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Human Metabolome Database Version 2.5

 

Showing metabocard for N-Acetylneuraminic acid (HMDB00230)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:46
Accession Number HMDB00230
Secondary Accession Numbers HMDB00800
Common Name N-Acetylneuraminic acid
Description N-acetylneuraminic acid (NeuAc) or sialic acid is an acetyl derivative of the amino sugar neuraminic acid. It occurs in many glycoproteins, glycolipids, and polysaccharides in both mammals and bacteria. The most abundant sialic acid, NeuAc, is synthesized in vivo from N-acetylated D-mannosamine (ManNAc) or D-glucosamine (GlcNAc). NeuAc and its activated form, CMP-NeuAc, are biosynthesized in five consecutive reactions: UDP-N-acetylglucosamine (UDP-GlcNAc) N-acetylmannosamine (ManNAc) ManNAc 6-phosphate NeuAc 9-phosphate NeuAc CMP-NeuAc. CMP-NeuAc is transported into the Golgi apparatus and, with the aid of specific sialyltransferases, added onto nonreducing positions on oligosaccharide chains of glycoproteins and glycolipids. NeuAc is widely distributed throughout human tissues and found in several fluids, including serum, cerebrospinal fluid, saliva, urine, amniotic fluid, and breast milk. It is found in high levels in the brain, adrenal glands, and the heart. Serum and urine levels of the free acid are elevated in individuals suffering from renal failure. Serum and saliva Neu5Ac levels are also elevated in alcoholics. A disorder known as Salla disease or infantile NeuAc storage disease is also characterized by high serum and urine levels of this compound. The negative charge of is responsible for the slippery feel of saliva and mucins coating the body's organs. This particular sialic acid is known to act as a "decoy" for invading pathogens. NeuAc is also becoming known as an agent necessary for mediating ganglioside distribution and structures in the brain. Sialic acid (SA) is an N-acetylated derivative of neuraminic acid that is an abundant terminal monosaccharide of glycoconjugates. Normal human serum SA is largely bound to glycoproteins or glycolipids (Total sialic acid, TSA, 1.5-2.5 mmol/L), with small amounts of free SA (1-3 umol/L). Negatively charged SA units stabilize glycoprotein conformation in cell surface receptors to increase cell rigidity. This enables signal recognition and adhesion to ligands, antibodies, enzymes and microbes. SA residues are antigenic determinant residues in carbohydrate chains of glycolipids and glycoproteins, chemical messengers in tissue and body fluids, and may regulate glomeruli basement membrane permeability. Sialic acids are structurally unique nine-carbon keto sugars occupying the interface between the host and commensal or pathogenic microorganisms. An important function of host sialic acid is to regulate innate immunity. Sialic acid is the moiety most actively recycled for metabolic purposes in the salvage pathways in glycosphingolipid metabolism. Sialic acid is indispensable for the neuritogenic activities of gangliosides constituents which are unique in that a sialic acid directly binds to the glucose of the cerebroside, they are mutually connected in tandem, and some are located in the internal parts of the sugar chain. Sialylation (sialic acid linked to galactose, N-acetylgalactosamine, or linked to another sialic acid) represents one of the most frequently occurring terminations of the oligosaccharide chains of glycoproteins and glycolipids. The biosynthesis of the various linkages is mediated by the different members of the sialyltransferase family. (PMID: 11425186, 11287396, 12770781, 16624269, 12510390, 15007099)
Synonyms
  1. Sialic acid
  2. Neu5Ac
  3. 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-2-Nonulosonate
  4. 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-2-Nonulosonic acid
  5. 5-N-Acetyl-D-neuraminate
  6. 5-N-Acetyl-D-neuraminic acid
  7. 5-N-Acetylneuraminate
  8. 5-N-Acetylneuraminic acid
  9. 5-acetamido-3,5-dideoxy-D-glycero-D-galacto-Nonulosonate
  10. 5-acetamido-3,5-dideoxy-D-glycero-D-galacto-Nonulosonic acid
  11. Aceneuramate
  12. Aceneuramic acid
  13. Acetylneuraminate
  14. Acetylneuraminic acid
  15. Lactaminate
  16. Lactaminic acid
  17. N-Acetyl-D-neuraminate
  18. N-Acetyl-D-neuraminic acid
  19. N-Acetylneuramate
  20. N-Acetylneuramic acid
  21. N-Acetylneuraminate
  22. N-Acetylneuraminic acid
  23. N-Acetylsialate
  24. N-Acetylsialic acid
  25. Beta-sialic acid
  26. b-sialic acid
  27. 5-(acetylamino)-3,5-dideoxy-D-glycero-b-D-galacto-2-Nonulopyranosonate
  28. 5-(acetylamino)-3,5-dideoxy-D-glycero-b-D-galacto-2-Nonulopyranosonic acid
  29. N-Acetyl-b-D-neuraminate
  30. N-Acetyl-b-D-neuraminic acid
  31. N-Acetyl-b-neuraminate
  32. b-5-acetamido-3,5-dideoxy-D-glycero-D-galacto-Nonulopyranosonate
  33. b-5-acetamido-3,5-dideoxy-D-glycero-D-galacto-Nonulopyranosonic acid
  34. NAN
  35. NANA
  36. 5-N-Acetyl-b-D-neuraminic acid
  37. 5-N-Acetyl-beta-D-neuraminic acid
  38. N-Acetyl-neuraminic acid
  39. N-acetyl-neuraminate
  40. N-Acetyl-beta-neuraminate
  41. 5-(acetylamino)-3,5-dideoxy-delta-glycero-delta-galacto-2-Nonulosonate
  42. 5-(acetylamino)-3,5-dideoxy-delta-glycero-delta-galacto-2-Nonulosonic acid
  43. 5-N-Acetyl-delta-neuraminate
  44. 5-N-Acetyl-delta-neuraminic acid
  45. 5-acetamido-3,5-dideoxy-delta-glycero-delta-galacto-Nonulosonate
  46. 5-acetamido-3,5-dideoxy-delta-glycero-delta-galacto-Nonulosonic acid
  47. N-Acetyl-delta-neuraminate
  48. N-Acetyl-delta-neuraminic acid
  49. 5-(acetylamino)-3,5-dideoxy-delta-glycero-beta-delta-galacto-2-Nonulopyranosonate
  50. 5-(acetylamino)-3,5-dideoxy-delta-glycero-beta-delta-galacto-2-Nonulopyranosonic acid
  51. N-Acetyl-beta-delta-neuraminate
  52. N-Acetyl-beta-delta-neuraminic acid
  53. beta-5-acetamido-3,5-dideoxy-delta-glycero-delta-galacto-Nonulopyranosonate
  54. beta-5-acetamido-3,5-dideoxy-delta-glycero-delta-galacto-Nonulopyranosonic acid
  55. 5-N-Acetyl-beta-delta-neuraminic acid
Chemical IUPAC Name 5-acetylamino-2,4-dihydroxy-6-(1,2,3-trihydroxypropyl)oxane-2-carboxylic acid
Chemical Formula C11H19NO9
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Disaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • carboxylic acid
  • secondary carboxylic acid amide
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 309.270
Monoisotopic Molecular Weight 309.105988
Isomeric SMILES CC(=O)N[C@@H]1[C@@H](O)C[C@](O)(O[C@H]1[C@H](O)[C@H](O)CO)C(O)=O
Canonical SMILES CC(=O)NC1C(O)CC(O)(OC1C(O)C(O)CO)C(O)=O
KEGG Compound ID C00270 Link Image
BioCyc ID N-ACETYLNEURAMINATE Link Image
BiGG ID 34458 Link Image
Wikipedia Link N-Acetylneuraminic acid Link Image
NuGOwiki Link HMDB00230 Link Image
Metagene Link HMDB00230 Link Image
METLIN ID 3321 Link Image
PubChem Compound 439197 Link Image
PubChem Substance 830764 Link Image
ChEBI ID 17012 Link Image
CAS Registry Number 131-48-6
InChI Identifier InChI=1/C11H19NO9/c1-4(14)12-7-5(15)2-11(20,10(18)19)21-9(7)8(17)6(16)3-13/h5-9,13,15-17,20H,2-3H2,1H3,(H,12,14)(H,18,19)/t5-,6+,7+,8+,9+,11-/m0/s1
Synthesis Reference Yamamoto, Toshihiro; Teshima, Tadashi; Inami, Kaoru; Shiba, Tetsuo. Synthesis of sialic acid through aldol condensation of glucose with oxalacetic acid. Tetrahedron Letters (1992), 33(3), 325-8.
