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Human Metabolome Database Version 2.5

 

Showing metabocard for N-Acetylmannosamine (HMDB01129)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-16 16:43:18
Accession Number HMDB01129
Secondary Accession Numbers Not Available
Common Name N-Acetylmannosamine
Description N-Acetylmannosamine is a monosaccharide that is used as a precursor in the chemical or enzymatic synthesis of the neuraminic acids found in glycolipids and glycoproteins. N-Acetyl-D-mannosamine (ManNAc) is a specific substrate for the synthesis of N-acetylneuraminic acid, the essential precursor of bacterial capsular polysialic acid (PA). N-Acetyl-D-mannosamine is used for the synthesis of sialic acid. It is also a synthetic intermediate for a number of carbohydrate-derived families of biologically active compounds and pharmaceutical candidates.
Synonyms
  1. 2-Acetamido-2-deoxy-D-mannose
  2. N-acetyl-D-mannosamine
  3. N-acetylmannosamine
Chemical IUPAC Name N-[2,4,5-trihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide
Chemical Formula C8H15NO6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Monosaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • secondary carboxylic acid amide
  • heterocyclic compound
Biofunction
  • Component of Aminosugars metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 221.208
Monoisotopic Molecular Weight 221.089935
Isomeric SMILES CC(=O)N[C@@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O
Canonical SMILES CC(=O)NC1C(O)OC(CO)C(O)C1O
KEGG Compound ID C00645 Link Image
BioCyc ID N-ACETYL-D-MANNOSAMINE Link Image
BiGG ID 35606 Link Image
Wikipedia Link N-Acetylmannosamine Link Image
NuGOwiki Link HMDB01129 Link Image
Metagene Link HMDB01129 Link Image
METLIN ID 6024 Link Image
PubChem Compound 439281 Link Image
PubChem Substance 3918 Link Image
ChEBI ID 17122 Link Image
CAS Registry Number 3615-17-6
InChI Identifier InChI=1/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5+,6-,7-,8u/m1/s1
Synthesis Reference Satoh, Chiyoko; Akio, Kiyomoto. Nitrogen-containing sugars. I. Synthesis of 2-acetamido-2-deoxy-D-mannose from 1-deoxy-1-nitro-D-mannitol pentaacetate. Chemical & Pharmaceutical Bulletin (1964), 12(5), 615-19.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 254.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.60 [Predicted by ALOGPS]; -2.1 [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
Show Experimental Conditions Link Image
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 (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts —
Muscle —
Concentrations (Normal) Not Available
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. Sugawara T, Irie K, Iwasawa H, Yoshikawa T, Okuno S, Watanabe HK, Kato T, Shibukawa M, Ito Y: Synthesis of omega-(methoxycarbonyl)alkyl and 9-(methoxycarbonyl)-3,6-dioxanonyl glycopyranosides for the preparation of carbohydrate-protein conjugates. Carbohydr Res. 1992 Jun 4;230(1):117-49. [PubMed Link Image]
  2. Salama I, Hinderlich S, Shlomai Z, Eisenberg I, Krause S, Yarema K, Argov Z, Lochmuller H, Reutter W, Dabby R, Sadeh M, Ben-Bassat H, Mitrani-Rosenbaum S: No overall hyposialylation in hereditary inclusion body myopathy myoblasts carrying the homozygous M712T GNE mutation. Biochem Biophys Res Commun. 2005 Mar 4;328(1):221-6. [PubMed Link Image]
