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Human Metabolome Database Version 2.5

 

Showing metabocard for 6,7-Dimethyl-8-(1-D-ribityl)lumazine (HMDB03826)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 06:28:05
Update Date 2009-05-05 20:59:44
Accession Number HMDB03826
Secondary Accession Numbers Not Available
Common Name 6,7-Dimethyl-8-(1-D-ribityl)lumazine
Description 6,7-Dimethyl-8-(1-D-ribityl)lumazine is an intermediate in riboflavin metabolism. 6,7-Dimethyl-8-(1-D-ribityl)lumazine is the second to last step in the synthesis of ribitol and is converted from 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine via the enzyme riboflavin synthase beta chain. It is then converted to riboflavin via the enzyme riboflavin synthase alpha chain (EC:2.5.1.9).
Synonyms
  1. DMDRL
  2. 6,7-Dimethyl-8-ribityllumazine
  3. 6,7-Dimethyl-8-(1'-D-ribityl)lumazine
  4. 6,7-dimethyl-8-(1-D-ribityl)lumazine
  5. 1-deoxy-1-[6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl]-D-ribitol
  6. 1-Deoxy-1-(3,4-dihydro-6,7-dimethyl-2,4-dioxo-8(2H)-pteridinyl)-ribitol
  7. 6,7-dimethyl-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]pteridine-2,4-dione
Chemical IUPAC Name 6,7-dimethyl-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]pteridine-2,4-dione
Chemical Formula C13H18N4O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
—
Class
—
Sub Class
—
Family
  • Microbial Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 326.305
Monoisotopic Molecular Weight 326.122620
Isomeric SMILES CC1=C(C)N(CC(O)C(O)C(O)CO)C2=NC(=O)NC(=O)C2=N1
Canonical SMILES CC1=C(C)N(CC(O)C(O)C(O)CO)C2=NC(=O)NC(=O)C2=N1
KEGG Compound ID C04332 Link Image
BioCyc ID DIMETHYL-D-RIBITYL-LUMAZINE Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB03826 Link Image
Metagene Link HMDB03826 Link Image
METLIN ID Not Available
PubChem Compound 168989 Link Image
PubChem Substance 6983 Link Image
ChEBI ID 17601 Link Image
CAS Registry Number 5118-16-1
InChI Identifier InChI=1/C13H18N4O6/c1-5-6(2)17(3-7(19)10(21)8(20)4-18)11-9(14-5)12(22)16-13(23)15-11/h7-8,10,18-21H,3-4H2,1-2H3,(H,16,22,23)
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.23 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity -3.145 Source: PhysProp
Predicted LogP/Hydrophobicity -3.3 [Predicted by PubChem via XLOGP] 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
Riboflavin Metabolism SMP00070 Link Image map00740 Link Image
General References Not Available
Metabolic Enzymes
  1. Riboflavin synthase alpha chain
  2. Riboflavin synthase alpha chain
  3. Riboflavin synthase alpha chain
  4. Riboflavin synthase alpha subunit
  5. Riboflavin synthase, alpha subunit
  6. Riboflavin synthase, alpha subunit
  7. Riboflavin synthase alpha chain
  8. Riboflavin synthase, alpha subunit
Enzyme 1 [top]
Enzyme 1 ID 16328
Enzyme 1 Name Riboflavin synthase alpha chain
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name ribE
Enzyme 1 Protein Sequence >Riboflavin synthase alpha chain 
MFSGIVEEYATVVALVKDQENIHFTLKCSFVNELKIDQSISHNGVCLTVVSMTEDTYTVT
AMKETLDRSNLRLLKVGDKVNVERSMMMNGRLDGHIVQGHVDQTAECIDIKDADGSWYFT
FKYAFDKEMAKRGYITVDKGSVTVNGVSLTVCNPTDDTFQVAIIPYTYEHTNFHTFGKGS
VVNLEFDIIGKYISRMIQYK
Enzyme 1 Number of Residues 200
Enzyme 1 Molecular Weight 22596.7
Enzyme 1 Theoretical pI 5.59
