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P17707 (DCAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme

Short name=AdoMetDC
Short name=SAMDC
EC=4.1.1.50
Gene names
Name:AMD1
Synonyms:AMD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2. Ref.8

Cofactor

Pyruvoyl group.

Enzyme regulation

Both proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.

Pathway

Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.

Subunit structure

Heterotetramer of two alpha and two beta chains.

Post-translational modification

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.

Sequence similarities

Belongs to the eukaryotic AdoMetDC family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P17707-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P17707-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6767S-adenosylmethionine decarboxylase beta chain
PRO_0000029959
Chain68 – 334267S-adenosylmethionine decarboxylase alpha chain
PRO_0000029960

Sites

Active site81
Active site111
Active site681Schiff-base intermediate with substrate; via pyruvic acid
Active site821Proton donor; for catalytic activity
Active site2291Proton acceptor; for processing activity
Active site2431Proton acceptor; for processing activity
Binding site71Substrate
Binding site671Substrate
Binding site2231Substrate
Binding site2471Substrate
Site67 – 682Cleavage (non-hydrolytic); by autolysis

Amino acid modifications

Modified residue681Pyruvic acid (Ser); by autocatalysis
Modified residue2981Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 148148Missing in isoform 2.
VSP_043209

Experimental info

Mutagenesis71F → A: No effect. Ref.11
Mutagenesis81E → Q: Loss of activity. Normal putrescine-stimulated processing.
Mutagenesis111E → Q: Loss of activity. Loss of putrescine-stimulated processing.
Mutagenesis151E → Q: Little effect.
Mutagenesis491C → A: Little effect.
Mutagenesis611E → Q: Little effect.
Mutagenesis671E → Q: Little effect.
Mutagenesis801K → A: Greatly reduced catalytic activity. No putrescine-stimulated processing.
Mutagenesis821C → A: Loss of activity. Greatly reduced putrescine-stimulated processing.
Mutagenesis2231F → A: No effect. Ref.11
Mutagenesis2261C → A: Little effect.
Mutagenesis2291S → A: Loss of processing. Ref.7
Mutagenesis2291S → C: Greatly reduced processing. Ref.7
Mutagenesis2291S → T: Greatly reduced catalytic activity but little effect on processing. Ref.7
Mutagenesis2431H → A: Greatly reduced catalytic activity and processing. Ref.7
Mutagenesis2431H → E: Greatly reduced catalytic activity and processing. Ref.7
Mutagenesis2431H → F: Loss of processing. Ref.7
Mutagenesis2431H → Y: Loss of processing. Ref.7
Mutagenesis2471E → Q: Little effect.
Mutagenesis2491E → Q: Little effect.
Sequence conflict1461A → G in AAA51716. Ref.1

Secondary structure

........................................................... 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 1BB433AF412C9179

FASTA33438,340
        10         20         30         40         50         60 
MEAAHFFEGT EKLLEVWFSR QQPDANQGSG DLRTIPRSEW DILLKDVQCS IISVTKTDKQ 

        70         80         90        100        110        120 
EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP 

       130        140        150        160        170        180 
SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG RMNSDCWYLY TLDFPESRVI SQPDQTLEIL 

       190        200        210        220        230        240 
MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TMFNPCGYSM NGMKSDGTYW 

       250        260        270        280        290        300 
TIHITPEPEF SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLASPQ 

       310        320        330 
KIEGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQQS 

« Hide

Isoform 2 [UniParc].

Checksum: AB97D68DA1BDB447
Show »

