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Human Metabolome Database Version 2.5

 

Showing metabocard for Selenomethionine (HMDB03966)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 09:10:37
Update Date 2009-05-05 20:59:48
Accession Number HMDB03966
Secondary Accession Numbers Not Available
Common Name Selenomethionine
Description Selenomethionine is an amino acid containing selenium that cannot be synthesized by higher animals, but can be obtained from plant material. Selenomethionine is the major seleno-compound in cereal grains (wheat grain, maize and rice), soybeans and enriched yeast. Seleno-compounds present in plants may have a profound effect upon the health of animals and human subjects. It is now known that the total Se content cannot be used as an indication of its efficacy, but knowledge of individual selenocompounds is necessary to fully assess the significance. Thus, speciation of the seleno-compounds has moved to the forefront. Since animals and man are dependent upon plants for their nutritional requirements, this makes the types of seleno-compounds in plants even more critical. Se enters the food chain through incorporation into plant proteins, mostly as selenocysteine and selenomethionine at normal Se levels. There are two possible pathways for the catabolism of selenomethionine. One is the transsulfuration pathway via selenocystathionine to produce selenocysteine, which in turn is degraded to H2Se by the enzyme b-lyase. The other pathway is the transamination-decarboxylation pathway. It was estimated that 90% of methionine is metabolized through this pathway and thus could be also the major route for selenomethionine catabolism. (PMID: 14748935, Br J Nutr. 2004 Jan;91(1):11-28.)
Synonyms
  1. (+-)-Selenomethionine
  2. (2S)-2-amino-4-(methylseleno)butanoic acid
  3. (S)-2-amino-4-(methylseleno)-Butanoic acid
  4. (S)-2-Amino-4-(methylseleno)butanoic acid
  5. (S)-2-Amino-4-(methylseleno)butyric acid
  6. 2-amino-4-(methylseleno)butanoate
  7. 2-amino-4-(methylseleno)butanoic acid
  8. 2-Amino-4-(methylselenyl)butyrate
  9. 2-Amino-4-(methylselenyl)butyric acid
  10. DL-Selenomethionine
  11. L(+)-Selenomethionine
  12. L-2-amino-4-(methylselenyl)-Butyric acid
  13. L-Selenomethionine
  14. L-Selenomethioninum
  15. MSE
  16. Selenium methionine
  17. Selenium-L-methionine
  18. Seleno-D,L-methionine
  19. Seleno-DL-methionine
  20. Seleno-L-methionine
  21. Selenomethionine Se 75
  22. SeMet
  23. Sethotope
  24. (2S)-2-amino-4-(methylseleno)butanoate
  25. (S)-2-amino-4-(methylseleno)-Butanoate
  26. (S)-2-Amino-4-(methylseleno)butanoate
Chemical IUPAC Name 2-amino-4-methylselanyl-butanoic acid
Chemical Formula C5H11NO2Se
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 196.106
Monoisotopic Molecular Weight 196.995499
Isomeric SMILES C[Se]CCC(N)C(O)=O
Canonical SMILES C[Se]CCC(N)C(O)=O
KEGG Compound ID C05335 Link Image
BioCyc ID SELENOMETHIONINE Link Image
BiGG ID 45598 Link Image
Wikipedia Link Selenomethionine Link Image
NuGOwiki Link HMDB03966 Link Image
Metagene Link HMDB03966 Link Image
METLIN ID 6993 Link Image
PubChem Compound 15103 Link Image
PubChem Substance 8161321 Link Image
ChEBI ID 27585 Link Image
CAS Registry Number 3211-76-5
InChI Identifier InChI=1/C5H11NO2Se/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)
Synthesis Reference Jakubke, Hans D.; Fischer, J.; Jost, Karel; Rudinger, Josef. Amino acids and peptides. LXXXVI. Synthesis of L-selenomethionine, L-selenoethionine, and their tert-butoxy-carbonyl derivatives. Collection of Czechoslovak Chemical Communications (1968), 33(11), 3910-12.
