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Human Metabolome Database Version 2.5

 

Showing metabocard for Se-Adenosylselenomethionine (HMDB11118)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-10-16 23:33:06
Update Date 2009-10-02 16:14:18
Accession Number HMDB11118
Secondary Accession Numbers Not Available
Common Name Se-Adenosylselenomethionine
Description Se-Adenosylselenomethionine is an intermediate in Selenoamino acid metabolism. Se-Adenosylselenomethionine is converted from Selenomethionine via the enzyme S-adenosylmethionine synthetase (EC 2.5.1.6). It is then converted to Se-Adenosylselenohomocysteine via the enzyme Transferases (EC 2.1.1.-).
Synonyms Not Available
Chemical IUPAC Name Not Available
Chemical Formula C15H23N6O5Se
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
Class
Sub Class
Family
  • Mammalian Metabolite
Species
  • cation
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • primary aromatic amine
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 446.340
Monoisotopic Molecular Weight 447.089508
Isomeric SMILES C[Se+](CCC(N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C1N=CN=C2N
Canonical SMILES C[Se+](CCC(N)C(O)=O)CC1OC(C(O)C1O)N1C=NC2=C1N=CN=C2N
KEGG Compound ID C05691 Link Image
BioCyc ID Not Available
BiGG ID 46296 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB11118 Link Image
Metagene Link HMDB11118 Link Image
METLIN ID Not Available
PubChem Compound 24892761 Link Image
PubChem Substance 7998 Link Image
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C15H22N6O5Se/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/p+1/t7?,8-,10-,11-,14-,27?/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.79 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.93 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Selenoamino Acid Metabolism SMP00029 Link Image map00450 Link Image
General References Not Available
Metabolic Enzymes
  1. S-adenosylmethionine synthase isoform type-1
  2. Protein arginine N-methyltransferase 3
  3. Methionine adenosyltransferase 2 subunit beta
  4. Methionine adenosyltransferase II, beta, isoform CRA_a
Enzyme 1 [top]
Enzyme 1 ID 5655
Enzyme 1 Name S-adenosylmethionine synthase isoform type-1
Enzyme 1 Synonyms
  1. AdoMet synthase 1
  2. Methionine adenosyltransferase 1
  3. MAT 1
  4. Methionine adenosyltransferase I/III
  5. MAT-I/III
Enzyme 1 Gene Name MAT1A
Enzyme 1 Protein Sequence >S-adenosylmethionine synthase isoform type-1
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
Enzyme 1 Number of Residues 395
Enzyme 1 Molecular Weight 43647.6
Enzyme 1 Theoretical pI 6.24
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • methionine adenosyltransferase activity
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 1 General Function Involved in methionine adenosyltransferase activity
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 [RN:R00177]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 55959182 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
TATGCTACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGGCGGCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTAGACCGCTCAGCTGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGATTTGGACTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
Enzyme 1 GenBank Gene ID AL359195 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 1
Enzyme 1 Locus 10q22
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. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. 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]
  7. 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]
  8. 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 5714
Enzyme 2 Name Protein arginine N-methyltransferase 3
Enzyme 2 Synonyms
  1. Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
Enzyme 2 Gene Name PRMT3