FASTA18621,301

References

« Hide 'large scale' references
[1]"Structure and regulation of mammalian S-adenosylmethionine decarboxylase."
Pajunen A., Crozat A., Jaenne O.A., Ihalainen R., Laitinen P.H., Stanley B., Madhubala R., Pegg A.E.
J. Biol. Chem. 263:17040-17049(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, PYRUVATE FORMATION AT SER-68.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Heart.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[6]"Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity."
Stanley B.A., Pegg A.E.
J. Biol. Chem. 266:18502-18506(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[7]"Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate."
Xiong H., Pegg A.E.
J. Biol. Chem. 274:35059-35066(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-229 AND HIS-243.
[8]"Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase."
Xiong H., Stanley B.A., Pegg A.E.
Biochemistry 38:2462-2470(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IMPORTANCE OF CYS-82 IN CATALYTIC ACTIVITY, INHIBITION BY IODOACETIC ACID.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"The crystal structure of human S-adenosylmethionine decarboxylase at 2.25-A resolution reveals a novel fold."
Ekstrom J.L., Mathews I.I., Stanley B.A., Pegg A.E., Ealick S.E.
Structure 7:583-595(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[11]"The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase."
Tolbert W.D., Ekstrom J.L., Mathews I.I., Secrist J.A. III, Kapoor P., Pegg A.E., Ealick S.E.
Biochemistry 40:9484-9494(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), REACTION MECHANISM, MUTAGENESIS OF PHE-7 AND PHE-223.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21154 mRNA. Translation: AAA51716.1.
AL832698 mRNA. Translation: CAI46113.1.
AL357515, AL365206 Genomic DNA. Translation: CAH73388.1.
AL365206, AL357515 Genomic DNA. Translation: CAI23233.1.
AL357515, AL365206 Genomic DNA. Translation: CAH73390.1.
AL365206 Genomic DNA. Translation: CAI23235.1.
CH471051 Genomic DNA. Translation: EAW48307.1.
CH471051 Genomic DNA. Translation: EAW48308.1.
CH471051 Genomic DNA. Translation: EAW48309.1.
BC000171 mRNA. Translation: AAH00171.1.
PIRDCHUDM. A31786.
RefSeqNP_001625.2. NM_001634.5.
UniGeneHs.159118.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I72X-ray2.00A69-334[»]
B1-67[»]
1I79X-ray2.01A69-334[»]
B1-67[»]
1I7BX-ray1.90A69-334[»]
B1-67[»]
1I7CX-ray2.40A69-334[»]
B1-67[»]
1I7MX-ray2.24A/C69-334[»]
B/D1-67[»]
1JENX-ray2.25A/C69-334[»]
B/D1-67[»]
1JL0X-ray1.50A/B1-334[»]
1MSVX-ray1.75A/B1-334[»]
3DZ2X-ray1.86A69-334[»]
B1-67[»]
3DZ3X-ray2.62A69-334[»]
B1-67[»]
3DZ4X-ray1.84A69-334[»]
B1-67[»]
3DZ5X-ray2.43A69-334[»]
B1-67[»]
3DZ6X-ray1.83A69-334[»]
B1-67[»]
3DZ7X-ray1.91A69-334[»]
B1-67[»]
3EP3X-ray1.84A69-328[»]
B1-67[»]
3EP4X-ray1.89A69-328[»]
B1-67[»]
3EP5X-ray1.99A69-328[»]
B1-67[»]
3EP6X-ray1.70A69-328[»]
B1-67[»]
3EP7X-ray2.00A69-328[»]
B1-67[»]
3EP8X-ray1.97A69-328[»]
B1-67[»]
3EP9X-ray2.35A69-328[»]
B1-67[»]
3EPAX-ray2.10A69-328[»]
B1-67[»]
3EPBX-ray1.75A69-328[»]
B1-67[»]
3H0VX-ray2.24A69-334[»]
B1-67[»]
3H0WX-ray1.81A69-334[»]
B1-67[»]
ProteinModelPortalP17707.
SMRP17707. Positions 4-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106759. 3 interactions.
DIPDIP-363N.
STRING9606.ENSP00000357880.

Chemistry

BindingDBP17707.
ChEMBLCHEMBL4181.
DrugBankDB00118. S-Adenosylmethionine.

PTM databases

PhosphoSiteP17707.

Polymorphism databases

DMDM116241324.

Proteomic databases

PaxDbP17707.
PRIDEP17707.

Protocols and materials databases

DNASU262.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368882; ENSP00000357877; ENSG00000123505. [P17707-2]
ENST00000368885; ENSP00000357880; ENSG00000123505. [P17707-1]
GeneID262.
KEGGhsa:262.
UCSCuc003puk.1. human. [P17707-1]

Organism-specific databases

CTD262.
GeneCardsGC06P111195.
HGNCHGNC:457. AMD1.
HPAHPA029281.
HPA029282.
MIM180980. gene.
neXtProtNX_P17707.
PharmGKBPA24763.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77566.
HOGENOMHOG000159915.
HOVERGENHBG000761.
InParanoidP17707.
KOK01611.
OMATIPRFEW.
OrthoDBEOG780RMV.
PhylomeDBP17707.
TreeFamTF313561.

Enzyme and pathway databases

BRENDA4.1.1.50. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP17707.
UniPathwayUPA00331; UER00451.

Gene expression databases

ArrayExpressP17707.
BgeeP17707.
CleanExHS_AMD1.
GenevestigatorP17707.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
InterProIPR001985. S-AdoMet_decarboxylase.
IPR018167. S-AdoMet_decarboxylase_subgr.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
[Graphical view]
PANTHERPTHR11570. PTHR11570. 1 hit.
PfamPF01536. SAM_decarbox. 1 hit.
[Graphical view]
PIRSFPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMSSF56276. SSF56276. 1 hit.
TIGRFAMsTIGR00535. SAM_DCase. 1 hit.
PROSITEPS01336. ADOMETDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAMD1. human.
EvolutionaryTraceP17707.
GenomeRNAi262.
NextBio1029.
PMAP-CutDBP17707.
PROP17707.
SOURCESearch...

Entry information

Entry nameDCAM_HUMAN
AccessionPrimary (citable) accession number: P17707
Secondary accession number(s): E1P5F7 expand/collapse secondary AC list , Q5VXN4, Q5VXN6, Q9BWK4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM