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Showing Protein Glucosamine-6-phosphate isomerase 1 (HMDBP00211)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 6 metabolites
Identification
HMDB Protein ID HMDBP00211
Secondary Accession Numbers
  • 5443
Name Glucosamine-6-phosphate isomerase 1
Synonyms
  1. GNPDA 1
  2. GlcN6P deaminase 1
  3. Glucosamine-6-phosphate deaminase 1
  4. Oscillin
Gene Name GNPDA1
Protein Type Unknown
Biological Properties
General Function Involved in carbohydrate metabolic process
Specific Function Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity).
Pathways
  • Amino sugar and nucleotide sugar metabolism
  • Amino Sugar Metabolism
  • G(M2)-Gangliosidosis: Variant B, Tay-sachs disease
  • Salla Disease/Infantile Sialic Acid Storage Disease
  • Sialuria or French Type Sialuria
  • Tay-Sachs Disease
Reactions
Glucosamine 6-phosphate + Water → Fructose 6-phosphate + Ammonia details
GO Classification
Biological Process
generation of precursor metabolites and energy
N-acetylglucosamine metabolic process
glucosamine catabolic process
single fertilization
carbohydrate metabolic process
Cellular Component
cytoplasm
Function
catalytic activity
isomerase activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, interconverting aldoses and ketoses
glucosamine-6-phosphate deaminase activity
Molecular Function
glucosamine-6-phosphate deaminase activity
hydrolase activity
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
amino sugar metabolic process
glucosamine metabolic process
n-acetylglucosamine metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 5
Locus 5q21
SNPs GNPDA1
Gene Sequence 
>870 bp
ATGAAGCTCATCATCCTGGAGCACTATTCTCAGGCGAGCGAGTGGGCGGCTAAATACATC
AGGAACCGTATCATCCAGTTTAACCCAGGGCCAGAGAAGTACTTCACCCTGGGGCTCCCC
ACTGGGAGTACCCCACTTGGCTGCTACAAGAAGCTGATTGAATACTATAAGAATGGGGAC
CTGTCCTTTAAATATGTGAAGACCTTCAACATGGATGAGTACGTGGGCCTTCCTCGAGAC
CACCCGGAGAGTTACCACTCCTTCATGTGGAACAACTTCTTCAAGCACATTGACATCCAC
CCAGAAAACACCCACATTCTGGATGGGAATGCAGTCGACCTACAGGCAGAATGTGATGCC
TTTGAAGAGAAGATCAAGGCTGCAGGTGGGATCGAGCTATTTGTTGGAGGCATCGGCCCT
GATGGACACATTGCCTTCAACGAGCCAGGCTCCAGTCTGGTGTCCAGGACCCGTGTGAAG
ACGCTGGCCATGGATACCATCCTGGCCAATGCTAGGTTCTTCGATGGAGAACTCACCAAG
GTGCCCACCATGGCCTTGACGGTGGGGGTGGGCACTGTCATGGATGCTAGAGAGGTGATG
ATCCTTATCACAGGTGCTCACAAGGCATTTGCTCTGTACAAGGCCATCGAGGAGGGAGTG
AACCACATGTGGACCGTGTCTGCCTTCCAGCAGCATCCCCGCACCGTGTTTGTGTGTGAC
GAGGATGCCACCTTGGAGCTGAAAGTGAAGACTGTCAAGTATTTCAAAGGTTTAATGCTT
GTTCATAACAAGTTGGTGGACCCCTTGTACAGTATCAAAGAGAAAGAAACTGAGAAAAGC
CAATCTTCGAAGAAACCATACAGCGATTAG
Protein Properties
Number of Residues 289
Molecular Weight 32668.29
Theoretical pI 6.912
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Glucosamine-6-phosphate isomerase 1
MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLPTGSTPLGCYKKLIEYYKNGD
LSFKYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA
FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGELTK
VPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD
EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKETEKSQSSKKPYSD
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P46926
UniProtKB/Swiss-Prot Entry Name GNPI1_HUMAN
PDB IDs
GenBank Gene ID AF048826
GeneCard ID GNPDA1
GenAtlas ID GNPDA1
HGNC ID HGNC:4417
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed:15372022 ]
  4. Wolosker H, Kline D, Bian Y, Blackshaw S, Cameron AM, Fralich TJ, Schnaar RL, Snyder SH: Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity. FASEB J. 1998 Jan;12(1):91-9. [PubMed:9438414 ]
  5. Shevchenko V, Hogben M, Ekong R, Parrington J, Lai FA: The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization. Gene. 1998 Aug 17;216(1):31-8. [PubMed:9714720 ]
  6. Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed:7584044 ]
  7. Arreola R, Valderrama B, Morante ML, Horjales E: Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study. FEBS Lett. 2003 Sep 11;551(1-3):63-70. [PubMed:12965206 ]