- GPI; HLN; GNP1; GNPI; GNPDA
- Summary
- Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an
allosteric enzyme that catalyzes the reversible conversion of
D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium
(Arreola et al., 2003 [PubMed 12965206]).[supplied by OMIM, Jan 2010]
- Preferred Names
- glucosamine-6-phosphate isomerase 1
- Names
- GNPDA 1
- glcN6P deaminase 1
- oscillin
Related articles in PubMed
- Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate deaminase. Alvarez-Añorve LI, et al. Biochim Biophys Acta, 2011 Dec. PMID 21807125
- Cloning and functional characterization of GNPI2, a novel human homolog of glucosamine-6-phosphate isomerase/oscillin. Zhang J, et al. J Cell Biochem, 2003 Apr 1. PMID 12616532
- The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization. Shevchenko V, et al. Gene, 1998 Aug 17. PMID 9714720
- Glucosamine 6-phosphate deaminase in normal human erythrocytes. Weidanz JA, et al. Br J Haematol, 1995 Sep. PMID 7577655
- Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity. Wolosker H, et al. FASEB J, 1998 Jan. PMID 9438414
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
- GNPDA1 siRNA induced GFAT2 which was hardly measurable in these cells under standard culture conditions, GNPDA2 siRNA increased GFAT1, and GFAT1 siRNA increased the expression of hyaluronan synthase 2 (HAS2). Silencing of GFAT1 stimulated GNPDA1 and GDPDA2, and inhibited cell migration.
- Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate deaminase.
- Sequence analysis and crystallographic structure of GNP1.
-
identification, chromosomal localization and functional analysis of cDNA encoding GNPI/Oscillin homolog named GNPI2.The enzyme, glucosamine-6-phosphate isomerase (GNPI) or deaminase (GNPDA) (EC 5.3.1.10), catalyzes the conversion of GNP to fructose-6-phosphate and ammonia, with an aldo/keto isomerization and an amination/deamination. A hamster sperm-derived protein (Oscillin) with high similarity to bacterial GNPI has been proved to be capable of inducing calcium oscillation in eggs at fertilization. GNPI/Oscillin was supposed to be an important factor in starting embryonic development. From the cDNA library of human dendritic cells (DC), we isolated a novel full-length cDNA encoding a 276-amino acid-residue protein that shares high homology with human GNPI/Oscillin. So, the novel molecule is named as GNPI2. The GNPI2 gene consists of seven exons and six introns. It is mapped to chromosome 4. Northern blot analysis indicated that the tissue distribution of GNPI2 mRNA is different from that of human GNPI or Oscillin mRNA. GNPI2 is ubiquitously expressed in most of human tissues with high expression in testis, ovary, placenta, and heart. Like GNPI, the recombinant GNPI2 has been proved to have the enzymatic activity to catalyze the conversion of GNP to fructose-6-phosphate. Our results indicated that GNPI2 is a novel protein with definite function as a GNPI.
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Konservoitu domeeni
SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A
ribose 5-phosphate isomerase (RPI_A), glucosamine-6-phosphate (GlcN6P)
deaminase, and 6-phosphogluconolactonase (6PGL). RPI catalyzes the
reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the
first step of the non-oxidative branch of the pentose phosphate
pathway. GlcN6P deaminase catalyzes the reversible conversion of GlcN6P
to D-fructose-6-phosphate (Fru6P) and ammonium, the last step of the
metabolic pathway of N-acetyl-D-glucosamine-6-phosphate. 6PGL converts
6-phosphoglucono-1,5-lactone to 6-phosphogluconate, the second step of
the oxidative phase of the pentose phosphate pathway.
glucosamine-6-phosphate isomerase 1 [Homo sapiens]
NCBI Reference Sequence: NP_005462.1
LOCUS NP_005462 289 aa linear PRI 22-NOV-2018 DEFINITION glucosamine-6-phosphate isomerase 1 [Homo sapiens]. ACCESSION NP_005462 VERSION NP_005462.1 DBSOURCE REFSEQ: accession NM_005471.5 KEYWORDS RefSeq. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 289) AUTHORS Oikari S, Makkonen K, Deen AJ, Tyni I, Karna R, Tammi RH and Tammi MI. TITLE Hexosamine biosynthesis in keratinocytes: roles of GFAT and GNPDA enzymes in the maintenance of UDP-GlcNAc content and hyaluronan synthesis JOURNAL Glycobiology 26 (7), 710-722 (2016) PUBMED 26887390 REMARK GeneRIF: GNPDA1 siRNA induced GFAT2 which was hardly measurable in these cells under standard culture conditions, GNPDA2 siRNA increased GFAT1, and GFAT1 siRNA increased the expression of hyaluronan synthase 2 (HAS2). Silencing of GFAT1 stimulated GNPDA1 and GDPDA2, and inhibited cell migration. REFERENCE 2 (residues 1 to 289) AUTHORS Alvarez-Anorve LI, Alonzo DA, Mora-Lugo R, Lara-Gonzalez S, Bustos-Jaimes I, Plumbridge J and Calcagno ML. TITLE Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate deaminase JOURNAL Biochim. Biophys. Acta 1814 (12), 1846-1853 (2011) PUBMED 21807125 REMARK GeneRIF: Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate deaminase. REFERENCE 3 (residues 1 to 289) AUTHORS Gonzalez-Begne M, Lu B, Han X, Hagen FK, Hand AR, Melvin JE and Yates JR. TITLE Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT) JOURNAL J. Proteome Res. 8 (3), 1304-1314 (2009) PUBMED 19199708 REFERENCE 4 (residues 1 to 289) AUTHORS Gonzales PA, Pisitkun T, Hoffert JD, Tchapyjnikov D, Star RA, Kleta R, Wang NS and Knepper MA. TITLE Large-scale proteomics and phosphoproteomics of urinary exosomes JOURNAL J. Am. Soc. Nephrol. 