  3. Kamerling JP, Strecker G, Farriaux JP, Dorland L, Haverkamp J, Vliegenthart JF: 2-Acetamidoglucal, a new metabolite isolated from the urine of a patient with sialuria. Biochim Biophys Acta. 1979 Mar 22;583(3):403-8. [PubMed Link Image]
  4. Sala G, Dupre T, Seta N, Codogno P, Ghidoni R: Increased biosynthesis of glycosphingolipids in congenital disorder of glycosylation Ia (CDG-Ia) fibroblasts. Pediatr Res. 2002 Nov;52(5):645-51. [PubMed Link Image]
  5. von Nicolai H, Esser P, Lauer E: Partial purification and properties of neuraminidase from Bifidobacterium lactentis. Hoppe Seylers Z Physiol Chem. 1981 Feb;362(2):153-62. [PubMed Link Image]
  6. Wikipedia Link Image
Metabolic Enzymes
  1. Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
  2. N-acylglucosamine 2-epimerase
  3. Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a)
  4. N-acetylneuraminate lyase
  5. UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
  6. cDNA, FLJ96858, Homo sapiens N-acetylneuraminic acid synthase (sialic acid synthase) (NANS), mRNA (N-acetylneuraminic acid synthase (Sialic acid synthase), isoform CRA_b)
Enzyme 1 [top]
Enzyme 1 ID 5568
Enzyme 1 Name Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Enzyme 1 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 1 Gene Name GNE
Enzyme 1 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 1 Number of Residues 722
Enzyme 1 Molecular Weight 79276
Enzyme 1 Theoretical pI 6.79
Enzyme 1 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 1 General Function Cell wall/membrane/envelope biogenesis
Enzyme 1 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 1 Pathways
Enzyme 1 Reactions
  • UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4775362 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9Y223 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GLCNE_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID AJ238764 Link Image
Enzyme 1 GeneCard ID GNE Link Image
Enzyme 1 GenAtlas ID GNE Link Image
Enzyme 1 HGNC ID HGNC:23657 Link Image
Enzyme 1 Chromosome Location 9
Enzyme 1 Locus 9p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5570
Enzyme 2 Name N-acylglucosamine 2-epimerase
Enzyme 2 Synonyms
  1. GlcNAc 2-epimerase
  2. N- acetyl-D-glucosamine 2-epimerase
  3. AGE
  4. Renin-binding protein
  5. RnBP
Enzyme 2 Gene Name RENBP
Enzyme 2 Protein Sequence >N-acylglucosamine 2-epimerase 
MEKERETLQAWKERVGQELDRVVAFWMEHSHDQEHGGFFTCLGREGRVYDDLKYVWLQGR
QVWMYCRLYRTFERFRHAQLLDAAKAGGEFLLRYARVAPPGKKCAFVLTRDGRPVKVQRT
IFSECFYTMAMNELWRATGEVRYQTEAVEMMDQIVHWVQEDASGLGRPQLQGAPAAEPMA
VPMMLLNLVEQLGEADEELAGKYAELGDWCARRILQHVQRDGQAVLENVSEGGKELPGCL
GRQQNPGHTLEAGWFLLRHCIRKGDPELRAHVIDKFLLLPFHSGWDPDHGGLFYFQDADN
FCPTQLEWAMKLWWPHSEAMIAFLMGYSDSGDPVLLRLFYQVAEYTFRQFRDPEYGEWFG
YLSREGKVALSIKGGPFKGCFHVPRCLAMCEEMLGALLSRPAPAPSPAPTPACRGAE
Enzyme 2 Number of Residues 417
Enzyme 2 Molecular Weight 47747
Enzyme 2 Theoretical pI 6.20
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
  • mannose-6-phosphate isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • hexose metabolism