Melting Point (Experimental) 186 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 227.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.78 [Predicted by ALOGPS]; -3.7 [Predicted by PubChem via XLOGP] 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
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Medium Energy
Download File
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High Energy
Download File
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Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Membrane proteins
  • lysosome
  • nucleus
Biofluid Location
  • Blood
  • Breast Milk
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adrenal Gland —
Brain —
Myelin —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 2.0 (1.0-3.0) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Gopaul KP, Crook MA: Sialic acid: a novel marker of cardiovascular disease? Clin Biochem. 2006 Jul;39(7):667-81. Epub 2006 Apr 19. [PubMed Link Image]
Biofluid Blood
Value 0.57 +/- 1.26 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Breast Milk
Value 32.3565576 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Wiederschain GYa, Newburg DS: Glycosidase activities and sugar release in human milk. Adv Exp Med Biol. 2001;501:573-7. [PubMed Link Image]
Biofluid CSF
Value 11.9 +/- 7.1 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Urine
Value 8.6 +/- 1.58 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
General References
  1. Domschke W, Lux G, Domschke S: Furan H2-antagonist ranitidine inhibits pentagastrin-stimulated gastric secretion stronger than cimetidine. Gastroenterology. 1980 Dec;79(6):1267-71. [PubMed Link Image]
  2. Bosmann HB: Platelet adhesiveness and aggregation. II. Surface sialic acid, glycoprotein: N-acetylneuraminic acid transferase, and neuraminidase of human blood platelets. Biochim Biophys Acta. 1972 Oct 25;279(3):456-74. [PubMed Link Image]
  3. Rack J, Sonnenberg A: The influence of smoking and intravenous nicotine on gastric mucus. Hepatogastroenterology. 1983 Dec;30(6):258-60. [PubMed Link Image]
  4. Bell JD, Brown JC, Nicholson JK, Sadler PJ: Assignment of resonances for 'acute-phase' glycoproteins in high resolution proton NMR spectra of human blood plasma. FEBS Lett. 1987 May 11;215(2):311-5. [PubMed Link Image]
  5. Brusque A, Rotta L, Pettenuzzo LF, Junqueira D, Schwarzbold CV, Wyse AT, Wannmacher CM, Dutra-Filho CS, Wajner M: Chronic postnatal administration of methylmalonic acid provokes a decrease of myelin content and ganglioside N-acetylneuraminic acid concentration in cerebrum of young rats. Braz J Med Biol Res. 2001 Feb;34(2):227-31. [PubMed Link Image]
  6. Seppala R, Renlund M, Bernardini I, Tietze F, Gahl WA: Renal handling of free sialic acid in normal humans and patients with Salla disease or renal disease. Lab Invest. 1990 Aug;63(2):197-203. [PubMed Link Image]
  7. Loomis RE, Prakobphol A, Levine MJ, Reddy MS, Jones PC: Biochemical and biophysical comparison of two mucins from human submandibular-sublingual saliva. Arch Biochem Biophys. 1987 Nov 1;258(2):452-64. [PubMed Link Image]
  8. Nakata D, Munster AK, Gerardy-Schahn R, Aoki N, Matsuda T, Kitajima K: Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates. Glycobiology. 2001 Aug;11(8):685-92. [PubMed Link Image]
  9. Suzuki M, Suzuki A, Yamakawa T, Matsunaga E: Characterization of 2,7-anhydro-N-acetylneuraminic acid in human wet cerumen. J Biochem (Tokyo). 1985 Feb;97(2):509-15. [PubMed Link Image]
  10. Baumkotter J, Cantz M, Mendla K, Baumann W, Friebolin H, Gehler J, Spranger J: N-Acetylneuraminic acid storage disease. Hum Genet. 1985;71(2):155-9. [PubMed Link Image]
  11. Weiss P, Tietze F, Gahl WA, Seppala R, Ashwell G: Identification of the metabolic defect in sialuria. J Biol Chem. 1989 Oct 25;264(30):17635-6. [PubMed Link Image]
  12. McGee DJ, Rest RF: Regulation of gonococcal sialyltransferase, lipooligosaccharide, and serum resistance by glucose, pyruvate, and lactate. Infect Immun. 1996 Nov;64(11):4630-7. [PubMed Link Image]
  13. Sonnenberg A, Steinkamp U, Weise A, Berges W, Wienbeck M, Rohner HG, Peter P: Salivary secretion in reflux esophagitis. Gastroenterology. 1982 Oct;83(4):889-95. [PubMed Link Image]
  14. Riebe D, Thorn W: Influence of carbohydrate moieties of human serum transferrin on the determination of its molecular mass by polyacrylamide gradient gel electrophoresis and staining with periodic acid-Schiff reagent. Electrophoresis. 1991 Apr;12(4):287-93. [PubMed Link Image]
  15. Watzlawick H, Walsh MT, Ehrhard I, Slayter HS, Haupt H, Schwick HG, Jourdian GW, Hase S, Schmid K, Brossmer R: The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism. Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal. Biochem J. 1991 Aug 1;277 ( Pt 3):753-8. [PubMed Link Image]
  16. Gopaul KP, Crook MA: Sialic acid: a novel marker of cardiovascular disease? Clin Biochem. 2006 Jul;39(7):667-81. Epub 2006 Apr 19. [PubMed Link Image]
  17. Wikipedia Link Image
Metabolic Enzymes
  1. Sialidase-2
  2. Sialidase-4
  3. Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
