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Human Metabolome Database Version 2.5

 

Showing metabocard for Beta-D-Fructose 2-phosphate (HMDB06800)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-08-12 14:10:56
Update Date 2009-05-05 21:01:13
Accession Number HMDB06800
Secondary Accession Numbers Not Available
Common Name Beta-D-Fructose 2-phosphate
Description beta-D-Fructose 2-phosphate is involved in the fructose eand mannose system. beta-D-Fructose 2-phosphate is produced from beta-D-Fructose 2,6-bisphosphate by the enzyme fructose-2,6-bisphosphate 6-phosphatase [EC 3.1.3.54].
Synonyms
  1. beta-D-Fructofuranose 2-phosphate
  2. beta-D-Fructose 2-phosphate
Chemical IUPAC Name Not Available
Chemical Formula C6H13O9P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Sugar Phosphates
Sub Class
  • Monosaccharide phosphates
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 260.136
Monoisotopic Molecular Weight 260.029724
Isomeric SMILES OC[C@H]1O[C@@](CO)(OP(O)(O)=O)[C@@H](O)[C@@H]1O
Canonical SMILES OCC1OC(CO)(OP(O)(O)=O)C(O)C1O
KEGG Compound ID C03267 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB06800 Link Image
Metagene Link HMDB06800 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C6H13O9P/c7-1-3-4(9)5(10)6(2-8,14-3)15-16(11,12)13/h3-5,7-10H,1-2H2,(H2,11,12,13)/t3-,4-,5+,6+/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 34.4 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.09 [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 Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
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
Fructose and Mannose Degradation SMP00064 Link Image map00051 Link Image
General References Not Available
Metabolic Enzymes
  1. Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a)
  2. 14 kDa phosphohistidine phosphatase
Enzyme 1 [top]
Enzyme 1 ID 12982
Enzyme 1 Name Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a)
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name PHPT1
Enzyme 1 Protein Sequence >Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a)
MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKV
SGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTW
ANDGY
Enzyme 1 Number of Residues 125
Enzyme 1 Molecular Weight 13833
Enzyme 1 Theoretical pI Not Available
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID B1AMX1 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name B1AMX1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence Not Available
Enzyme 1 GenBank Gene ID Not Available
Enzyme 1 GeneCard ID B1AMX1 Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References Not Available
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 21022
Enzyme 2 Name 14 kDa phosphohistidine phosphatase
Enzyme 2 Synonyms
  1. Phosphohistidine phosphatase 1
  2. Protein janus-A homolog
Enzyme 2 Gene Name PHPT1
Enzyme 2 Protein Sequence >14 kDa phosphohistidine phosphatase
MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKV
SGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTW
ANDGY
Enzyme 2 Number of Residues 125
Enzyme 2 Molecular Weight 13832.4
Enzyme 2 Theoretical pI 5.98
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Involved in phosphohistidine phosphatase activity
Enzyme 2 Specific Function Exhibits phosphohistidine phosphatase activity
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 8895093 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9NRX4 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PHP14_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >378 bp
ATGGCGGTGGCGGACCTCGCTCTCATTCCTGATGTGGACATCGACTCCGACGGCGTCTTC
AAGTATGTGCTGATCCGAGTCCACTCGGCTCCCCGCTCCGGGGCTCCGGCTGCAGAGAGC
AAGGAGATCGTGCGCGGCTACAAGTGGGCTGAGTACCATGCGGACATCTACGACAAAGTG
TCGGGCGACATGCAGAAGCAAGGCTGCGACTGTGAGTGTCTGGGCGGCGGGCGCATCTCC
CACCAGAGTCAGGACAAGAAGATTCACGTGTACGGCTATTCCATGGCCTATGGTCCTGCC
CAGCACGCCATTTCAACTGAGAAAATCAAAGCCAAGTACCCCGACTACGAGGTCACCTGG
GCTAACGACGGCTACTGA
Enzyme 2 GenBank Gene ID AF164795 Link Image
Enzyme 2 GeneCard ID PHPT1 Link Image
Enzyme 2 GenAtlas ID PHPT1 Link Image
Enzyme 2 HGNC ID HGNC:30033 Link Image
Enzyme 2 Chromosome Location 9
Enzyme 2 Locus 9q34.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Ek P, Pettersson G, Ek B, Gong F, Li JP, Zetterqvist O: Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase. Eur J Biochem. 2002 Oct;269(20):5016-23. [PubMed Link Image]
  2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  3. Lai CH, Chiu JY, Lin W: Identification of the human crooked neck gene by comparative gene identification. Biochim Biophys Acta. 2001 Feb 16;1517(3):449-54. [PubMed Link Image]
  4. 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]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [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. Ma R, Kanders E, Sundh UB, Geng M, Ek P, Zetterqvist O, Li JP: Mutational study of human phosphohistidine phosphatase: effect on enzymatic activity. Biochem Biophys Res Commun. 2005 Nov 25;337(3):887-91. Epub 2005 Sep 30. [PubMed Link Image]
  8. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  9. Busam RD, Thorsell AG, Flores A, Hammarstrom M, Persson C, Hallberg BM: First structure of a eukaryotic phosphohistidine phosphatase. J Biol Chem. 2006 Nov 10;281(45):33830-4. Epub 2006 Sep 21. [PubMed Link Image]
  10. Gong W, Li Y, Cui G, Hu J, Fang H, Jin C, Xia B: Solution structure and catalytic mechanism of human protein histidine phosphatase 1. Biochem J. 2009 Mar 1;418(2):337-44. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available