  • mannose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 Specific Function Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity
Enzyme 2 Pathways
Enzyme 2 Reactions
  • N-acyl-D-glucosamine = N-acyl-D-mannosamine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 220053 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P51606 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name RENBP_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1254 bp 
ATGGAGAAAGAGCGAGAGACTCTGCAGGCCTGGAAGGAGCGCGTGGGGCAGGAGCTGGAC
CGCGTGGTGGCTTTCTGGATGGAGCACTCCCACGACCAGGAGCACGGGGGCTTCTTCACG
TGCCTTGGCCGCGAGGGGCGGGTGTATGATGACCTCAAGTATGTGTGGCTGCAGGGGAGG
CAGGTATGGATGTATTGTCGCCTGTACCGCACTTTCGAGCGCTTCCGCCATGCTCAGCTT
CTGGACGCAGCAAAAGCAGGTGGTGAGTTCTTGCTGCGGTATGCCCGGGTGGCACCTCCT
GGCAAGAAGTGTGCCTTTGTGCTGACTCGGGACGGCCGCCCGGTCAAGGTGCAGCGAACC
ATCTTCAGTGAGTGTTTCTACACCATGGCCATGAACGAGCTGTGGAGAGCCACAGGGGAA
GTGCGGTACCAGACGGAAGCGGTGGAGATGATGGATCAGATCGTCCACTGGGTGCAGGAG
GACGCGTCGGGACTGGGCCGGCCCCAGCTCCAGGGGGCCCCGGCTGCGGAGCCCATGGCG
GTGCCCATGATGCTACTGAACCTGGTGGAGCAGCTCGGGGAGGCAGATGAGGAGCTGGCG
GGCAAATACGCAGAGCTGGGGGACTGGTGCGCCCGGAGGATTCTGCAGCACGTGCAGAGG
GATGGACAAGCTGTGCTGGAGAATGTGTCAGAGGGTGGCAAGGAACTTCCTGGCTGCCTG
GGGAGACAGCAGAACCCAGGCCACACGCTGGAAGCCGGCTGGTTTCTGCTCCGTCATTGC
ATTCGGAAAGGCGACCCCGAACTTCGAGCCCACGTGATTGACAAGTTCCTATTGTTGCCC
TTCCACTCCGGATGGGACCCTGACCACGGAGGCCTCTTTTACTTCCAGGATGCTGATAAC
TTCTGCCCCACCCAGCTGGAGTGGGCCATGAAGCTCTGGTGGCCACACAGTGAAGCCATG
ATTGCCTTCCTCATGGGTTACAGTGACAGTGGGGACCCTGTGCTGCTGCGCCTCTTCTAC
CAAGTGGCTGAGTACACCTTCCGCCAGTTTCGCGATCCCGAGTACGGGGAATGGTTTGGC
TACCTGAGCCGAGAGGGCAAGGTGGCCCTCTCCATCAAGGGAGGTCCTTTCAAAGGCTGC
TTCCACGTGCCGCGGTGCCTAGCCATGTGCGAGGAGATGCTGGGCGCCCTGCTGAGCCGC
CCCGCCCCCGCCCCCTCCCCCGCCCCCACCCCCGCCTGCCGAGGCGCGGAATAA
Enzyme 2 GenBank Gene ID D10232 Link Image
Enzyme 2 GeneCard ID RENBP Link Image
Enzyme 2 GenAtlas ID RENBP Link Image
Enzyme 2 HGNC ID HGNC:9959 Link Image
Enzyme 2 Chromosome Location X
Enzyme 2 Locus Xq28
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Inoue H, Takahashi S, Fukui K, Miyake Y: Genetic and molecular properties of human and rat renin-binding proteins with reference to the function of the leucine zipper motif. J Biochem (Tokyo). 1991 Oct;110(4):493-500. [PubMed Link Image]
  2. Takahashi S, Takahashi K, Kaneko T, Ogasawara H, Shindo S, Kobayashi M: Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase. J Biochem (Tokyo). 1999 Feb;125(2):348-53. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 12982
Enzyme 3 Name Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name PHPT1
Enzyme 3 Protein Sequence >Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a) 
MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKV
SGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTW
ANDGY
Enzyme 3 Number of Residues 125
Enzyme 3 Molecular Weight 13833
Enzyme 3 Theoretical pI Not Available
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID B1AMX1 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B1AMX1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID Not Available
Enzyme 3 GeneCard ID B1AMX1 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 12984
Enzyme 4 Name N-acetylneuraminate lyase
Enzyme 4 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 4 Gene Name NPL