Enzyme 1 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 1 General Function Involved in riboflavin synthase activity
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine [RN:R00066]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 60491220 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q5LBQ6 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name Q5LBQ6_BACFN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >603 bp 
ATGAAAAAATCCTTCGAAGAGGCCCTCAAACACAGAAGGACCTATTATTCGATAACAAAC
CAGTCTCCGGTTTCTGATGAGGAAATAGAGCGGATTGTCAATTTAGCTGTCACTCATGTG
CCTTCTGCTTTCAACTCTCAATCGACTCGTGTAGTGCTATTGTTGGGTGAGAATCATAAG
AAATTATGGCATATCGTAAAAGAAACATTGCGAAAGATCGTCCCACCGGAAGTTTTTAAA
ACGACGGAAGCCAAAATCGACAACTCTTTTGCAAGCGGATACGGAACTGTTTTATTCTTC
GAAGATCAGTCGGTCGTTAAGGGATTGCAGGAAGCATTCAGCAGTTATAAGGATAACTTC
CCCGGGTGGTCGCTGCAGACTTCTGCGATGCATCAGCTGGCTGTATGGACGATGTTGGAA
GATGTCGGCTTCGGAGCTTCTTTGCAACATTACAATCCGCTGATCGATGAAGAAGTACGC
CATACCTGGCATTTGCCTGAAGAGTGGCATCTGATTGCCGAAATGCCGTTTGGACTTCCG
GTACAGGGACCTGGCGATAAAGATTTTAAAGATTTGGATACCCGGGTCAAGGTATTTAAA
TAA
Enzyme 1 GenBank Gene ID CR626927 Link Image
Enzyme 1 GeneCard ID ribE Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus BF2767
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Cerdeno-Tarraga AM, Patrick S, Crossman LC, Blakely G, Abratt V, Lennard N, Poxton I, Duerden B, Harris B, Quail MA, Barron A, Clark L, Corton C, Doggett J, Holden MT, Larke N, Line A, Lord A, Norbertczak H, Ormond D, Price C, Rabbinowitsch E, Woodward J, Barrell B, Parkhill J: Extensive DNA inversions in the B. fragilis genome control variable gene expression. Science. 2005 Mar 4;307(5714):1463-5. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 16329
Enzyme 2 Name Riboflavin synthase alpha chain
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name Not Available
Enzyme 2 Protein Sequence >Riboflavin synthase alpha chain 
MFSGIVEEYATVVALVKDQENIHFTLKCSFVNELKIDQSISHNGVCLTVVSMTEDTYTVT
AMKETLDRSNLRLLKVGDKVNVERSMMMNGRLDGHIVQGHVDQTAECIDIKDADGSWYFT
FKYAFDKEMAKRGYITVDKGSVTVNGVSLTVCNPTDDTFQVAIIPYTYEHTNFHTFGKGS
VVNLEFDIIGKYISRMIQYK
Enzyme 2 Number of Residues 200
Enzyme 2 Molecular Weight 22596.7
Enzyme 2 Theoretical pI 5.59
Enzyme 2 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function Not Available
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 52214388 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q64SM7 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q64SM7_BACFR Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >603 bp 
ATGAAAAAATCCTTCGAAGAGGCCCTCAAACACAGAAGGACCTATTATTCGATAACAAAC
CAGTCTCCGGTTTCTGATGAGGAAATAGAGCGGATTGTCAATTTAGCTGTCACTCATGTG
CCTTCTGCTTTCAACTCTCAATCGACTCGTGTAGTGCTATTGCTGGGTGAGAATCATAAG
AAATTATGGCATATCGTAAAAGAAACATTGCGAAAGATCGTCCCACCGGAAGTTTTTAAA
ACGACGGAAGCCAAAATCGACAACTCTTTTGCAAGCGGATACGGAACTGTTTTATTCTTC
GAAGATCAGTCGGTCGTTAAGGGATTGCAGGAAGCATTCAGCAGTTATAAGGATAACTTC
CCCGGGTGGTCGCTGCAGACTTCTGCGATGCATCAGCTGGCTGTATGGACGATGCTGGAA
GATGTCGGCTTCGGAGCTTCTTTGCAACATTACAATCCGCTGATCGATGAAGAAGTACGC
CATACCTGGCATTTGCCTGAAGAGTGGCATCTGATTGCCGAAATGCCGTTTGGACTTCCG
GTACAGGGACCTGGCGATAAAGATTTTAAAGATTTGGATACCCGGGTCAAGGTATTTAAA
TAA
Enzyme 2 GenBank Gene ID AP006841 Link Image
Enzyme 2 GeneCard ID Not Available
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus BF2752