  4. Sialic acid synthase
  5. N-acylneuraminate cytidylyltransferase
  6. Sialate O-acetylesterase precursor
  7. N-acylneuraminate-9-phosphatase
  8. N-acetylneuraminate lyase
  9. cDNA FLJ78026
  10. Sialidase 1 (Lysosomal sialidase) (Sialidase 1 (Lysosomal sialidase), isoform CRA_a) (NEU1 protein)
  11. cDNA FLJ31531 fis, clone NT2RI2000585, highly similar to Sialate O-acetylesterase (EC 3.1.1.53)
  12. cDNA, FLJ96858, Homo sapiens N-acetylneuraminic acid synthase (sialic acid synthase) (NANS), mRNA (N-acetylneuraminic acid synthase (Sialic acid synthase), isoform CRA_b)
  13. cDNA FLJ30910 fis, clone FEBRA2006270, highly similar to N-acylneuraminate-9-phosphatase (EC 3.1.3.29)
Enzyme 1 [top]
Enzyme 1 ID 5552
Enzyme 1 Name Sialidase-2
Enzyme 1 Synonyms
  1. Cytosolic sialidase
  2. N-acetyl-alpha- neuraminidase 2
Enzyme 1 Gene Name NEU2
Enzyme 1 Protein Sequence >Sialidase-2 
MASLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRASKKDEHAELIVLRRGDYD
APTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQVTEQQQLQTRAN
VTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLNDRARSLVVPAYA
YRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL
RARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSVISFPSPRSGPGSPAQWLLYTHPTH
SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYE
EIVFLMFTLKQAFPAEYLPQ
Enzyme 1 Number of Residues 380
Enzyme 1 Molecular Weight 42231
Enzyme 1 Theoretical pI 6.83
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Hydrolyzes sialylated compounds
Enzyme 1 Pathways
Enzyme 1 Reactions
  • Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4688894 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9Y3R4 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name NEUR2_HUMAN Link Image
Enzyme 1 PDB ID 1VCU Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1143 bp 
ATGGCGTCCCTTCCTGTCCTGCAGAAGGAGAGCGTGTTCCAGTCGGGAGCCCATGCCTAC
AGAATCCCTGCCCTGCTCTACCTGCCTGGGCAGCAGTCCCTGCTGGCCTTCGCGGAACAG
CGGGCAAGCAAGAAGGATGAGCACGCAGAGCTGATTGTCCTGCGCAGAGGAGACTACGAC
GCACCCACCCACCAGGTTCAGTGGCAAGCTCAGGAGGTGGTGGCCCAGGCCCGGCTGGAT
GGCCACCGGTCCATGAACCCATGCCCCTTGTATGACGCGCAGACGGGGACCCTCTTCCTC
TTCTTCATTGCCATCCCTGGGCAAGTCACGGAGCAACAGCAGCTGCAGACCAGGGCCAAT
GTGACGCGGCTGTGCCAAGTCACCAGCACTGACCACGGGAGGACCTGGAGCTCCCCCAGA
GACCTCACTGATGCGGCCATCGGCCCAGCCTACCGGGAGTGGTCCACCTTTGCAGTGGGC
CCGGGGCATTGTTTGCAGCTTAACGACAGGGCCCGGAGCCTGGTGGTGCCCGCCTACGCC
TACCGGAAACTTCACCCCATCCAAAGGCCGATCCCCTCTGCCTTCTGCTTCCTCAGCCAT
GACCATGGGCGCACGTGGGCGCGAGGGCACTTTGTGGCCCAGGACACCCTGGAGTGCCAG
GTGGCCGAAGTCGAGACTGGGGAGCAGAGGGTGGTGACCCTCAACGCGAGAAGCCACCTC
CGAGCCAGGGTCCAGGCCCAGAGCACCAATGACGGGCTTGATTTCCAGGAGTCTCAGCTG
GTGAAGAAGCTGGTGGAGCCGCCGCCCCAGGGCTGCCAGGGGAGCGTCATCAGCTTCCCC
AGCCCCCGCTCGGGGCCTGGCTCCCCAGCCCAGTGGCTGCTCTACACTCACCCCACACAC
TCCTGGCAGAGGGCCGACCTGGGTGCCTACCTCAACCCGCGACCTCCAGCCCCTGAGGCC
TGGTCAGAGCCGGTACTGCTGGCCAAGGGCAGCTGTGCCTACTCAGACCTCCAGAGCATG
GGCACCGGCCCTGATGGGTCCCCCTTGTTTGGGTGTCTGTACGAAGCCAATGATTACGAG
GAGATTGTCTTTCTCATGTTCACCCTGAAGCAAGCCTTCCCAGCTGAGTACCTGCCTCAG
TGA
Enzyme 1 GenBank Gene ID Y16535 Link Image
Enzyme 1 GeneCard ID NEU2 Link Image
Enzyme 1 GenAtlas ID NEU2 Link Image
Enzyme 1 HGNC ID HGNC:7759 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q37
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Monti E, Preti A, Rossi E, Ballabio A, Borsani G: Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases. Genomics. 1999 Apr 1;57(1):137-43. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5558
Enzyme 2 Name Sialidase-4
Enzyme 2 Synonyms
  1. N-acetyl-alpha-neuraminidase 4
Enzyme 2 Gene Name NEU4
Enzyme 2 Protein Sequence >Sialidase-4 
MGVPRTPSRTVLFERERTGLTYRVPSLLPVPPGPTLLAFVEQRLSPDDSHAHRLVLRRGT
LAGGSVRWGALHVLGTAALAEHRSMNPCPVHDAGTGTVFLFFIAVLGHTPEAVQIATGRN
AARLCCVASRDAGLSWGSARDLTEEAIGGAVQDWATFAVGPGHGVQLPSGRLLVPAYTYR
VDRRECFGKICRTSPHSFAFYSDDHGRTWRCGGLVPNLRSGECQLAAVDGGQAGSFLYCN
ARSPLGSRVQALSTDEGTSFLPAERVASLPETAWGCQGSIVGFPAPAPNRPRDDSWSVGP
GSPLQPPLLGPGVHEPPEEAAVDPRGGQVPGGPFSRLQPRGDGPRQPGPRPGVSGDVGSW
TLALPMPFAAPPQSPTWLLYSHPVGRRARLHMGIRLSQSPLDPRSWTEPWVIYEGPSGYS
DLASIGPAPEGGLVFACLYESGARTSYDEISFCTFSLREVLENVPASPKPPNLGDKPRGC
CWPS
Enzyme 2 Number of Residues 484
Enzyme 2 Molecular Weight 51573
Enzyme 2 Theoretical pI 7.84
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Has sialidase activity towards synthetic substrates, such as 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid (4-MU-NANA or 4MU-NeuAc)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 18073364 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8WWR8 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name NEUR4_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1455 bp 
ATGGGGGTCCCTCGTACCCCTTCACGGACAGTGCTCTTCGAGCGGGAGAGGACGGGCCTG
ACCTACCGCGTGCCCTCGCTGCTCCCCGTGCCCCCCGGGCCCACCCTGCTGGCCTTTGTG
GAGCAGCGGCTCAGCCCTGACGACTCCCACGCCCACCGCCTGGTGCTGAGGAGGGGCACG
CTGGCCGGGGGCTCCGTGCGGTGGGGTGCCCTGCACGTGCTGGGGACAGCAGCCCTGGCG
GAGCACCGGTCCATGAACCCCTGCCCTGTGCACGATGCTGGCACGGGCACCGTCTTCCTC
TTCTTCATCGCGGTGCTGGGCCACACGCCTGAGGCCGTGCAGATCGCCACGGGAAGGAAC
GCCGCGCGCCTCTGCTGTGTGGCCAGCCGTGACGCCGGCCTCTCGTGGGGCAGCGCCCGG