Enzyme 4 Protein Sequence >N-acetylneuraminate lyase 
MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSV
SERRQVAEEWVTKGKDKLDQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWT
KDILINFLKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGILDKIPTFQGLKFSDTDLL
DFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFS
LALNYQFCIQRFINFVVKLGFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKL
KSLDFLSFTDLKDGNLEAGS
Enzyme 4 Number of Residues 320
Enzyme 4 Molecular Weight 35163
Enzyme 4 Theoretical pI 5.22
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 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 4 Pathways
Enzyme 4 Reactions
  • N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate [RN:R01811] ALL_REAC R01811
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 13430285 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9BXD5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NPL_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AF338436 Link Image
Enzyme 4 GeneCard ID Q9BXD5 Link Image
Enzyme 4 GenAtlas ID NPL Link Image
Enzyme 4 HGNC ID HGNC:16781 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. 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15263
Enzyme 5 Name UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name GNE
Enzyme 5 Protein Sequence >UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a) 
METYGYLQRESCFQGPHELYFKNLSKRNKQIMEKNGNNRKLRVCVATCNRADYSKLAPIM
FGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVG
LALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHA
ITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDV
KSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKG
IEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGE
NVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCF
PPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLI
LQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLH
LPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH
LVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQ
AAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALS
SVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY
Enzyme 5 Number of Residues 753
Enzyme 5 Molecular Weight 83067
Enzyme 5 Theoretical pI 6.93
Enzyme 5 GO Classification
Function
  • ATP binding
  • UDP-N-acetylglucosamine 2-epimerase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • isomerase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on carbohydrates and derivatives
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • N-acetylglucosamine metabolism
  • UDP-N-acetylglucosamine metabolism
  • alcohol metabolism
  • amine metabolism
  • amino sugar metabolism
  • carbohydrate biosynthesis
  • cellular metabolism
  • glucosamine metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • lipopolysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • monosaccharide metabolism
  • nitrogen compound metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
—
Enzyme 5 General Function Cell wall/membrane/envelope biogenesis
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine [RN:R00420] ALL_REAC R00420
  • (other) R00414