Melting Point (Experimental) 275 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 109.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.46 [Predicted by ALOGPS]; -3.01 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Fibroblasts —
Kidney —
Pancreas —
Prostate —
Concentrations (Normal)
Biofluid Urine
Value 0 - 0.002 umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Kuehnelt D, Kienzl N, Traar P, Le NH, Francesconi KA, Ochi T: Selenium metabolites in human urine after ingestion of selenite, L-selenomethionine, or DL-selenomethionine: a quantitative case study by HPLC/ICPMS. Anal Bioanal Chem. 2005 Sep;383(2):235-46. Epub 2005 Oct 12. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.69 (0.56 - 0.82) uM
Age Adult:>18 yrs old
Sex N/A
Condition Abnormal
Comments Volunteers in a Phase I multiple-dose safety and clinical study of L-selenomethionine
References
  • Elmore E, Siddiqui S, Navidi M, Steele VE, Redpath JL: Correlation of in vitro chemopreventive efficacy data from the human epidermal cell assay with animal efficacy data and clinical trial plasma levels. J Cell Biochem. 2005 Jun 1;95(3):571-88. [PubMed Link Image]
Biofluid Blood
Value 0.303 +/- 0.099 uM
Age Adult:>18 yrs old
Sex N/A
Condition Prostate cancer
Comments Not Available
References
  • Nyman DW, Suzanne Stratton M, Kopplin MJ, Dalkin BL, Nagle RB, Jay Gandolfi A: Selenium and selenomethionine levels in prostate cancer patients. Cancer Detect Prev. 2004;28(1):8-16. [PubMed Link Image]
Associated Disorders
Condition References
Prostate cancer
  • Nyman DW, Suzanne Stratton M, Kopplin MJ, Dalkin BL, Nagle RB, Jay Gandolfi A: Selenium and selenomethionine levels in prostate cancer patients. Cancer Detect Prev. 2004;28(1):8-16. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Selenoamino Acid Metabolism SMP00029 Link Image map00450 Link Image
General References
  1. Pointner H, Kinast H, Flegel U: 75Se-selenomethionine excretion in bile and pancreatic juice. Digestion. 1975;12(1):61-4. [PubMed Link Image]
  2. Greenwald P, Milner JA, Anderson DE, McDonald SS: Micronutrients in cancer chemoprevention. Cancer Metastasis Rev. 2002;21(3-4):217-30. [PubMed Link Image]
  3. Seo YR, Sweeney C, Smith ML: Selenomethionine induction of DNA repair response in human fibroblasts. Oncogene. 2002 May 23;21(23):3663-9. [PubMed Link Image]
  4. Yang X, Tian Y, Ha P, Gu L: [Determination of the selenomethionine content in grain and human blood] Wei Sheng Yan Jiu. 1997 Mar;26(2):113-6. [PubMed Link Image]
  5. Hoang TT, Chen Y, May SW, Browner RF: Analysis of organoselenium compounds in human urine using active carbon and chemically modified silica sol-gel surface-assisted laser desorption/ionization high-resolution time-of-flight mass spectrometry. Anal Chem. 2004 Apr 1;76(7):2062-70. [PubMed Link Image]
  6. Dorea JG: Selenium and breast-feeding. Br J Nutr. 2002 Nov;88(5):443-61. [PubMed Link Image]
  7. Wally J, Halbrooks PJ, Vonrhein C, Rould MA, Everse SJ, Mason AB, Buchanan SK: The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding. J Biol Chem. 2006 Aug 25;281(34):24934-44. Epub 2006 Jun 22. [PubMed Link Image]
  8. Cabanero AI, Madrid Y, Camara C: Selenium long-term administration and its effect on mercury toxicity. J Agric Food Chem. 2006 Jun 14;54(12):4461-8. [PubMed Link Image]
  9. Wan XS, Zhou Z, Kennedy AR, Kopelovich L: In vitro evaluation of chemopreventive agents using cultured human prostate epithelial cells. Oncol Rep. 2003 Nov-Dec;10(6):2009-14. [PubMed Link Image]