GACCTCACCGAGGAGGCCATCGGTGGTGCCGTGCAGGACTGGGCCACATTCGCTGTGGGT
CCCGGCCACGGCGTGCAGCTGCCCTCAGGCCGCCTGCTGGTACCCGCCTACACCTACCGC
GTGGACCGCCTAGAGTGTTTTGGCAAGATCTGCCGGACCAGCCCTCACTCCTTCGCCTTC
TACAGCGATGACCACGGCCGCACCTGGCGCTGTGGAGGCCTCGTGCCCAACCTGCGCTCA
GGCGAGTGCCAGCTGGCGGCGGTGGACGGTGGGCAGGCCGGCAGCTTCCTCTACTGCAAT
GCCCGGAGCCCACTGGGCAGCCGTGTGCAGGCGCTCAGCACTGACGAGGGCACCTCCTTC
CTGCCCGCAGAGCGCGTGGCTTCCCTGCCCGAGACTGCCTGGGGCTGCCAGGGCAGCATC
GTGGGCTTCCCAGCCCCCGCCCCCAACAGGCCACGGGATGACAGTTGGTCAGTGGGCCCC
AGGAGTCCCCTCCAGCCTCCACTCCTCGGTCCTGGAGTCCACGAACCCCCAGAGGAGGCT
GCTGTAGACCCCCGTGGAGGCCAGGTGCCTGGTGGGCCCTTCAGCCGTCTGCAGCCTCGG
GGGGATGGCCCCAGGCAGCCTGGCCCCAGGCCTGGGGTCAGTGGGGATGTGGGGTCCTGG
ACCCTGGCACTCCCCATGCCCTTTGCTGCCCCGCCCCAGAGCCCCACGTGGCTGCTGTAC
TCCCACCCAGTGGGGCGCAGGGCTCGGCTACACATGGGTATCCGCCTGAGCCAGTCCCCG
CTGGACCCGCGCAGCTGGACAGAGCCCTGGGTGATCTACGAGGGCCCCAGCGGCTACTCC
GACCTGGCGTCCATCGGGCCGGCTCCTGAGGGGGGCCTGGTTTTTGCCTGCCTGTACGAG
AGCGGGGCCAGGACCTCCTATGATGAGATTTCCTTTTGTACATTCTCCCTGCGTGAGGTC
CTGGAGAACGTGCCCGCCAGCCCCAAGCCGCCCAACCTTGGGGACAAGCCTCGGGGGTGC
TGCTGGCCCTCCTGA
Enzyme 2 GenBank Gene ID AJ277883 Link Image
Enzyme 2 GeneCard ID NEU4 Link Image
Enzyme 2 GenAtlas ID NEU4 Link Image
Enzyme 2 HGNC ID HGNC:21328 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2q37.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5568
Enzyme 3 Name Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Enzyme 3 Synonyms
  1. UDP-GlcNAc-2-epimerase/ManAc kinase[Includes: UDP-N- acetylglucosamine 2-epimerase
  2. Uridine diphosphate-N- acetylglucosamine-2-epimerase
  3. UDP-GlcNAc-2-epimerase
  4. N- acetylmannosamine kinase
  5. ManAc kinase]
Enzyme 3 Gene Name GNE
Enzyme 3 Protein Sequence >Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase 
MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRM
IEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALA
TSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILL
AGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDAL
ISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGN
SSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKI
YGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLR
VAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNP
REGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTL
ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREA
KKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTM
NPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRR
IY
Enzyme 3 Number of Residues 722
Enzyme 3 Molecular Weight 79276
Enzyme 3 Theoretical pI 6.79
Enzyme 3 GO Classification
Function
  • UDP-N-acetylglucosamine 2-epimerase activity
  • catalytic activity
  • isomerase activity
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on carbohydrates and derivatives
Process
  • N-acetylglucosamine metabolism
  • UDP-N-acetylglucosamine metabolism
  • amine metabolism
  • amino sugar metabolism
  • carbohydrate biosynthesis
  • glucosamine metabolism
  • lipopolysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • nitrogen compound metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
—
Enzyme 3 General Function Cell wall/membrane/envelope biogenesis
Enzyme 3 Specific Function Regulates and initiates biosynthesis of N- acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells
Enzyme 3 Pathways
Enzyme 3 Reactions
  • UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 4775362 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9Y223 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GLCNE_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2169 bp 
ATGGAGAAGAATGGAAATAACCGAAAGCTGCGGGTTTGTGTTGCTACTTGTAACCGTGCA
GATTATTCTAAACTTGCCCCGATCATGTTTGGCATTAAAACCGAACCTGAGTTCTTTGAA
CTTGATGTTGTGGTACTTGGCTCTCACCTGATAGATGACTATGGAAATACATATCGAATG
ATTGAACAAGATGACTTTGACATTAACACCAGGCTACACACAATTGTGAGGGGAGAAGAT
GAGGCAGCCATGGTGGAGTCAGTAGGCCTGGCCCTAGTGAAGCTGCCAGATGTCCTTAAT
CGCCTGAAGCCTGATATCATGATTGTTCATGGAGACAGGTTTGATGCCCTGGCTCTGGCC
ACATCTGCTGCCTTGATGAACATCCGAATCCTTCACATTGAAGGTGGGGAAGTCAGTGGG
ACCATTGATGACTCTATCAGACATGCCATAACAAAACTGGCTCATTATCATGTGTGCTGC
ACCCGCAGTGCAGAGCAGCACCTGATATCCATGTGTGAGGACCATGATCGCATCCTTTTG
GCAGGCTGCCCTTCCTATGACAAACTTCTCTCAGCCAAGAACAAAGACTACATGAGCATC
ATTCGCATGTGGCTAGGTGATGATGTAAAATCTAAAGATTACATTGTTGCACTACAGCAC
CCTGTGACCACTGACATTAAGCATTCCATAAAAATGTTTGAATTAACATTGGATGCACTT
ATCTCATTTAACAAGCGGACCCTAGTCCTGTTTCCAAATATTGACGCAGGGAGCAAAGAG
ATGGTTCGAGTGATGCGGAAGAAGGGCATTGAGCATCATCCCAACTTTCGTGCAGTTAAA
CACGTCCCATTTGACCAGTTTATACAGTTGGTTGCCCATGCTGGCTGTATGATTGGGAAC
AGCAGCTGTGGGGTTCGAGAAGTTGGAGCTTTTGGAACACCTGTGATCAACCTGGGAACA
CGTCAGATTGGAAGAGAAACAGGGGAGAATGTTCTTCATGTCCGGGATGCTGACACCCAA
GACAAAATATTGCAAGCACTGCACCTTCAGTTTGGTAAACAGTACCCTTGTTCAAAGATA
TATGGGGATGGAAATGCTGTTCCAAGGATTTTGAAGTTTCTCAAATCTATCGATCTTCAA
GAGCCACTGCAAAAGAAATTCTGCTTTCCTCCTGTGAAGGAGAATATCTCTCAAGATATT
GACCATATTCTTGAAACTCTAAGTGCCTTGGCCGTTGATCTTGGCGGGACGAACCTCCGA
GTTGCAATAGTCAGCATGAAGGGTGAAATAGTTAAGAAGTATACTCAGTTCAATCCTAAA
ACCTATGAAGAGAGGATTAATTTAATCCTACAGATGTGTGTGGAAGCTGCAGCAGAAGCT
GTAAAACTGAACTGCAGAATTTTGGGAGTAGGCATTTCCACAGGTGGCCGTGTAAATCCT
CGGGAAGGAATTGTGCTGCATTCAACCAAACTGATCCAAGAGTGGAACTCTGTGGACCTT
