine biosynthetic process Source: PomBase
  • spermine biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Pyruvate, S-adenosyl-L-methionine, Schiff base

Enzyme and pathway databases

ReactomeiR-SPO-351202. Metabolism of polyamines.
UniPathwayiUPA00331; UER00451.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50)
Short name:
AdoMetDC
Short name:
SAMDC
Cleaved into the following 2 chains:
Gene namesi
Name:spe2
ORF Names:SPBP4H10.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.05c.
PomBaseiSPBP4H10.05c. spe2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8484S-adenosylmethionine decarboxylase beta chainBy similarityPRO_0000030031Add
BLAST
Chaini85 – 378294S-adenosylmethionine decarboxylase alpha chainBy similarityPRO_0000030032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851Pyruvic acid (Ser); by autocatalysisBy similarity

Post-translational modificationi

Is synthesized initially as an inactive proenzyme. 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. 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. 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 produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 852Cleavage (non-hydrolytic); by autolysis

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

MaxQBiQ9P7E3.

Interactioni

Protein-protein interaction databases

BioGridi277849. 2 interactions.
MINTiMINT-4705284.

Structurei

3D structure databases

ProteinModelPortaliQ9P7E3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic AdoMetDC family.Curated

Phylogenomic databases

HOGENOMiHOG000159915.
InParanoidiQ9P7E3.
KOiK01611.
OMAiYQSFTPR.
OrthoDBiEOG70PC6X.
PhylomeDBiQ9P7E3.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
InterProiIPR001985. S-AdoMet_decarboxylase.
IPR018167. S-AdoMet_decarboxylase_subgr.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
[Graphical view]
PANTHERiPTHR11570. PTHR11570. 1 hit.
PfamiPF01536. SAM_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR00535. SAM_DCase. 1 hit.
PROSITEiPS01336. ADOMETDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9P7E3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPTLVVDQE NSEEFNTSSF EGPEKLLELW FSAPIKTNLS AGEKANLGLK
60 70 80 90 100
AVSRNDWDDM LAQAQCKVLS VVNSEEIDAY LLSESSMFVF AHKIILKTCG
110 120 130 140 150
TTTLLASLPR LLEIASSVGF DRPLRIFYSR KNFLYPERQL APHTSWEEEV
160 170 180 190 200
RYLQLFFPSG CSYVVGPTNK NHWHLFSDLA DDYSLLEDSL DPEDETLEVL
210 220 230 240 250
MTDMSPERSL QFYAPSLDVV RSARGDDYVR EKNNLSGGHI LGSYVADESG
260 270 280 290 300
VRDLCSTSDK KAVLDAFQFE PIGFSSNMIY KDRYATIHVT PQEHCSYASF
310 320 330 340 350
ETNVSQFQFG RSISETIEKT VKTFGANKFC LTLFQAKGAS QEKHFSAKLK
360 370
SFSSYKREEF IVYDFPGYDL IFASFTAV
Length:378
Mass (Da):42,712
Last modified:October 1, 2000 - v1
Checksum:i10AEA8B3DAF62894
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045111 Genomic DNA. Translation: BAB12576.1.
AB045110 mRNA. Translation: BAB12575.1.
CU329671 Genomic DNA. Translation: CAB83163.1.
RefSeqiNP_596179.1. NM_001022098.2.

Genome annotation databases

EnsemblFungiiSPBP4H10.05c.1; SPBP4H10.05c.1:pep; SPBP4H10.05c.
GeneIDi2541338.
KEGGispo:SPBP4H10.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045111 Genomic DNA. Translation: BAB12576.1.
AB045110 mRNA. Translation: BAB12575.1.
CU329671 Genomic DNA. Translation: CAB83163.1.
RefSeqiNP_596179.1. NM_001022098.2.

3D structure databases

ProteinModelPortaliQ9P7E3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277849. 2 interactions.
MINTiMINT-4705284.

Proteomic databases

MaxQBiQ9P7E3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP4H10.05c.1; SPBP4H10.05c.1:pep; SPBP4H10.05c.
GeneIDi2541338.
KEGGispo:SPBP4H10.05c.

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.05c.
PomBaseiSPBP4H10.05c. spe2.

Phylogenomic databases

HOGENOMiHOG000159915.
InParanoidiQ9P7E3.
KOiK01611.
OMAiYQSFTPR.
OrthoDBiEOG70PC6X.
PhylomeDBiQ9P7E3.

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.
ReactomeiR-SPO-351202. Metabolism of polyamines.

Miscellaneous databases

PROiQ9P7E3.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
InterProiIPR001985. S-AdoMet_decarboxylase.
IPR018167. S-AdoMet_decarboxylase_subgr.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
[Graphical view]
PANTHERiPTHR11570. PTHR11570. 1 hit.
PfamiPF01536. SAM_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR00535. SAM_DCase. 1 hit.
PROSITEiPS01336. ADOMETDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Antizyme regulates the degradation of ornithine decarboxylase in fission yeast Schizosaccharomyces pombe. Study in the spe2 knockout strains."
    Chattopadhyay M.K., Murakami Y., Matsufuji S.
    J. Biol. Chem. 276:21235-21241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiDCAM_SCHPO
AccessioniPrimary (citable) accession number: Q9P7E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.