  10. Nakanishi F, Kasuga T, Kobayashi T, Miyabayashi H, Yano K: [Method of analysis of regional dynamics of the pancreas with 75Se-selenomethionine] Kaku Igaku. 1977 Apr;14(2):223-32. [PubMed Link Image]
  11. Agnew JE, McCarthy DM, Melmed RNBOUCHIER IA: Count rate analysis as an adjunct to the 75Se-selenomethionine pancreas scan. Br J Radiol. 1969 Oct;42(502):762-9. [PubMed Link Image]
  12. Kuehnelt D, Kienzl N, Traar P, Le NH, Francesconi KA, Ochi T: Selenium metabolites in human urine after ingestion of selenite, L-selenomethionine, or DL-selenomethionine: a quantitative case study by HPLC/ICPMS. Anal Bioanal Chem. 2005 Sep;383(2):235-46. Epub 2005 Oct 12. [PubMed Link Image]
  13. Wikipedia Link Image
Metabolic Enzymes
  1. S-adenosylmethionine synthetase isoform type-1
  2. Methionyl-tRNA synthetase, cytoplasmic
  3. Methionine adenosyltransferase 2 subunit beta
  4. Methionyl-tRNA synthetase, mitochondrial
  5. Methionine adenosyltransferase II, beta, isoform CRA_a
Enzyme 1 [top]
Enzyme 1 ID 5655
Enzyme 1 Name S-adenosylmethionine synthetase isoform type-1
Enzyme 1 Synonyms
  1. Methionine adenosyltransferase 1
  2. AdoMet synthetase 1
  3. Methionine adenosyltransferase I/III
  4. MAT-I/III
Enzyme 1 Gene Name MAT1A
Enzyme 1 Protein Sequence >S-adenosylmethionine synthetase isoform type-1 
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
Enzyme 1 Number of Residues 395
Enzyme 1 Molecular Weight 43648
Enzyme 1 Theoretical pI 6.24
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • methionine adenosyltransferase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular metabolism
  • metabolism
  • one-carbon compound metabolism
  • physiological process
Component
—
Enzyme 1 General Function Coenzyme transport and metabolism
Enzyme 1 Specific Function Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 220066 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q00266 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name METK1_HUMAN Link Image
Enzyme 1 PDB ID 1O9T Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1188 bp 
ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCCACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGCGGCCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTGGACCGCTCAGCCGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGACTTGGATTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
Enzyme 1 GenBank Gene ID D49357 Link Image
Enzyme 1 GeneCard ID MAT1A Link Image
Enzyme 1 GenAtlas ID MAT1A Link Image
Enzyme 1 HGNC ID HGNC:6903 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed Link Image]
  2. Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [PubMed Link Image]
  3. Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed Link Image]
  4. Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed Link Image]
  5. Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed Link Image]
  6. Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5895
Enzyme 2 Name Methionyl-tRNA synthetase, cytoplasmic
Enzyme 2 Synonyms
  1. Methionine--tRNA ligase
  2. MetRS
Enzyme 2 Gene Name MARS
Enzyme 2 Protein Sequence >Methionyl-tRNA synthetase, cytoplasmic 
MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLF
STSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRA
LTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQE
PCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAW
EKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRL
RQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTP
QQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDK
CGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQF
ITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWW
KNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGV
GVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMF
VSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ
VNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSI
LLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQ
QIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK
Enzyme 2 Number of Residues 900
Enzyme 2 Molecular Weight 101117
Enzyme 2 Theoretical pI 6.05
Enzyme 2 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • methionine-tRNA ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • metabolism
  • methionyl-tRNA aminoacylation
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
—
Enzyme 2 General Function Translation, ribosomal structure and biogenesis
Enzyme 2 Specific Function ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1702932 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P56192 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SYMC_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2703 bp 
ATGAGACTGTTCGTGAGTGATGGCGTCCCGGGTTGCTTGCCGGTGCTGGCCGCCGCCGGG
AGAGCCCGGGGCAGAGCAGAGGTGCTGATCAGCACTGTAGGCCCGGAAGATTGTGTGGTC
CCGTTCCTGACCCGGCCTAAGGTCCCTGTCTTGCAGGTGGATAGCGGCAACTACCTCTTC
TCCACTAGTGCAATCTGCCGATATTTTTTTTTGTTATCTGGCTGGGAGCAAGATGACCTC
ACTAACCAGTGGCTGGAATGGGAAGCGACAGAGCTGCAGCCAGCTTTGTCTGCTCCCCTG
TACTATTTAGTGGTCCAAGGCAAGAAGGGGGAAGATGTTCTTGGTTCAGTGCGGAGAGCC
CTGACTCACATTGACCACAGCTTGAGTCGTCAGAACTGTCCTTTCCTGGCTGGGGAGACA
GAATCTCTAGCCGACATTGTTTTGTGGGGAGCCCAATACCCATTACTGCAAGATCCCGCC
TACCTCCCTGAGGAGCTGAGTGCCCTGCACAGCTGGTTCCAGACACTGAGTACCCAGGAA
CCATGTCAGCGAGCTGCAGAGACTGTACTGAAACAGCAAGGTGTCCTGGCTCTCCGGCCT
TACCTCCAAAAGCAGCCCCAGCCCAGCCCCGCTGAGGGAAGGGCTGTCACCAATGAGCCT
GAGGAGGAGGAGCTGGCTACCCTATCTGAGGAGGAGATTGCTATGGCTGTTACTGCTTGG
GAGAAGGGCCTAGAAAGTTTGCCCCCGCTGCGGCCCCAGCAGAATCCAGTGTTGCCTGTG
GCTGGAGAAAGGAATGTGCTCATCACCAGTGCCCTCCCTTACGTCAACAATGTCCCCCAC
CTTGGGAACATCATTGGTTGTGTGCTCAGTGCCGATGTCTTTGCCAGGTACTCTCGCCTC
CGCCAGTGGAACACCCTCTATCTGTGTGGGACAGATGAGTATGGTACAGCAACAGAGACC
AAGGCTCTGGAGGAGGGACTAACCCCCCAGGAGATCTGCGACAAGTACCACATCATCCAT
GCTGACATCTACCGCTGGTTTAACATTTCGTTTGATATTTTTGGTCGCACCACCACTCCA
CAGCAGACCAAAATCACCCAGGACATTTTCCAGCAGTTGCTGAAACGAGGTTTTGTGCTG
CAAGATACTGTGGAGCAACTGCGATGTGAGCACTGTGCTCGCTTCCTGGCTGACCGCTTC
GTGGAGGGCGTGTGTCCCTTCTGTGGCTATGAGGAGGCTCGGGGTGACCAGTGTGACAAG
TGTGGCAAGCTCATCAATGCTGTCGAGCTTAAGAAGCCTCAGTGTAAAGTCTGCCGATCA
TGCCCTGTGGTGCAGTCGAGCCAGCACCTGTTTCTGGACCTGCCTAAGCTGGAGAAGCGA
CTGGAGGAGTGGTTGGGGAGGACATTGCCTGGCAGTGACTGGACACCCAATGCCCAGTTT
ATCACCCGTTCTTGGCTTCGGGATGGCCTCAAGCCACGCTGCATAACCCGAGACCTCAAA
TGGGGAACCCCTGTACCCTTAGAAGGTTTTGAAGACAAGGTATTCTATGTCTGGTTTGAT
GCCACTATTGGCTATCTGTCCATCACAGCCAACTACACAGACCAGTGGGAGAGATGGTGG
AAGAACCCAGAGCAAGTGGACCTGTATCAGTTCATGGCCAAAGACAATGTTCCTTTCCAT
AGCTTAGTCTTTCCTTGCTCAGCCCTAGGAGCTGAGGATAACTATACCTTGGTCAGCCAC
CTCATTGCTACAGAGTACCTGAACTATGAGGATGGGAAATTCTCTAAGAGCCGCGGTGTG
GGAGTGTTTGGGGACATGGCCCAGGACACGGGGATCCCTGCTGACATCTGGCGCTTCTAT
CTGCTGTACATTCGGCCTGAGGGCCAGGACAGTGCTTTCTCCTGGACGGACCTGCTGCTG
AAGAATAATTCTGAGCTGCTTAACAACCTGGGCAACTTCATCAACAGAGCTGGGATGTTT
GTGTCTAAGTTCTTTGGGGGCTATGTGCCTGAGATGGTGCTCACCCCTGATGATCAGCGC
CTGCTGGGCCATGTCACCCTGGAGCTCCAGCACTATCACCAGCTACTTGAGAAGGTTCGG
ATCCGGGATGCCTTGCGCAGTATCCTCACCATATCTCGACATGGCAACCAATATATTCAG
GTGAATGAGCCCTGGAAGCGGATTAAAGGCAGTGAGGCTGACAGGCAACGGGCAGGAACA
GTGACTGGCTTGGCAGTGAATATAGCTGCCTTGCTCTCTGTCATGCTTCAGCCTTACATG
CCCACGGTTAGTGCCACAATCCAGGCCCAGCTGCAGCTCCCACCTCCAGCCTGCAGTATC
CTGCTGACAAACTTCCTGTGTACCTTACCAGCAGGACACCAGATTGGCACAGTCAGTCCC