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 150368575 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A6PZH2 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A6PZH2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2262 bp 
ATGGAAACCTATGGTTATCTGCAGAGGGAGTCATGCTTTCAAGGACCTCATGAACTCTAT
TTTAAGAACCTCTCAAAACGAAACAAGCAAATCATGGAGAAGAATGGAAATAACCGAAAG
CTGCGGGTTTGTGTTGCTACTTGTAACCGTGCAGATTATTCTAAACTTGCCCCGATCATG
TTTGGCATTAAAACCGAACCTGAGTTCTTTGAACTTGATGTTGTGGTACTTGGCTCTCAC
CTGATAGATGACTATGGAAATACATATCGAATGATTGAACAAGATGACTTTGACATTAAC
ACCAGGCTACACACAATTGTGAGGGGAGAAGATGAGGCAGCCATGGTGGAGTCAGTAGGC
CTGGCCCTAGTGAAGCTGCCAGATGTCCTTAATCGCCTGAAGCCTGATATCATGATTGTT
CATGGAGACAGGTTTGATGCCCTGGCTCTGGCCACATCTGCTGCCTTGATGAACATCCGA
ATCCTTCACATTGAAGGTGGGGAAGTCAGTGGGACCATTGATGACTCTATCAGACATGCC
ATAACAAAACTGGCTCATTATCATGTGTGCTGCACCCGCAGTGCAGAGCAGCACCTGATA
TCCATGTGTGAGGACCATGATCGCATCCTTTTGGCAGGCTGCCCTTCCTATGACAAACTT
CTCTCAGCCAAGAACAAAGACTACATGAGCATCATTCGCATGTGGCTAGGTGATGATGTA
AAATCTAAAGATTACATTGTTGCACTACAGCACCCTGTGACCACTGACATTAAGCATTCC
ATAAAAATGTTTGAATTAACATTGGATGCACTTATCTCATTTAACAAGCGGACCCTAGTC
CTGTTTCCAAATATTGACGCAGGGAGCAAAGAGATGGTTCGAGTGATGCGGAAGAAGGGC
ATTGAGCATCATCCCAACTTTCGTGCAGTTAAACACGTCCCATTTGACCAGTTTATACAG
TTGGTTGCCCATGCTGGCTGTATGATTGGGAACAGCAGCTGTGGGGTTCGAGAAGTTGGA
GCTTTTGGAACACCTGTGATCAACCTGGGAACACGTCAGATTGGAAGAGAAACAGGGGAG
AATGTTCTTCATGTCCGGGATGCTGACACCCAAGACAAAATATTGCAAGCACTGCACCTT
CAGTTTGGTAAACAGTACCCTTGTTCAAAGATATATGGGGATGGAAATGCTGTTCCAAGG
ATTTTGAAGTTTCTCAAATCTATCGATCTTCAAGAGCCACTGCAAAAGAAATTCTGCTTT
CCTCCTGTGAAGGAGAATATCTCTCAAGATATTGACCATATTCTTGAAACTCTAAGTGCC
TTGGCCGTTGATCTTGGCGGGACGAACCTCCGAGTTGCAATAGTCAGCATGAAGGGTGAA
ATAGTTAAGAAGTATACTCAGTTCAATCCTAAAACCTATGAAGAGAGGATTAATTTAATC
CTACAGATGTGTGTGGAAGCTGCAGCAGAAGCTGTAAAACTGAACTGCAGAATTTTGGGA
GTAGGCATTTCCACAGGTGGCCGTGTAAATCCTCGGGAAGGAATTGTGCTGCATTCAACC
AAACTGATCCAAGAGTGGAACTCTGTGGACCTTAGGACCCCCCTTTCTGACACTTTGCAT
CTCCCTGTGTGGGTAGACAATGATGGCAACTGTGCTGCCCTGGCGGAAAGGAAATTTGGC
CAAGGAAAGGGACTGGAAAACTTTGTTACACTTATCACAGGCACAGGAATCGGTGGTGGA
ATTATCCATCAGCATGAATTGATCCACGGAAGCTCCTTCTGTGCTGCAGAACTGGGCCAC
CTTGTTGTGTCTCTGGATGGGCCTGATTGTTCCTGTGGAAGCCATGGGTGCATTGAAGCA
TACGCCTCTGGAATGGCCTTGCAGAGGGAGGCAAAAAAGCTCCATGATGAGGACCTGCTC
TTGGTGGAAGGGATGTCAGTGCCAAAAGATGAGGCTGTGGGTGCGCTCCATCTCATCCAA
GCTGCGAAACTTGGCAATGCGAAGGCCCAGAGCATCCTAAGAACAGCTGGAACAGCTTTG
GGTCTTGGGGTTGTGAACATCCTCCATACCATGAATCCCTCCCTTGTGATCCTCTCCGGA
GTCCTGGCCAGTCACTATATCCACATTGTCAAAGACGTCATTCGCCAGCAGGCCTTGTCC
TCCGTGCAGGACGTGGATGTGGTGGTTTCGGATTTGGTTGACCCCGCCCTGCTGGGTGCT
GCCAGCATGGTTCTGGACTACACAACACGCAGGATCTACTAG
Enzyme 5 GenBank Gene ID AM697708 Link Image
Enzyme 5 GeneCard ID A6PZH2 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16530
Enzyme 6 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 6 Synonyms Not Available
Enzyme 6 Gene Name NANS
Enzyme 6 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 6 Number of Residues 359
Enzyme 6 Molecular Weight 40308
Enzyme 6 Theoretical pI 6.73
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Cell wall/membrane/envelope biogenesis
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B2RE98 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2RE98_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AK316608 Link Image
Enzyme 6 GeneCard ID B2RE98 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available