20 (2), 363-379 (2009) PUBMED 19056867 REFERENCE 5 (residues 1 to 289) AUTHORS Arreola R, Valderrama B, Morante ML and Horjales E. TITLE Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study JOURNAL FEBS Lett. 551 (1-3), 63-70 (2003) PUBMED 12965206 REMARK GeneRIF: Sequence analysis and crystallographic structure of GNP1. REFERENCE 6 (residues 1 to 289) AUTHORS Nakamura Y, Miura K, Fujino Y, Iwao H, Ogita S and Yamanaka S. TITLE Evolution, structure, and expression of GNPI/Oscillin orthologous genes JOURNAL Genomics 68 (2), 179-186 (2000) PUBMED 10964516 REFERENCE 7 (residues 1 to 289) AUTHORS Shevchenko V, Hogben M, Ekong R, Parrington J and Lai FA. TITLE The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization JOURNAL Gene 216 (1), 31-38 (1998) PUBMED 9714720 REFERENCE 8 (residues 1 to 289) AUTHORS Wolosker H, Kline D, Bian Y, Blackshaw S, Cameron AM, Fralich TJ, Schnaar RL and Snyder SH. TITLE Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity JOURNAL FASEB J. 12 (1), 91-99 (1998) PUBMED 9438414 REFERENCE 9 (residues 1 to 289) AUTHORS Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML and Horjales E. TITLE Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution JOURNAL Structure 3 (12), 1323-1332 (1995) PUBMED 8747459 REFERENCE 10 (residues 1 to 289) AUTHORS Weidanz JA, Campbell P, DeLucas LJ, Jin J, Moore D, Roden L, Yu H, Heilmann E and Vezza AC. TITLE Glucosamine 6-phosphate deaminase in normal human erythrocytes JOURNAL Br. J. Haematol. 91 (1), 72-79 (1995) PUBMED 7577655 COMMENT VALIDATED REFSEQ: This record has undergone validation or preliminary review. The reference sequence was derived from BC022322.1, AC005740.1 and CA432951.1. Summary: Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium (Arreola et al., 2003 [PubMed 12965206]).[supplied by OMIM, Jan 2010]. Sequence Note: The RefSeq transcript and protein were derived from transcript and genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR3476690.856559.1, SRR1660805.207409.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..289 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="5" /map="5q31.3" Protein 1..289 /product="glucosamine-6-phosphate isomerase 1" /EC_number="3.5.99.6" /note="oscillin; GNPDA 1; glcN6P deaminase 1" /calculated_mol_wt=32537 Region 1..253 /region_name="SugarP_isomerase" /note="SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A ribose 5-phosphate isomerase (RPI_A), glucosamine-6-phosphate (GlcN6P) deaminase, and 6-phosphogluconolactonase (6PGL). RPI catalyzes the reversible conversion of ribose-5-phosphate to...; cl00339" /db_xref="CDD:320918" Site order(41..44,71..72,137..138,143,145,172,208) /site_type="active" /db_xref="CDD:238693" Site 64 /site_type="other" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (P46926.1)" Site order(150,152..153,161,216..222,230..232) /site_type="other" /note="trimer interface [polypeptide binding]" /db_xref="CDD:238693" Site order(151..152,158..161) /site_type="other" /note="allosteric site" /db_xref="CDD:238693" Site 161 /site_type="other" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine. {ECO:0000250|UniProtKB:O88958}; propagated from UniProtKB/Swiss-Prot (P46926.1)" Site order(163,166..176,180..182) /site_type="active" /note="active site lid [active]" /db_xref="CDD:238693" Site order(168,206,210,241,244..247) /site_type="other" /note="hexamer (dimer of trimers) interface [polypeptide binding]" /db_xref="CDD:238693" CDS 1..289 /gene="GNPDA1" /gene_synonym="GNP1; GNPDA; GNPI; GPI; HLN" /coded_by="NM_005471.5:40..909" /db_xref="CCDS:CCDS4272.1" /db_xref="GeneID:10007" /db_xref="HGNC:HGNC:4417" /db_xref="MIM:601798" ORIGIN 1 mkliilehys qasewaakyi rnriiqfnpg pekyftlglp tgstplgcyk klieyykngd 61 lsfkyvktfn mdeyvglprd hpesyhsfmw nnffkhidih penthildgn avdlqaecda 121 feekikaagg ielfvggigp dghiafnepg sslvsrtrvk tlamdtilan arffdgeltk 181 vptmaltvgv gtvmdarevm ilitgahkaf alykaieegv nhmwtvsafq qhprtvfvcd 241 edatlelkvk tvkyfkglml vhnklvdply sikeketeks qsskkpysd //
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