Enzyme 2 SNPs Not Available
Enzyme 2 General References
  1. Kuwahara T, Yamashita A, Hirakawa H, Nakayama H, Toh H, Okada N, Kuhara S, Hattori M, Hayashi T, Ohnishi Y: Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation. Proc Natl Acad Sci U S A. 2004 Oct 12;101(41):14919-24. Epub 2004 Oct 4. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 16330
Enzyme 3 Name Riboflavin synthase alpha chain
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name ribB
Enzyme 3 Protein Sequence >Riboflavin synthase alpha chain 
MFTGIVEEVGILRKITANGKSGKVTILSNKILDGTNLGDSIAVNGVCLTVSNLGKNEFTA
DVMMETIRSTNLGLLNANDKVNLERAMSLSSRFGGHIVTGHVDGKGTICKFEKDENAVLV
SIRPDKKLLSSMILKGSVAIDGVSLTISYLDDEIFKVSIIPHTKINTILLTKNVGDFVNL
ESDVIGKYVNNFMANNYKELNSNSSNHKSNIDKDFLFKNGF
Enzyme 3 Number of Residues 221
Enzyme 3 Molecular Weight 24032.4
Enzyme 3 Theoretical pI 8.22
Enzyme 3 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 3 General Function Involved in riboflavin synthase activity
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine [RN:R00066]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 115249269 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q186Q6 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q186Q6_CLOD6 Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >666 bp 
ATGGAACTATTATCAAAATTACCTTTGGCTGATGTACCATATACAAGTTCAATGCAATTG
TTTTTATTTCTAACTGCATTAATGTTTTTACCATTTGTAATGTTCATGATGACAAGCTTT
GTCAGAATAGTTATAAGTTTATCATTTTTGAAATCAGCATTAGGAGCACAGCAAGCAATT
CCAAGTCAAATTTTGGTAGGACTTGCAATAGTATTGACAATATTTATAATGAGACCAGTA
TTAAATGAGATAAACGAAAAGGCATTACAACCATATATGAAAGAAGAAGTTACTATGGAA
GAAGCTATGAAGGAAGCAGAAGGACCTATTAAAGAGTTTTTATTAACACAAACCAGACAG
ACAGATTTAGATTTATTTGTAGAACAGGCTGGTTTAAAAGAAAAGAAATTAACTCGTGAA
AATATACCACTATCTGTTGTAGTTCCAGCATTTGCTATAAGCGAACTAAAAACTGCTTTT
CAAATAGGTTTTTTAATATATATACCATTTTTGATAATAGACCTTGTTGTGGCAAGTGTT
TTGATGTCTATGGGTATGTTTATGTTGCCTCCAGTCATGATATCATTACCATTTAAGTTA
TTATTATTTGTAATGGTGGATGGATGGAACTTGATAGTAAAAACATTGATATTGGGATTT
GGATAG
Enzyme 3 GenBank Gene ID AM180355 Link Image
Enzyme 3 GeneCard ID ribB Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus CD1699
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Sebaihia M, Wren BW, Mullany P, Fairweather NF, Minton N, Stabler R, Thomson NR, Roberts AP, Cerdeno-Tarraga AM, Wang H, Holden MT, Wright A, Churcher C, Quail MA, Baker S, Bason N, Brooks K, Chillingworth T, Cronin A, Davis P, Dowd L, Fraser A, Feltwell T, Hance Z, Holroyd S, Jagels K, Moule S, Mungall K, Price C, Rabbinowitsch E, Sharp S, Simmonds M, Stevens K, Unwin L, Whithead S, Dupuy B, Dougan G, Barrell B, Parkhill J: The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat Genet. 2006 Jul;38(7):779-86. Epub 2006 Jun 25. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16331
Enzyme 4 Name Riboflavin synthase alpha subunit
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name risA
Enzyme 4 Protein Sequence >Riboflavin synthase alpha subunit 
MFTGIVEEIGEVISIDKNEKSSLLKIRANKVLEDTKIGDSISTNGVCLTITTKGKDYFTA
YVMGETLRKSNIGNLKKSSKVNLERAMSINSRFNGHIVTGHIDSTGEIISFKDEGEAIWV
EIKVSYELSKYIVYKGSIAIDGISLTIAEVKGESFKVSVIPHSQEETTLTKRKIGDLVNI
ECDPIGKYVEKLLGFNKDNRKKKSVLTEEFLTINGFI
Enzyme 4 Number of Residues 217
Enzyme 4 Molecular Weight 24089.5
Enzyme 4 Theoretical pI 8.19