Enzyme 2 Protein Sequence >Protein arginine N-methyltransferase 3
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSA
EETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEY
LKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAR
EDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRT
ESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLN
KLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYP
DICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIK
HIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHW
KQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ
Enzyme 2 Number of Residues 531
Enzyme 2 Molecular Weight 59902.7
Enzyme 2 Theoretical pI 5.00
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • protein methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid alkylation
  • protein amino acid methylation
  • protein modification process
Component
  • cell part
  • cytoplasm
  • intracellular
  • intracellular part
Enzyme 2 General Function Involved in protein methyltransferase activity
Enzyme 2 Specific Function Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 45946104 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O60678 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ANM3_HUMAN Link Image
Enzyme 2 PDB ID 1F3L Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1596 bp
ATGTGCTCGTTAGCGTCAGGCGCTACCGGCGGCCGGGGCGCTGTGGAGAATGAGGAGGAC
CTGCCAGAACTGTCGGACAGCGGGGACGAGGCCGCCTGGGAGGATGAGGACGATGCAGAT
CTCCCCCACGGCAAGCAGCAGACCCCCTGCCTGTTCTGTAACAGGTTATTCACATCTGCT
GAAGAAACATTTTCACACTGTAAGTCTGAGCATCAGTTTAATATTGACAGCATGGTTCAT
AAACATGGACTTGAATTTTATGGATACATTAAGCTAATAAATTTTATTAGACTTAAGAAT
CCTACAGTTGAGTACATGAATTCCATATACAACCCAGTGCCTTGGGAGAAAGAAGAGTAT
TTGAAGCCAGTATTAGAAGATGACCTTTTACTTCAATTTGATGTAGAAGATCTTTATGAA
CCGGTGTCAGTACCCTTCTCATACCCCAATGGACTCAGTGAAAATACATCTGTTGTTGAA
AAATTGAAACATATGGAAGCCAGGGCACTGTCTGCTGAAGCCGCATTGGCCAGAGCACGT
GAGGATCTGCAGAAAATGAAACAATTTGCTCAGGATTTTGTGATGCACACAGATGTCAGA
ACCTGCTCGTCATCTACTAGTGTCATTGCGGACCTCCAGGAGGATGAGGATGGTGTTTAT
TTCAGCTCATACGGGCATTATGGGATACATGAAGAAATGCTAAAGGACAAAATACGAACA
GAAAGCTACCGAGATTTCATATACCAAAATCCACATATCTTCAAAGACAAGGTAGTTTTG
GATGTTGGGTGTGGAACTGGAATTCTCTCTATGTTTGCTGCTAAAGCTGGGGCGAAGAAG
GTTCTTGGAGTTGATCAATCTGAAATACTTTACCAGGCAATGGATATTATAAGACTAAAT
AAACTTGAAGATACTATTACACTAATTAAAGGAAAGATTGAAGAAGTTCATCTTCCTGTA
GAAAAAGTAGATGTTATCATATCTGAGTGGATGGGCTATTTTCTTCTGTTTGAGTCTATG
TTAGATTCTGTCCTTTATGCAAAGAACAAATACTTGGCAAAAGGAGGCTCGGTCTACCCT
GACATTTGCACTATCAGCCTTGTAGCAGTGAGTGATGTGAATAAACATGCTGATAGAATT
GCTTTTTGGGATGATGTCTATGGCTTCAAGATGTCCTGCATGAAGAAAGCAGTTATTCCA
GAAGCTGTTGTGGAAGTTTTAGATCCGAAGACTCTTATTTCAGAACCTTGTGGTATTAAG
CATATAGATTGCCATACGACGTCTATCTCAGATTTGGAATTTTCATCAGATTTTACCCTG
AAAATCACAAGGACATCCATGTGCACGGCAATTGCTGGCTACTTTGATATATATTTTGAG
AAGAATTGCCACAACAGGGTCGTGTTCTCTACGGGCCCTCAGAGCACCAAAACACACTGG
AAACAAACAGTATTTCTACTGGAAAAACCATTTTCAGTTAAAGCAGGTGAAGCCTTGAAA
GGAAAGGTCACAGTTCACAAGAATAAGAAAGATCCACGTTCTCTCACCGTGACCCTCACG
TTGAATAATTCAACTCAAACTTATGGTCTCCAGTGA
Enzyme 2 GenBank Gene ID BC037544 Link Image
Enzyme 2 GeneCard ID PRMT3 Link Image
Enzyme 2 GenAtlas ID PRMT3 Link Image
Enzyme 2 HGNC ID HGNC:30163 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 11p15.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Tang J, Gary JD, Clarke S, Herschman HR: PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J Biol Chem. 1998 Jul 3;273(27):16935-45. [PubMed Link Image]
  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. Epub 2008 Jul 31. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  5. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  6. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [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. DTDP-4-keto-6-deoxy-D-glucose 4-reductase
  2. Methionine adenosyltransferase II beta
  3. MAT II beta
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 37551.5