TTGTTCCAAAAATTGGAAAATGACCAGATTGAAAGTTTAAGGCAGCGCTTTGGAGGGGGC
CAGGCAAAAACGTCCCCGAAGCCAGCAGTTGTAGAGACTGTTACAACAGCCAAGCCACAG
CAGATACAAGCGCTGATGGATGAAGTGACAAAACAAGGAAACATTGTCCGAGAACTGAAA
GCACAAAAGGCAGACAAGAACGAGGTTGCTGCGGAGGTGGCGAAACTCTTGGATCTAAAG
AAACAGTTGGCTGTAGCTGAGGGGAAACCCCCTGAAGCCCCTAAAGGCAAGAAGAAAAAG
TAA
Enzyme 2 GenBank Gene ID X94754 Link Image
Enzyme 2 GeneCard ID MARS Link Image
Enzyme 2 GenAtlas ID MARS Link Image
Enzyme 2 HGNC ID HGNC:6898 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Lage H, Dietel M: Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. Gene. 1996 Oct 31;178(1-2):187-9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 9553
Enzyme 3 Name Methionine adenosyltransferase 2 subunit beta
Enzyme 3 Synonyms
  1. Methionine adenosyltransferase II beta
  2. MAT II beta
  3. Methionine adenosyltransferase 2 beta subunit
  4. DTDP-4-keto-6-deoxy-D-glucose 4- reductase
Enzyme 3 Gene Name MAT2B
Enzyme 3 Protein Sequence >Methionine adenosyltransferase 2 subunit beta 
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
Enzyme 3 Number of Residues 334
Enzyme 3 Molecular Weight 37552
Enzyme 3 Theoretical pI Not Available
Enzyme 3 GO Classification
Function
  • catalytic activity
  • dTDP-4-dehydrorhamnose reductase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carbohydrate biosynthesis
  • extracellular polysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
—
Enzyme 3 General Function Cell wall/membrane/envelope biogenesis
Enzyme 3 Specific Function Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S- adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S- adenosylmethionine inhibition
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • ATP + H2O + L-Methionine --> S-Adenosyl-L-methionine + Phosphate + Diphosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 6815285 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9NZL9 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name MAT2B_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AF182814 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID MAT2B Link Image
Enzyme 3 HGNC ID HGNC:6905 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. LeGros HL Jr, Halim AB, Geller AM, Kotb M: Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II). J Biol Chem. 2000 Jan 28;275(4):2359-66. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15078
Enzyme 4 Name Methionyl-tRNA synthetase, mitochondrial
Enzyme 4 Synonyms
  1. Mitochondrial methionine--tRNA ligase
  2. MtMetRS
  3. Methionine--tRNA ligase 2
Enzyme 4 Gene Name MARS2
Enzyme 4 Protein Sequence >Methionyl-tRNA synthetase, mitochondrial 
MLRTSVLRLLGRTGASRLSLLEDFGPRYYSSGSLSAGDDACDVRAYFTTPIFYVNAAPHI
GHLYSALLADALCRHRRLRGPSTAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQ
FQQLFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEA
KVTQQPGPSGDSFPVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHH
VVLQWLDEELPDLSVSRRSSHLHWGIPVPGDDSQTIYVWLDALVNYLTVIGYPNAEFKSW
WPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPRT
CLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRCTAKRINPSET
YPAFCTTCFPSEPGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCV
RQTNGFVQRHAPWKLNWESPVDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRLG
VSASERSLGELYFLPRFYGHPCPFEGRRLGPETGLLFPRLDQSRTWLVKAHRT
Enzyme 4 Number of Residues 593
Enzyme 4 Molecular Weight 66591
Enzyme 4 Theoretical pI 8.14
Enzyme 4 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • methionine-tRNA ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • metabolism
  • methionyl-tRNA aminoacylation