Enzyme 4 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 4 General Function Involved in riboflavin synthase activity
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 18144151 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8XMX1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q8XMX1_CLOPE Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >654 bp 
ATGTTAATATTAGAAAGTAATTCACAGTCAGTGGCAGCTGAAAGTTATAGAACCTTAAGA
ACAAATATACAATACTCTTCCTTTGATAATCCTGTTAAGTCAATTGTTATAACTAGTTCA
GAGCCAGGAGAAGGAAAATCGACAACAAGTGCTAACTTAGCTCTTTCCTTTGCGCAAGAT
GGAAAAAGGGTTATCATTATAGACTGTGATTTAAGAAAACCAGTTGTACATAAAAACTTG
GGAATAAGTAATTCTATAGGGCTATCAGAATTTTTAATTGGAAAGGCTGAATTTTCTAAG
GTAGTTTACAAACATGAATCAGGACTTCATGTATTACCTTCAGGTTTAGTTCCTCCAAAT
CCAGCTGAGATGTTAGCTTCAAGAGCTATGGAGCATCTTTTAACTCAATTAGAGGAAAAA
TATGATTATATAATATTAGATACTCCTCCAGTTAATGCAGTAACAGATTCAAAAATACTT
TCAACAAAGGTGGATGGAACAATATTAGTTGTAAAGTATGGTTATACAAAGAAGGATGCT
GTAATAGAAGCTGTAAAGGGATTAAGAGCAGTTAAAGCTAATATAATAGGAACAGTATTT
AATGGAGAGGAAAATCAAAGGGGAAAATACTATCATTATTATAAAAAAGATTAA
Enzyme 4 GenBank Gene ID BA000016 Link Image
Enzyme 4 GeneCard ID risA Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus CPE0567
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Shimizu T, Ohtani K, Hirakawa H, Ohshima K, Yamashita A, Shiba T, Ogasawara N, Hattori M, Kuhara S, Hayashi H: Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):996-1001. Epub 2002 Jan 15. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16332
Enzyme 5 Name Riboflavin synthase, alpha subunit
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name ribE
Enzyme 5 Protein Sequence >Riboflavin synthase, alpha subunit 
MFTGIVEEIGEVISIDKNEKSSLLKIRANKVLEDTKIGDSISTNGVCLTITTKGKDYFTA
YVMGETLRKSNLGNLKKSSKVNLERAMSINGRFNGHIVTGHIDSTGEIISFKDEGEAIWV
EIKVSYELSKYIVYKGSIAIDGISLTIAEVKGESFKVSVIPHSQEETTLTKRKIGDLVNI
ECDSIGKYVEKLLGFKKDSRKKKSVLTEEFLTINGFI
Enzyme 5 Number of Residues 217
Enzyme 5 Molecular Weight 24036.5
Enzyme 5 Theoretical pI 8.63
Enzyme 5 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 5 General Function Involved in riboflavin synthase activity
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine [RN:R00066]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 110673895 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q0TTN9 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q0TTN9_CLOP1 Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >654 bp 
ATGTTAATATTAGAAAATAATCCAAAATCAGTGGCAGCTGAAAGTTATAGAACCTTAAGA
ACAAACATACAATACTCTTCCTTTGATAATCCAGTAAAATCTATTGTTATTACTAGTTCT
GAGCCAGGAGAAGGAAAGTCAACAACAAGTGCTAACTTAGCTCTTTCCTTTGCGCAAGAT
GGAAAAAAGGTAATTCTTATAGATTGTGATTTAAGAAAACCAGTTGTACATAAAGAATTT
CAAATTAGTAATTCTAGAGGATTATCAGAATTTTTAATTGGAAATGTTGAATTTTCTAAG
GTGGTTTACAAACATGAATCAGGACTTCATGTACTACCTTCAGGATTAGTTCCTCCAAAC
CCTGCTGAGATGTTAGCTTCAAGAGCTATGGAACATCTTTTAACTCAATTAGAGGAAAAA
TATGATTACATAATATTAGATACTCCTCCAGTTAATGCAGTAACAGATTCAAAAATACTT
TCAACAAAGGTAGATGGAACAATACTAGTTGTAAAGTATGGATATACAAAAAAGGATGCT
GTAATTGAAGCTGTAAAGGGCTTAAGGGCAGTTAATGCTAATATAATAGGAACAGTATTT
AATGGAGAGGAAAATCAAAGGGGAAAATACTATCATTATTATAAAAAAGATTAA
Enzyme 5 GenBank Gene ID CP000246 Link Image
Enzyme 5 GeneCard ID ribE Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus CPF_0547
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16333
Enzyme 6 Name Riboflavin synthase, alpha subunit