Enzyme 3 Theoretical pI 7.39
Enzyme 3 GO Classification
Function
  • binding
  • 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 metabolic process
  • cellular polysaccharide biosynthetic process
  • extracellular polysaccharide biosynthetic process
  • metabolic process
  • polysaccharide biosynthetic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
Enzyme 3 General Function Involved in dTDP-4-dehydrorhamnose reductase activity
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 Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
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 >1005 bp
ATGGTGGGGAGGGAGAAAGAACTGTCTATACACTTTGTTCCCGGGAGCTGTCGGCTGGTG
GAGGAGGAAGTTAACATCCCTAATAGGAGGGTTCTGGTTACTGGTGCCACTGGGCTTCTT
GGCAGAGCTGTACACAAAGAATTTCAGCAGAATAATTGGCATGCAGTTGGCTGTGGTTTC
AGAAGAGCAAGACCAAAATTTGAACAGGTTAATCTGTTGGATTCTAATGCAGTTCATCAC
ATCATTCATGATTTTCAGCCCCATGTTATAGTACATTGTGCAGCAGAGAGAAGACCAGAT
GTTGTAGAAAATCAGCCAGATGCTGCCTCTCAACTTAATGTGGATGCTTCTGGGAATTTA
GCAAAGGAAGCAGCTGCTGTTGGAGCATTTCTCATCTACATTAGCTCAGATTATGTATTT
GATGGAACAAATCCACCTTACAGAGAGGAAGACATACCAGCTCCCCTAAATTTGTATGGC
AAAACAAAATTAGATGGAGAAAAGGCTGTCCTGGAGAACAATCTAGGAGCTGCTGTTTTG
AGGATTCCTATTCTGTATGGGGAAGTTGAAAAGCTCGAAGAAAGTGCTGTGACTGTTATG
TTTGATAAAGTGCAGTTCAGCAACAAGTCAGCAAACATGGATCACTGGCAGCAGAGGTTC
CCCACACATGTCAAAGATGTGGCCACTGTGTGCCGGCAGCTAGCAGAGAAGAGAATGCTG
GATCCATCAATTAAGGGAACCTTTCACTGGTCTGGCAATGAACAGATGACTAAGTATGAA
ATGGCATGTGCAATTGCAGATGCCTTCAACCTCCCCAGCAGTCACTTAAGACCTATTACT
GACAGCCCTGTCCTAGGAGCACAACGTCCGAGAAATGCTCAGCTTGACTGCTCCAAATTG
GAGACCTTGGGCATTGGCCAACGAACACCATTTCGAATTGGAATCAAAGAATCACTTTGG
CCTTTCCTCATTGACAAGAGATGGAGACAAACGGTCTTTCATTAG
Enzyme 3 GenBank Gene ID AF182814 Link Image
Enzyme 3 GeneCard ID MAT2B Link Image
Enzyme 3 GenAtlas ID MAT2B Link Image
Enzyme 3 HGNC ID HGNC:6905 Link Image
Enzyme 3 Chromosome Location 5
Enzyme 3 Locus 5q34-q35
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. Ohira M, Morohashi A, Nakamura Y, Isogai E, Furuya K, Hamano S, Machida T, Aoyama M, Fukumura M, Miyazaki K, Suzuki Y, Sugano S, Hirato J, Nakagawara A: Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma. Cancer Lett. 2003 Jul 18;197(1-2):63-8. [PubMed Link Image]
  4. 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]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. LeGros L, Halim AB, Chamberlin ME, Geller A, Kotb M: Regulation of the human MAT2B gene encoding the regulatory beta subunit of methionine adenosyltransferase, MAT II. J Biol Chem. 2001 Jul 6;276(27):24918-24. Epub 2001 May 3. [PubMed Link Image]
  8. Martinez-Chantar ML, Garcia-Trevijano ER, Latasa MU, Martin-Duce A, Fortes P, Caballeria J, Avila MA, Mato JM: Methionine adenosyltransferase II beta subunit gene expression provides a proliferative advantage in human hepatoma. Gastroenterology. 2003 Apr;124(4):940-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16535
Enzyme 4 Name Methionine adenosyltransferase II, beta, isoform CRA_a
Enzyme 4 Synonyms
  1. SubName: cDNA, FLJ92687, Homo sapiens methionine adenosyltransferase II, beta (MAT2B), mRNA
Enzyme 4 Gene Name MAT2B
Enzyme 4 Protein Sequence >Methionine adenosyltransferase II, beta, isoform CRA_a
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
Enzyme 4 Number of Residues 334
Enzyme 4 Molecular Weight 37552
Enzyme 4 Theoretical pI 7.39
Enzyme 4 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 4 General Function Cell wall/membrane/envelope biogenesis
Enzyme 4 Specific Function Not Available
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 Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID B2R5Y6 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B2R5Y6_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK312365 Link Image
Enzyme 4 GeneCard ID B2R5Y6 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
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