AGGACCCCCCTTTCTGACACTTTGCATCTCCCTGTGTGGGTAGACAATGATGGCAACTGT
GCTGCCCTGGCGGAAAGGAAATTTGGCCAAGGAAAGGGACTGGAAAACTTTGTTACACTT
ATCACAGGCACAGGAATCGGTGGTGGAATTATCCATCAGCATGAATTGATCCACGGAAGC
TCCTTCTGTGCTGCAGAACTGGGCCACCTTGTTGTGTCTCTGGATGGGCCTGATTGTTCC
TGTGGAAGCCATGGGTGCATTGAAGCATACGCCTCTGGAATGGCCTTGCAGAGGGAGGCA
AAAAAGCTCCATGATGAGGACCTGCTCTTGGTGGAAGGGATGTCAGTGCCAAAAGATGAG
GCTGTGGGTGCGCTCCATCTCATCCAAGCTGCGAAACTTGGCAATGCGAAGGCCCAGAGC
ATCCTAAGAACAGCTGGAACAGCTTTGGGTCTTGGGGTTGTGAACATCCTCCATACCATG
AATCCCTCCCTTGTGATCCTCTCCGGAGTCCTGGCCAGTCACTATATCCACATTGTCAAA
GACGTCATTCGCCAGCAGGCCTTGTCCTCCGTGCAGGACGTGGATGTGGTGGTTTCGGAT
TTGGTTGACCCCGCCCTGCTGGGTGCTGCCAGCATGGTTCTGGACTACACAACACGCAGG
ATCTACTAG
Enzyme 3 GenBank Gene ID AJ238764 Link Image
Enzyme 3 GeneCard ID GNE Link Image
Enzyme 3 GenAtlas ID GNE Link Image
Enzyme 3 HGNC ID HGNC:23657 Link Image
Enzyme 3 Chromosome Location 9
Enzyme 3 Locus 9p13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Seppala R, Lehto VP, Gahl WA: Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme. Am J Hum Genet. 1999 Jun;64(6):1563-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5569
Enzyme 4 Name Sialic acid synthase
Enzyme 4 Synonyms
  1. N-acetylneuraminate synthase
  2. N- acetylneuraminic acid synthase
  3. N-acetylneuraminate-9-phosphate synthase
  4. N-acetylneuraminic acid phosphate synthase
Enzyme 4 Gene Name NANS
Enzyme 4 Protein Sequence >Sialic acid synthase 
MPLELELCPGRWVGGQHPCFIIAEIGQNHQGDLDVAKRMIRMAKECGADCAKFQKSELEF
KFNRKALERPYTSKHSWGKTYGEHKRHLEFSHDQYRELQRYAEEVGIFFTASGMDEMAVE
FLHELNVPFFKVGSGDTNNFPYLEKTAKKGRPMVISSGMQSMDTMKQVYQIVKPLNPNFC
FLQCTSAYPLQPEDVNLRVISEYQKLFPDIPIGYSGHETGIAISVAAVALGAKVLERHIT
LDKTWKGSDHSASLEPGELAELVRSVRLVERALGSPTKQLLPCEMACNEKLGKSVVAKVK
IPEGTILTMDMLTVKVGEPKGYPPEDIFNLVGKKVLVTVEEDDTIMEELVDNHGKKIKS
Enzyme 4 Number of Residues 359
Enzyme 4 Molecular Weight 40308
Enzyme 4 Theoretical pI 6.73
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Cell wall/membrane/envelope biogenesis
Enzyme 4 Specific Function Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3- deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N- acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively
Enzyme 4 Pathways
Enzyme 4 Reactions
  • phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O = N-acylneuraminate 9-phosphate + phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 8453156 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NR45 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SIAS_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1080 bp 
ATGCCGCTGGAGCTGGAGCTGTGTCCCGGGCGCTGGGTGGGCGGGCAACACCCGTGCTTC
ATCATTGCCGAGATCGGCCAGAACCACCAGGGCGACCTGGACGTAGCCAAGCGCATGATC
CGCATGGCCAAGGAGTGTGGGGCTGATTGTGCCAAGTTCCAGAAGAGTGAGCTAGAATTC
AAGTTTAATCGGAAAGCCTTGGAGAGGCCATACACCTCGAAGCATTCCTGGGGGAAGACG
TACGGGGAGCACAAACGACATCTGGAGTTCAGCCATGACCAGTACAGGGAGCTGCAGAGG
TACGCCGAGGAGGTTGGGATCTTCTTCACTGCCTCTGGCATGGATGAGATGGCAGTTGAA
TTCCTGCATGAACTGAATGTTCCATTTTTCAAAGTTGGATCTGGAGACACTAATAATTTT
CCTTATCTGGAAAAGACAGCCAAAAAAGGTCGCCCAATGGTGATCTCCAGTGGGATGCAG
TCAATGGACACCATGAAGCAAGTTTATCAGATCGTGAAGCCCCTCAACCCCAACTTCTGC
TTCTTGCAGTGTACCAGCGCATACCCGCTCCAGCCTGAGGACGTCAACCTGCGGGTCATC
TCGGAATATCAGAAGCTCTTTCCTGACATTCCCATAGGGTATTCTGGGCATGAAACAGGC
ATAGCGATATCTGTGGCCGCAGTGGCTCTGGGGGCCAAGGTGTTGGAACGTCACATAACT
TTGGACAAGACCTGGAAGGGGAGTGACCACTCGGCCTCGCTGGAGCCTGGAGAACTGGCC
GAGCTGGTGCGGTCAGTGCGTCTTGTGGAGCGTGCCCTGGGCTCCCCAACCAAGCAGCTG
CTGCCCTGTGAGATGGCCTGCAATGAGAAGCTGGGCAAGTCTGTGGTGGCCAAAGTGAAA
ATTCCGGAAGGCACCATTCTAACAATGGACATGCTCACCGTGAAGGTGGGTGAGCCCAAA
GCCTATCCTCCTGAAGACATCTTTAATCTAGTGGGCAAGAAGGTCCTGGTCACTGTTGAA
GAGGATGACACCATCATGGAAGAATTGGTAGATAATCATGGCAAAAAAATCAAGTCTTAA
Enzyme 4 GenBank Gene ID AF257466 Link Image
Enzyme 4 GeneCard ID NANS Link Image
Enzyme 4 GenAtlas ID NANS Link Image
Enzyme 4 HGNC ID HGNC:19237 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Lawrence SM, Huddleston KA, Pitts LR, Nguyen N, Lee YC, Vann WF, Coleman TA, Betenbaugh MJ: Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero- D-galacto-nononic acid biosynthetic ability. J Biol Chem. 2000 Jun 9;275(23):17869-77. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5636
Enzyme 5 Name N-acylneuraminate cytidylyltransferase
Enzyme 5 Synonyms
  1. CMP-N- acetylneuraminic acid synthetase
  2. CMP-NeuNAc synthetase
Enzyme 5 Gene Name CMAS
Enzyme 5 Protein Sequence >N-acylneuraminate cytidylyltransferase 
MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPL
KNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSS
TSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRW
SEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEM
RAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEI
ISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKE
MGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEH
ICLLMEKVNNSCQK
Enzyme 5 Number of Residues 434
Enzyme 5 Molecular Weight 48380
Enzyme 5 Theoretical pI 8.02
Enzyme 5 GO Classification
Function
—
Process
  • carbohydrate biosynthesis
  • lipopolysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 22085790 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q8NFW8 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NEUA_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1305 bp 
ATGGACTCGGTGGAGAAGGGGGCCGCCACCTCCGTCTCCAACCCGCGGGGGCGACCGTCC
CGGGGCCGGCCGCCGAAGCTGCAGCGCAACTCTCGCGGCGGCCAGGGCCGAGGTGTGGAG
AAGCCCCCGCACCTGGCAGCCCTAATTCTGGCCCGGGGAGGCAGCAAAGGCATCCCCCTG
AAGAACATTAAGCACCTGGCGGGGGTCCCGCTCATTGGCTGGGTCCTGCGTGCGGCCCTG
GATTCAGGGGCCTTCCAGAGTGTATGGGTTTCGACAGACCATGATGAAATTGAGAATGTG
GCCAAACAATTTGGTGCACAAGTTCATCGAAGAAGTTCTGAAGTTTCAAAAGACAGCTCT
ACCTCACTAGATGCCATCATAGAATTTCTTAATTATYATAATGAGGKTGACATTGTAGGA
AATATTCAAGCTACTTCTYCATGTTTACATCCTACTGATCTTCAAAAAGTTGCAGAAATG
ATTCGAGAAGAAGGATATGATTCTGKTTTCTCTGTTGTGAGACGCCATCAGTTTCGATGG
AGTGAAATTCAGAAAGGAGTTCGTGAAGTGACCGAACCTCTGAATTTAAATCCAGCTAAA
CGGCCTCGTCGACAAGACTGGGATGGAGAATTATATGAAAATGGCTCATTTTATTTTGCT
AAAAGACATTTGATAGAGATGGGTTACTTGCAGGGTGGAAAAATGGCATACTACGAAATG
CGAGCTGAACATAGTGTGGATATAGATGTGGATATTGATTGGCCTATTGCAGAGCAAAGA
GTATTAAGATATGGCTATTTTGGCAAAGAGAAGCTTAAGGAAATAAAACTTTTGGTTTGC
AATATTGATGGATGTCTCACCAATGGCCACATTTATGTATCAGGAGACCAAAAAGAAATA
ATATCTTATGATGTAAAAGATGCTATTGGGATAAGTTTATTAAAGAAAAGTGGTATTGAG
GTGAGGCTAATCTCAGAAAGGGCCTGTTCAAAGCAGACGCTGTCTTCTTTAAAACTGGAT
TGCAAAATGGAAGTCAGTGTATCAGACAAGCTAGCAGTTGTAGATGAATGGAGAAAAGAA
ATGGGCCTGTGCTGGAAAGAAGTGGCATATCTTGGAAATGAAGTGTCTGATGAAGAGTGC
TTGAAGAGAGTGGGCCTAAGTGGCGCTCCTGCTGATGCCTGTTCCTACGCCCAGAAGGCT
GTTGGATACATTTGCAAATGTAATGGTGGCCGTGGTGCCATCCGAGAATTTGCAGAGCAC
ATTTGCCTACTAATGGAAAAAGTTAATAATTCATGCCAAAAATAG
Enzyme 5 GenBank Gene ID AF397212 Link Image
Enzyme 5 GeneCard ID CMAS Link Image
Enzyme 5 GenAtlas ID CMAS Link Image
Enzyme 5 HGNC ID HGNC:18290 Link Image
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
Enzyme 6 [top]
Enzyme 6 ID 5786
Enzyme 6 Name Sialate O-acetylesterase precursor
Enzyme 6 Synonyms
  1. Sialic acid-specific 9-O-acetylesterase
  2. H-Lse
Enzyme 6 Gene Name SIAE
Enzyme 6 Protein Sequence >Sialate O-acetylesterase precursor 
MVAPGLVLGLVLPLILWADRSAGIGFRFASYINNDMVLQKEPAGAVIWGFGTPGATVTVT
LRQGQETIMKKVTSVKAHSDTWMVVLDPMKPGGPFEVMAQQTLEKINFTLRVHDVLFGDV
WLCSGQSNMQMTVLQIFNATRELSNTAAYQSVRILSVSPIQAEQELEDLVAVDLQWSKPT
SENLGHGYFKYMSAVCWLFGRHLYDTLQYPIGLIASSWGGTPIEAWSSGRSLKACGVPKQ
GSIPYDSVTGPSKHSVLWNAMIHPLCNMTLKGVVWYQGESNINYNTDLYNCTFPALIEDW
RETFHRGSQGQTERFFPFGLVQLSSDLSKKSSDDGFPQIRWHQTADFGYVPNPKMPNTFM
AVAMDLCDRDSPFGSIHPRDKQTVAYRLHLGARALAYGEKNLTFEGPLPEKIELLAHKGL
LNLTYYQQIQVQKKDNKIFEISCCSDHRCKWLPASMNTVSTQSLTLAIDSCHGTVVALRY
AWTTWPCEYKQCPLYHPSSALPAPPFIAFITDQGPGHQSNVAK
Enzyme 6 Number of Residues 523
Enzyme 6 Molecular Weight 58315
Enzyme 6 Theoretical pI 7.35
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-23
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 10186503 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9HAT2 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name SIAE_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1572 bp 
ATGGTCGCGCCGGGGCTTGTACTCGGGCTGGTGCTGCCATTAATCCTGTGGGCCGACAGA
AGTGCAGGTATTGGTTTTCGCTTTGCTTCATACATCAATAATGATATGGTGCTGCAGAAG
GAGCCTGCTGGGGCAGTGATATGGGGCTTCGGTACACCTGGAGCCACAGTGACCGTGACC
CTGCGCCAAGGTCAGGAAACCATCATGAAGAAAGTGACCAGTGTGAAAGCTCACTCTGAT
ACGTGGATGGTGGTACTGGATCCTATGAAGCCTGGAGGACCTTTCGAAGTGATGGCACAA
CAGACTTTGGAGAAAATAAACTTCACCCTGAGAGTTCATGACGTCCTGTTTGGAGATGTC
TGGCTCTGTAGTGGGCAGAGTAACATGCAGATGACTGTGTTACAGATATTTAATGCTACA
AGGGAGTTGTCTAACACTGCGGCATATCAGTCTGTCCGCATCCTCTCTGTCTCTCCCATT
CAAGCAGAGCAGGAGCTGGAGGACCTTGTTGCGGTTGACTTGCAGTGGTCTAAGCCCACC
TCAGAAAACTTAGGCCATGGATATTTCAAGTACATGTCAGCAGTGTGCTGGCTCTTTGGA
CGTCACCTTTATGACACTCTGCAGTATCCCATCGGGCTGATCGCCTCCAGCTGGGGCGGG
ACACCCATTGAAGCCTGGTCATCTGGACGGTCACTGAAAGCCTGTGGGGTCCCTAAACAA
GGGTCCATTCCATACGATTCTGTAACTGGTCCCAGTAAGCACTCTGTTCTCTGGAATGCC
ATGATCCATCCACTGTGCAATATGACTCTGAAAGGGGTAGTATGGTACCAGGGGGAGTCC
AATATAAATTATAACACGGATCTGTACAATTGCACATTCCCTGCACTCATCGAAGACTGG
CGTGAAACCTTCCACCGTGGTTCCCAGGGGCAGACGGAGCGTTTCTTCCCATTTGGACTT
GTCCAGTTATCTTCAGATTTGTCTAAGAAGAGCTCAGACGATGGATTTCCCCAGATCCGT
TGGCATCAAACAGCAGACTTCGGCTATGTCCCCAACCCAAAGATGCCCAATACTTTCATG
GCTGTAGCTATGGATCTCTGTGATAGAGACTCGCCTTTTGGCAGCATCCACCCTCGAGAT
AAACAGACTGTGGCTTATCGGCTGCATTTGGGGGCCCGTGCTCTGGCTTATGGTGAGAAG
AATTTGACCTTTGAAGGACCACTGCCTGAGAAGATAGAACTCTTGGCTCACAAGGGGCTG
CTCAATCTCACATATTACCAGCAAATCCAGGTGCAGAAAAAGGACAACAAGATATTTGAG
ATCTCCTGTTGCAGTGACCATCGATGCAAGTGGCTTCCAGCTTCTATGAACACCGTCTCC
ACCCAGTCCCTGACCCTGGCGATCGATTCTTGTCATGGCACTGTGGTTGCTCTCCGCTAT
GCTTGGACCACGTGGCCTTGTGAATATAAGCAGTGTCCCCTATACCACCCCAGTAGTGCC
CTGCCAGCCCCTCCCTTCATTGCTTTCATTACAGACCAGGGTCCTGGACATCAGAGCAAT
GTTGCTAAATGA
Enzyme 6 GenBank Gene ID AF303378 Link Image
Enzyme 6 GeneCard ID SIAE Link Image
Enzyme 6 GenAtlas ID SIAE Link Image
Enzyme 6 HGNC ID HGNC:18187 Link Image
Enzyme 6 Chromosome Location 11
Enzyme 6 Locus 11q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 12983
Enzyme 7 Name N-acylneuraminate-9-phosphatase
Enzyme 7 Synonyms
  1. Neu5Ac-9-Pase
  2. Haloacid dehalogenase-like hydrolase domain-containing protein 4
Enzyme 7 Gene Name NANP
Enzyme 7 Protein Sequence >N-acylneuraminate-9-phosphatase 
MGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKEC
FHPYNTCITDLRTSHWEEAIQETKGGAANRKLAEECYFLWKSTRLQHMTLAEDVKAMLTE