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
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Enzyme 4 General Function Translation, ribosomal structure and biogenesis
Enzyme 4 Specific Function ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 37196758 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q96GW9 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SYMM_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1782 bp 
ATGCTGCGAACGTCCGTCCTCCGCCTGCTAGGACGCACGGGGGCTAGTAGGCTGTCTCTC
CTGGAGGACTTCGGCCCACGCTACTACAGTTCGGGCTCCCTCAGTGCCGGCGATGATGCT
TGTGATGTGCGCGCCTACTTCACTACACCCATTTTCTACGTGAACGCGGCGCCGCACATC
GGGCACCTGTACTCGGCACTACTGGCGGACGCCCTATGCCGCCACCGTCGCCTCCGAGGT
CCCAGCACGGCCGCCACGCGATTCTCCACTGGTACCGACGAGCACGGGCTGAAGATTCAG
CAGGCAGCAGCTACCGCGGGCCTGGCCCCGACCGAGCTGTGCGACCGAGTCTCTGAGCAG
TTCCAGCAGCTTTTCCAGGAGGCCGGTATCTCCTGCACAGATTTCATCCGCACCACGGAG
GCCCGGCACCGGGTGGCTGTGCAGCACTTCTGGGGGGTGCTTAAGTCCCGCGGTCTGCTC
TACAAGGGCGTCTATGAAGGTTGGTATTGCGCTTCCGACGAGTGCTTCCTGCCTGAGGCC
AAGGTCACCCAGCAGCCGGGCCCATCGGGGGATTCGTTTCCTGTATCTCTCGAGAGCGGG
CATCCAGTCTCCTGGACCAAGGAAGAAAACTACATTTTCAGGCTTTCCCAGTTCCGGAAG
CCACTCCAGCGGTGGCTGCGGGGCAACCCTCAGGCGATCACCCCCGAACCATTTCATCAC
GTAGTTCTTCAGTGGCTGGACGAGGAGCTGCCCGACCTGTCCGTGTCTCGCAGAAGTAGC
CACTTGCACTGGGGCATTCCGGTGCCCGGGGATGATTCGCAGACCATCTATGTATGGCTG
GATGCCCTGGTCAACTACCTCACTGTAATTGGCTACCCAAATGCTGAGTTCAAATCTTGG
TGGCCGGCCACCTCTCATATCATAGGTAAGGACATTCTCAAATTCCATGCCATCTATTGG
CCTGCCTTCCTGTTAGGGGCCGGCATGAGCCCGCCACAGCGCATCTGTGTCCATTCCCAC
TGGACAGTCTGTGGCCAAAAGATGTCCAAGAGCTTGGGCAACGTGGTGGATCCTAGGACT
TGCCTTAACCGCTATACCGTGGATGGCTTCCGCTACTTTCTCCTTCGGCAGGGCGTCCCC
AACTGGGACTGTGACTACTATGATGAAAAGGTGGTTAAGTTGCTGAACTCCGAGCTGGCA
GATGCCTTGGGAGGTCTCTTGAACCGATGCACTGCCAAAAGAATAAATCCTTCTGAGACC
TACCCAGCCTTCTGCACTACCTGCTTCCCTAGTGAGCCAGGGTTGGTGGGGCCGTCAGTT
CGTGCTCAGGCAGAGGATTATGCTCTGGTGAGCGCAGTGGCCACTTTGCCAAAGCAGGTA
GCAGACCACTATGATAACTTTCGGATATATAAGGCTCTGGAGGCCGTGTCCAGCTGTGTC
CGGCAAACTAATGGTTTTGTCCAAAGGCATGCACCATGGAAGCTGAACTGGGAGAGCCCA
GTGGATGCTCCCTGGCTGGGTACTGTGCTTCATGTGGCCTTGGAATGTTTGCGAGTCTTT
GGGACTTTGCTGCAGCCTGTCACCCCAAGCCTAGCTGACAAGATGATGTCTAGGCTGGGG
GTCTCTGCCTCAGAGAGGAGTCTTGGAGAGCTCTATTTCTTGCCTCGATTCTATGGACAT
CCATGCCCTTTTGAAGGGAGGAGGCTGGGACCTGAAACTGGGCTTTTGTTTCCAAGACTA
GACCAGTCCAGGACTTGGCTGGTGAAAGCCCACCGGACCTAG
Enzyme 4 GenBank Gene ID AB107013 Link Image
Enzyme 4 GeneCard ID Q96GW9 Link Image
Enzyme 4 GenAtlas ID MARS2 Link Image
Enzyme 4 HGNC ID HGNC:25133 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16535
Enzyme 5 Name Methionine adenosyltransferase II, beta, isoform CRA_a
Enzyme 5 Synonyms
  1. SubName: cDNA, FLJ92687, Homo sapiens methionine adenosyltransferase II, beta (MAT2B), mRNA
Enzyme 5 Gene Name MAT2B
Enzyme 5 Protein Sequence >Methionine adenosyltransferase II, beta, isoform CRA_a 
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
Enzyme 5 Number of Residues 334
Enzyme 5 Molecular Weight 37552
Enzyme 5 Theoretical pI 7.39
Enzyme 5 GO Classification
Function
  • catalytic activity
  • dTDP-4-dehydrorhamnose reductase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carbohydrate biosynthesis
  • extracellular polysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
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Enzyme 5 General Function Cell wall/membrane/envelope biogenesis
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B2R5Y6 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B2R5Y6_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK312365 Link Image
Enzyme 5 GeneCard ID B2R5Y6 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available