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name ribE
Enzyme 6 Protein Sequence >Riboflavin synthase, alpha subunit 
MFTGIVEEIGEVISIDKNEKSSLLKIRANKVLEDTKIGDSISTNGVCLTITTKGKDYFTA
YVMGETLRKSNLGNLKKSSKVNLERAMSINGRFNGHIVTGHIDSTGEIISFKDEGEAIWV
EIKVSYELSKYIVYKGSIAIDGISLTIAEVKGESFKVSVIPHSQEETTLTKRKIGDLVNI
ECDPIGKYVEKLLGFKKDSRKKKSVLTEEFLTINGFI
Enzyme 6 Number of Residues 217
Enzyme 6 Molecular Weight 24046.5
Enzyme 6 Theoretical pI 8.63
Enzyme 6 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 6 General Function Involved in riboflavin synthase activity
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine [RN:R00066]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 110684379 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q0SVJ1 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q0SVJ1_CLOPS Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >654 bp 
ATGTTAATATTAGAGAAAAATCCAAAGTCAGTAGCAGCTGAAAGTTATAGAACCTTAAGA
ACAAACATACAATACTCTTCCTTTGATAATCCGGTAAAATCTATTGTTATTACTAGCTCT
GAGCCAGGAGAAGGTAAATCAACAACAAGTGCTAACTTAGCTCTTTCCTTTGCGCAAGAT
GGAAAAAAAGTAATACTTATAGACTGTGATTTAAGAAAACCAGTTGTACATAAAGAATTT
CAAATTAGTAATTCTAGAGGATTATCAGAATTTTTAATTGGAAATGTTGAATTTTCTAAG
GTGGTTTATAAACATGAATCAGGACTTCATGTCTTGCCTTCGGGATTAGTTCCTCCAAAT
CCAGCTGAAATGTTAGCTTCAAGATCTATGGAGCATCTTTTAACTCAATTAGAAGAAAAG
TATGATTACATAATATTAGACACTCCTCCAGTTAATGCAGTTACAGATTCAAAAATACTT
TCAACAAAGGTTGATGGAACAATACTTGTTGTAAAGTATGGTTATACAAAGAAGGATGGA
GTAATAGAGGCTGTAAAGGGACTAAGAGCAGTTAAAGCTAATATAATAGGAACAGTATTT
AATGGAGAGGAAAATCAAAGGGGAAAATACTATCACTATTATAAGAAAGATTAA
Enzyme 6 GenBank Gene ID CP000312 Link Image
Enzyme 6 GeneCard ID ribE Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus CPR_0531
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16334
Enzyme 7 Name Riboflavin synthase alpha chain
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name ribE
Enzyme 7 Protein Sequence >Riboflavin synthase alpha chain 
MFTGIVQGTAKLVSIDEKPNFRTHVVELPDHMLDGLETGASVAHNGCCLTVTEINGNHVS
FDLMKETLRITNLGDLKVGDWVNVERAAKFSDEIGGHLMSGHIMTTAEVAKILTSENNRQ
IWFKVQDSQLMKYILYKGFIGIDGISLTVGEVTPTRFCVHLIPETLERTTLGKKKLGARV
NIEIDPQTQAVVDTVERVLAARENAMNQPGTEA
Enzyme 7 Number of Residues 213
Enzyme 7 Molecular Weight 23444.8
Enzyme 7 Theoretical pI 5.88
Enzyme 7 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 7 General Function Involved in riboflavin synthase activity
Enzyme 7 Specific Function Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)- ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2- butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)- pyrimidinedione
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine [RN:R00066]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 42740 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P0AFU8 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name RISA_ECOLI Link Image
Enzyme 7 PDB ID 1I8D Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >642 bp 
ATGTTTACGGGGATTGTACAGGGCACCGCAAAACTGGTGTCGATTGACGAGAAACCAAAT
TTTCGTACGCATGTGGTGGAGTTACCCGACCACATGCTGGACGGCCTGGAAACCGGTGCT
TCCGTGGCGCATAACGGTTGCTGCCTGACCGTGACGGAAATTAACGGCAACCATGTCAGT
TTTGACCTGATGAAAGAAACGTTACGCATTACCAATCTTGGCGATTTAAAAGTGGGGGAT
TGGGTAAACGTTGAGCGTGCGGCGAAATTCAGTGATGAAATTGGCGGACACTTAATGTCA
GGTCATATTATGACCACTGCTGAAGTGGCGAAAATATTAACCTCAGAAAATAATCGCCAG