LRKEVRLLLLTNGDRQTQREKIEACACQSYFDAVVVGGEQREEKPAPSIFYYCCNLLGVQ
PGDCVMVGDTLETDIQGGLNAGLKATVWINKNGIVPLKSSPVPHYMVSSVLELPALLQSI
DCKVSMST
Enzyme 7 Number of Residues 248
Enzyme 7 Molecular Weight 27813
Enzyme 7 Theoretical pI 6.35
Enzyme 7 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoglycolate phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function N-acylneuraminate 9-phosphate + H(2)O = N- acylneuraminate + phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate [RN:R02597] ALL_REAC R02597 > R01805
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID Q8TBE9 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NANP_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AL031673 Link Image
Enzyme 7 GeneCard ID Q8TBE9 Link Image
Enzyme 7 GenAtlas ID NANP Link Image
Enzyme 7 HGNC ID HGNC:16140 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 12984
Enzyme 8 Name N-acetylneuraminate lyase
Enzyme 8 Synonyms
  1. NALase
  2. N-acetylneuraminic acid aldolase
  3. N-acetylneuraminate pyruvate-lyase
  4. Sialic acid lyase
  5. Sialate lyase
  6. Sialate-pyruvate lyase
  7. Sialic acid aldolase
Enzyme 8 Gene Name NPL
Enzyme 8 Protein Sequence >N-acetylneuraminate lyase 
MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSV
SERRQVAEEWVTKGKDKLDQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWT
KDILINFLKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGILDKIPTFQGLKFSDTDLL
DFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFS
LALNYQFCIQRFINFVVKLGFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKL
KSLDFLSFTDLKDGNLEAGS
Enzyme 8 Number of Residues 320
Enzyme 8 Molecular Weight 35163
Enzyme 8 Theoretical pI 5.22
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface
Enzyme 8 Pathways
Enzyme 8 Reactions
  • N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate [RN:R01811] ALL_REAC R01811
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 13430285 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9BXD5 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NPL_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AF338436 Link Image
Enzyme 8 GeneCard ID Q9BXD5 Link Image
Enzyme 8 GenAtlas ID NPL Link Image
Enzyme 8 HGNC ID HGNC:16781 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Sood R, Bonner TI, Makalowska I, Stephan DA, Robbins CM, Connors TD, Morgenbesser SD, Su K, Faruque MU, Pinkett H, Graham C, Baxevanis AD, Klinger KW, Landes GM, Trent JM, Carpten JD: Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus. Genomics. 2001 Apr 15;73(2):211-22. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 13110
Enzyme 9 Name cDNA FLJ78026
Enzyme 9 Synonyms
  1. Sialidase 3
  2. Membrane sialidase, isoform CRA_a
Enzyme 9 Gene Name NEU3
Enzyme 9 Protein Sequence >cDNA FLJ78026 
MRPADLPPRPMEESPASSSAPTETEEPGSSAEVMEEVTTCSFNSPLFRQEDDRGITYRIP
ALLYIPPTHTFLAFAEKRSTRRDEDALHLVLRRGLRIGQLVQWGPLKPLMEATLPGHRTM
NPCPVWEQKSGCVFLFFICVRGHVTERQQIVSGRNAARLCFIYSQDAGCSWSEVRDLTEE
VIGSELKHWATFAVGPGHGIQLQSGRLVIPAYTYYIPSWFFCFQLPCKTRPHSLMIYSDD
LGVTWHHGRLIRPMVTVECEVAEVTGRAGHPVLYCSARTPNRCRAEALSTDHGEGFQRLA
LSRQLCEPPHGCQGSVVSFRPLEIPHRCQDSSSKDAPTIQQSSPGSSLRLEEEAGTPSES
WLLYSHPTSRKQRVDLGIYLNQTPLEAACWSRPWILHCGPCGYSDLAALEEEGLFGCLFE
CGTKQECEQIAFRLFTHREILSHLQGDCTSPGRNPSQFKSN
Enzyme 9 Number of Residues 461
Enzyme 9 Molecular Weight 51675
Enzyme 9 Theoretical pI 6.64
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 158261907 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID A8K327 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name A8K327_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK290442 Link Image
Enzyme 9 GeneCard ID A8K327 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15246
Enzyme 10 Name Sialidase 1 (Lysosomal sialidase) (Sialidase 1 (Lysosomal sialidase), isoform CRA_a) (NEU1 protein)
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name NEU1
Enzyme 10 Protein Sequence >Sialidase 1 (Lysosomal sialidase) (Sialidase 1 (Lysosomal sialidase), isoform CRA_a) (NEU1 protein) 
MTGERPSTALPDRRWGPRILGFWGGCRVWVFAAIFLLLSLAASWSKAENDFGLVQPLVTM
EQLLWVSGRQIGSVDTFRIPLITATPRGTLLAFAEARKMSSSDEGAKFIALRRSMDQGST
WSPTAFIVNDGDVPDGLNLGAVVSDVETGVVFLFYSLCAHKAGCQVASTMLVWSKDDGVS
WSTPRNLSLDIGTEVFAPGPGSGIQKQREPRKGRLIVCGHGTLERDGVFCLLSDDHGASW
RYGSGVSGIPYGQPKQENDFNPDECQPYELPDGSVVINARNQNNYHCHCRIVLRSYDACD
TLRPRDVTFDPELVDPVVAAGAVVTSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWRKET
VQLWPGPSGYSSLATLEGSMDGEEQAPQLYVLYEKGRNHYTESISVAKISVYGTL
Enzyme 10 Number of Residues 415
Enzyme 10 Molecular Weight 45468
Enzyme 10 Theoretical pI 5.68
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 49456787 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q5JQI0 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q5JQI0_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1245 bp 
ATGACTGGGGAGCGACCCAGCACGGCGCTCCCGGACAGACGCTGGGGGCCGCGGATTCTG
GGCTTCTGGGGAGGCTGTAGGGTTTGGGTGTTTGCCGCGATCTTCCTGCTGCTGTCTCTG
GCAGCCTCCTGGTCCAAGGCTGAGAACGACTTCGGTCTGGTGCAGCCGCTGGTGACCATG
GAGCAACTGCTGTGGGTGAGCGGGAGACAGATCGGCTCAGTGGACACCTTCCGCATCCCG
CTCATCACAGCCACTCCGCGGGGCACTCTTCTCGCCTTTGCTGAGGCGAGGAAAATGTCC
