Canmetcon
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Identification
HMDB Protein ID HMDBP00420
Secondary Accession Numbers
  • 5657
  • HMDBP07169
  • HMDBP07401
Name S-adenosylmethionine decarboxylase proenzyme
Synonyms
  1. AdoMetDC
  2. S-adenosylmethionine decarboxylase alpha chain
  3. S-adenosylmethionine decarboxylase beta chain
  4. SAMDC
  5. SubName: Adenosylmethionine decarboxylase 1, isoform CRA_b
  6. SubName: Putative uncharacterized protein DKFZp313L1234
Gene Name AMD1
Protein Type Unknown
Biological Properties
General Function Involved in adenosylmethionine decarboxylase activity
Specific Function Not Available
Pathways
  • Arginine and proline metabolism
  • Cystathionine Beta-Synthase Deficiency
  • Cysteine and methionine metabolism
  • Glycine N-methyltransferase Deficiency
  • Homocystinuria-megaloblastic anemia due to defect in cobalamin metabolism, cblG complementation type
  • Hypermethioninemia
  • Methionine Adenosyltransferase Deficiency
  • Methionine Metabolism
  • Methylenetetrahydrofolate Reductase Deficiency (MTHFRD)
  • S-Adenosylhomocysteine (SAH) Hydrolase Deficiency
  • S-adenosylmethioninamine biosynthesis
  • Spermidine and Spermine Biosynthesis
Reactions
S-Adenosylmethionine → (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2) details
S-Adenosylmethionine + Hydrogen Ion → S-Adenosylmethioninamine + Carbon dioxide details
GO Classification
Biological Process
small molecule metabolic process
S-adenosylmethioninamine biosynthetic process
spermidine biosynthetic process
spermine biosynthetic process
Cellular Component
cytosol
Function
catalytic activity
lyase activity
carbon-carbon lyase activity
carboxy-lyase activity
adenosylmethionine decarboxylase activity
Molecular Function
adenosylmethionine decarboxylase activity
Process
metabolic process
cellular metabolic process
spermidine biosynthetic process
cellular amino acid derivative metabolic process
cellular biogenic amine metabolic process
polyamine metabolic process
polyamine biosynthetic process
spermine biosynthetic process
cellular amino acid and derivative metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location 6
Locus 6q21
SNPs AMD1
Gene Sequence
>1005 bp
ATGGAAGCTGCACATTTTTTCGAAGGGACCGAGAAGCTGCTGGAGGTTTGGTTCTCCCGG
CAGCAGCCCGACGCAAACCAAGGATCTGGGGATCTTCGCACTATCCCAAGATCTGAGTGG
GACATACTTTTGAAGGATGTGCAATGTTCAATCATAAGTGTGACAAAAACTGACAAGCAG
GAAGCTTATGTACTCAGTGAGAGTAGCATGTTTGTCTCCAAGAGACGTTTCATTTTGAAG
ACATGTGGTACCACCCTCTTGCTGAAAGCACTGGTTCCCCTGTTGAAGCTTGCTAGGGAT
TACAGTGGGTTTGACTCAATTCAAAGCTTCTTTTATTCTCGTAAGAATTTCATGAAGCCT
TCTCACCAAGGGTACCCACACCGGAATTTCCAGGAAGAAATAGAGTTTCTTAATGCAATT
TTCCCAAATGGAGCAGCATATTGTATGGGACGTATGAATTCTGACTGTTGGTACTTATAT
ACTCTGGATTTCCCAGAGAGTCGGGTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTG
ATGAGTGAGCTTGACCCAGCAGTTATGGACCAGTTCTACATGAAAGATGGTGTTACTGCA
AAGGATGTCACTCGTGAGAGTGGAATTCGTGACCTGATACCAGGTTCTGTCATTGATGCC
ACAATGTTCAATCCTTGTGGGTATTCGATGAATGGAATGAAATCGGATGGAACTTATTGG
ACTATTCACATCACTCCAGAACCAGAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGT
CAGACCTCCTATGATGACCTGATCAGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTT
GTGACCACCTTGTTTGTTAATCAGAGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAG
AAGATTGAAGGTTTTAAGCGTCTTGATTGCCAGAGTGCTATGTTCAATGATTACAATTTT
GTTTTTACCAGTTTTGCTAAGAAGCAGCAACAACAGCAGAGTTGA
Protein Properties
Number of Residues 334
Molecular Weight 21301.015
Theoretical pI 5.073
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>S-adenosylmethionine decarboxylase proenzyme
MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKP
SHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEIL
MSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYW
TIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQ
KIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS
GenBank ID Protein 55664717
UniProtKB/Swiss-Prot ID P17707
UniProtKB/Swiss-Prot Entry Name DCAM_HUMAN
PDB IDs
GenBank Gene ID AL357515
GeneCard ID AMD1
GenAtlas ID AMD1
HGNC ID HGNC:457
References
General References
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Pajunen A, Crozat A, Janne OA, Ihalainen R, Laitinen PH, Stanley B, Madhubala R, Pegg AE: Structure and regulation of mammalian S-adenosylmethionine decarboxylase. J Biol Chem. 1988 Nov 15;263(32):17040-9. [PubMed:2460457 ]
  5. Stanley BA, Pegg AE: Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J Biol Chem. 1991 Oct 5;266(28):18502-6. [PubMed:1917972 ]
  6. Xiong H, Pegg AE: Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. J Biol Chem. 1999 Dec 3;274(49):35059-66. [PubMed:10574985 ]
  7. Xiong H, Stanley BA, Pegg AE: Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase. Biochemistry. 1999 Feb 23;38(8):2462-70. [PubMed:10029540 ]
  8. Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE: The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Structure. 1999 May;7(5):583-95. [PubMed:10378277 ]
  9. Tolbert WD, Ekstrom JL, Mathews II, Secrist JA 3rd, Kapoor P, Pegg AE, Ealick SE: The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry. 2001 Aug 14;40(32):9484-94. [PubMed:11583147 ]