ATCTGGTTTAAAGTCCAGGATAGTCAGTTGATGAAATATATTCTGTACAAAGGATTTATT
GGCATCGACGGTATTAGCCTGACCGTCGGCGAAGTCACGCCAACGCGTTTTTGCGTCCAT
TTAATTCCGGAAACACTGGAACGCACGACTCTTGGGAAGAAAAAACTTGGCGCACGCGTC
AACATTGAAATCGATCCACAAACTCAGGCAGTGGTAGATACGGTAGAACGTGTGCTGGCG
GCACGAGAAAATGCCATGAATCAACCAGGCACAGAAGCCTGA
Enzyme 7 GenBank Gene ID X69109 Link Image
Enzyme 7 GeneCard ID ribE Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Eberhardt S, Richter G, Gimbel W, Werner T, Bacher A: Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli. Eur J Biochem. 1996 Dec 15;242(3):712-9. [PubMed Link Image]
  2. Hensel M, Shea JE, Baumler AJ, Gleeson C, Blattner F, Holden DW: Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12. J Bacteriol. 1997 Feb;179(4):1105-11. [PubMed Link Image]
  3. Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [PubMed Link Image]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  6. Truffault V, Coles M, Diercks T, Abelmann K, Eberhardt S, Luttgen H, Bacher A, Kessler H: The solution structure of the N-terminal domain of riboflavin synthase. J Mol Biol. 2001 Jun 15;309(4):949-60. [PubMed Link Image]
  7. Liao DI, Wawrzak Z, Calabrese JC, Viitanen PV, Jordan DB: Crystal structure of riboflavin synthase. Structure. 2001 May 9;9(5):399-408. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16835
Enzyme 8 Name Riboflavin synthase, alpha subunit
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name ribC
Enzyme 8 Protein Sequence >Riboflavin synthase, alpha subunit 
MFTGIVQGTAKLVSIDEKPNFRTHVVELPDHMLDGLETGASVAHNGCCLTVTEINGNHVS
FDLMKETLRITNLGDLKVGDWVNVERAAKFSDEIGGHLMSGHIMTTAEVAKILTSENNRQ
IWFKVQDSQLMKYILYKGFIGIDGISLTVGEVTPTRFCVHLIPETLERTTLGKKKLGARV
NIEIDPQTQAVVDTVERVLAARENAMNQPGTEA
Enzyme 8 Number of Residues 213
Enzyme 8 Molecular Weight 23444.8
Enzyme 8 Theoretical pI 5.88
Enzyme 8 GO Classification
Function
  • catalytic activity
  • riboflavin synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolic process
  • nitrogen compound metabolic process
  • riboflavin biosynthetic process
  • riboflavin metabolic process
Component
—
Enzyme 8 General Function Involved in riboflavin synthase activity
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 169888584 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID B1XFX2 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B1XFX2_ECODH Link Image
Enzyme 8 PDB ID 1I8D Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >642 bp 
ATGCGCAGTAAGTATATCGTCATTGAGGGGCTGGAAGGCGCAGGCAAAACTACCGCGCGT
AATGTGGTGGTTGAGACGCTCGAGCAACTGGGTATCCGCGACATGGTTTTCACTCGGGAA
CCTGGCGGTACGCAACTTGCCGAAAAGTTAAGAAGCCTGGTGCTGGATATCAAATCGGTA
GGCGATGAAGTCATTACCGATAAAGCCGAAGTTCTGATGTTTTATGCCGCGCGCGTTCAA
CTGGTAGAAACGGTCATCAAACCAGCTCTGGCTAACGGCACCTGGGTGATTGGCGATCGC
CACGATCTCTCCACTCAGGCGTATCAGGGCGGCGGACGTGGTATTGACCAACATATGCTG
GCAACACTGCGTGATGCTGTTCTCGGGGATTTTCGCCCCGACTTAACGCTCTATCTCGAT
GTTACCCCGGAAGTTGGCTTAAAACGCGCGCGTGCGCGCGGCGAGCTGGATCGTATTGAG
CAAGAATCTTTCGATTTCTTTAATCGCACCCGCGCCCGCTATCTGGAACTGGCAGCACAA
GATAAAAGCATTCATACCATTGATGCCACCCAGCCGCTGGAGGCCGTGATGGATGCAATC
CGCACTACCGTGACCCACTGGGTGAAGGAGTTGGACGCATGA
Enzyme 8 GenBank Gene ID CP000948 Link Image
Enzyme 8 GeneCard ID ribC Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus ECDH10B_1796
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available