TCATCCGATGAGGGGGCCAAGTTCATCGCCCTGCGGAGGTCCATGGACCAGGGCAGCACA
TGGTCTCCTACAGCGTTCATTGTCAATGATGGGGATGTCCCCGATGGGCTGAACCTTGGG
GCAGTAGTGAGCGATGTTGAGACAGGAGTAGTATTTCTTTTCTACTCCCTTTGTGCTCAC
AAGGCCGGCTGCCAGGTGGCCTCTACCATGTTGGTATGGAGCAAGGATGATGGTGTTTCC
TGGAGCACACCCCGGAATCTCTCCCTGGATATTGGCACTGAAGTGTTTGCCCCTGGACCG
GGCTCTGGTATTCAGAAACAGCGGGAGCCACGGAAGGGCCGCCTCATCGTGTGTGGCCAT
GGGACGCTGGAGCGGGACGGAGTCTTCTGTCTCCTCAGCGATGATCATGGTGCCTCCTGG
CGCTACGGAAGTGGGGTCAGCGGCATCCCCTACGGTCAGCCCAAGCAGGAAAATGATTTC
AATCCTGATGAATGCCAGCCCTATGAGCTCCCAGATGGCTCAGTCGTCATCAATGCCCGA
AACCAGAACAACTACCACTGCCACTGCCGAATTGTCCTCCGCAGCTATGATGCCTGTGAT
ACACTAAGGCCCCGTGATGTGACCTTCGACCCTGAGCTCGTGGACCCTGTGGTAGCTGCA
GGAGCTGTAGTCACCAGCTCCGGCATTGTCTTCTTCTCCAACCCAGCACATCCAGAGTTC
CGAGTGAACCTGACCCTGCGATGGAGCTTCAGCAATGGTACCTCATGGCGGAAAGAGACA
GTCCAGCTATGGCCAGGCCCCAGTGGCTATTCATCCCTGGCAACCCTGGAGGGCAGCATG
GATGGAGAGGAGCAGGCCCCCCAGCTCTACGTCCTGTATGAGAAAGGCCGGAACCACTAC
ACAGAGAGCATCTCCGTGGCCAAAATCAGTGTCTATGGGACACTC
Enzyme 10 GenBank Gene ID CR541916 Link Image
Enzyme 10 GeneCard ID Q5JQI0 Link Image
Enzyme 10 GenAtlas ID NEU1 Link Image
Enzyme 10 HGNC ID HGNC:7758 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16428
Enzyme 11 Name cDNA FLJ31531 fis, clone NT2RI2000585, highly similar to Sialate O-acetylesterase (EC 3.1.1.53)
Enzyme 11 Synonyms
  1. SubName: Sialic acid acetylesterase
Enzyme 11 Gene Name SIAE
Enzyme 11 Protein Sequence >cDNA FLJ31531 fis, clone NT2RI2000585, highly similar to Sialate O-acetylesterase (EC 3.1.1.53) 
MVAPGLVLGLVLPLILWADRSAGIGFRFASYINNDMVLQKEPAGAVIWGFGTPGATVTVT
LRQGQETIMKKVTSVKAHSDTWMVVLDPMKPGGPFEVMAQQTLEKINFTLRVHDVLFGDV
WLCSGQSNMQMTVLQIFNATRELSNTAAYQSVRILSVSPIQAEQELEDLVAVDLQWSKPT
SENLGHGYFKYMSAVCWLFGRHLYDTLQYPIGLIASSWGGTPIEAWSSGRSLKACGVPKQ
GSIPYDSVTGPSKHSVLWNAMIHPLCNMTLKGVVWYQGESNINYNTDLYNCTFPALIEDW
RETFHRGSQGQTERFFPFGLVQLSSDLSKKSSDDGFPQIRWHQTADFGYVPNPKMPNTFM
AVAMDLCDRDSPFGSIHPRDKQTVAYRLHLGARALAYGEKNLTFEGPLPEKIELLAHKGL
LNLTYYQQIQVQKKDNKIFEISCCSDHRCKWLPASMNTVSTQSLTLAIDSCHGTVVALRY
AWTTWPCEYKQCPLYHPSSALPAPPFIAFITDQGPGHQSNVAK
Enzyme 11 Number of Residues 523
Enzyme 11 Molecular Weight 58315
Enzyme 11 Theoretical pI 7.35
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate [RN:R01810] ALL_REAC R01810
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID B3KPB0 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B3KPB0_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK056093 Link Image
Enzyme 11 GeneCard ID B3KPB0 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location 11
Enzyme 11 Locus 11q24
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16530
Enzyme 12 Name cDNA, FLJ96858, Homo sapiens N-acetylneuraminic acid synthase (sialic acid synthase) (NANS), mRNA (N-acetylneuraminic acid synthase (Sialic acid synthase), isoform CRA_b)
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name NANS
Enzyme 12 Protein Sequence >cDNA, FLJ96858, Homo sapiens N-acetylneuraminic acid synthase (sialic acid synthase) (NANS), mRNA (N-acetylneuraminic acid synthase (Sialic acid synthase), isoform CRA_b) 
MPLELELCPGRWVGGQHPCFIIAEIGQNHQGDLDVAKRMIRMAKECGADCAKFQKSELEF
KFNRKALERPYTSKHSWGKTYGEHKRHLEFSHDQYRELQRYAEEVGIFFTASGMDEMAVE
FLHELNVPFFKVGSGDTNNFPYLEKTAKKGRPMVISSGMQSMDTMKQVYQIVKPLNPNFC
FLQCTSAYPLQPEDVNLRVISEYQKLFPDIPIGYSGHETGIAISVAAVALGAKVLERHIT
LDKTWKGSDHSASLEPGELAELVRSVRLVERALGSPTKQLLPCEMACNEKLGKSVVAKVK
IPEGTILTMDMLTVKVGEPKGYPPEDIFNLVGKKVLVTVEEDDTIMEELVDNHGKKIKS
Enzyme 12 Number of Residues 359
Enzyme 12 Molecular Weight 40308
Enzyme 12 Theoretical pI 6.73
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Cell wall/membrane/envelope biogenesis
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID B2RE98 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B2RE98_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK316608 Link Image
Enzyme 12 GeneCard ID B2RE98 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16531
Enzyme 13 Name cDNA FLJ30910 fis, clone FEBRA2006270, highly similar to N-acylneuraminate-9-phosphatase (EC 3.1.3.29)
Enzyme 13 Synonyms
  1. SubName: N-acetylneuraminic acid phosphatase
Enzyme 13 Gene Name NANP
Enzyme 13 Protein Sequence >cDNA FLJ30910 fis, clone FEBRA2006270, highly similar to N-acylneuraminate-9-phosphatase (EC 3.1.3.29) 
MGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKEC
FHPYNTCITDLRTSHWEEAIQETKGGAANRKLAEECYFLWKSTRLQHMTLAEDVKAMLTE
LRKEVRLLLLTNGDRQTQREKIEACACQSYFDAVVVGGEQREEKPAPSIFYYCCNLLGVQ
PGDCVMVGDTLETDIQGGLNAGLKATVWINKNGIVPLKSSPVPHYMVSSVLELPALLQSI
DCKVSMST
Enzyme 13 Number of Residues 248
Enzyme 13 Molecular Weight 27813
Enzyme 13 Theoretical pI 6.35
Enzyme 13 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoglycolate phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate [RN:R02597] ALL_REAC R02597 > R01805
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B3KP12 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B3KP12_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK055472 Link Image
Enzyme 13 GeneCard ID B3KP12 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location 20
Enzyme 13 Locus 20p11.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available