Full text data of GNPDA1
GNPDA1
(GNPI, HLN, KIAA0060)
[Confidence: low (only semi-automatic identification from reviews)]
Glucosamine-6-phosphate isomerase 1; 3.5.99.6 (Glucosamine-6-phosphate deaminase 1; GNPDA 1; GlcN6P deaminase 1; Oscillin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Glucosamine-6-phosphate isomerase 1; 3.5.99.6 (Glucosamine-6-phosphate deaminase 1; GNPDA 1; GlcN6P deaminase 1; Oscillin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46926
ID GNPI1_HUMAN Reviewed; 289 AA.
AC P46926; D3DQE7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Glucosamine-6-phosphate isomerase 1;
DE EC=3.5.99.6;
DE AltName: Full=Glucosamine-6-phosphate deaminase 1;
DE Short=GNPDA 1;
DE Short=GlcN6P deaminase 1;
DE AltName: Full=Oscillin;
GN Name=GNPDA1; Synonyms=GNPI, HLN, KIAA0060;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9438414;
RA Wolosker H., Kline D., Bian Y., Blackshaw S., Cameron A.M.,
RA Fralich T.J., Schnaar R.L., Snyder S.H.;
RT "Molecularly cloned mammalian glucosamine-6-phosphate deaminase
RT localizes to transporting epithelium and lacks oscillin activity.";
RL FASEB J. 12:91-99(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9714720; DOI=10.1016/S0378-1119(98)00335-7;
RA Shevchenko V., Hogben M., Ekong R., Parrington J., Lai F.A.;
RT "The human glucosamine-6-phosphate deaminase gene: cDNA cloning and
RT expression, genomic organization and chromosomal localization.";
RL Gene 216:31-38(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Testis;
RA Hirata S., Koh T., Hoshi K.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT.
RX PubMed=12965206; DOI=10.1016/S0014-5793(03)00896-2;
RA Arreola R., Valderrama B., Morante M.L., Horjales E.;
RT "Two mammalian glucosamine-6-phosphate deaminases: a structural and
RT genetic study.";
RL FEBS Lett. 551:63-70(2003).
CC -!- FUNCTION: Seems to trigger calcium oscillations in mammalian eggs.
CC These oscillations serve as the essential trigger for egg
CC activation and early development of the embryo (By similarity).
CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 6-phosphate + H(2)O = D-
CC fructose 6-phosphate + NH(3).
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06544.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF048826; AAC05123.1; -; mRNA.
DR EMBL; AJ002231; CAA05259.1; -; mRNA.
DR EMBL; AF029914; AAB84217.1; -; mRNA.
DR EMBL; AF035809; AAB88748.1; -; Genomic_DNA.
DR EMBL; AF035804; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035805; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035806; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035807; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035808; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; D31766; BAA06544.2; ALT_INIT; mRNA.
DR EMBL; AC005740; AAC62119.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61890.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61891.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61892.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61893.1; -; Genomic_DNA.
DR EMBL; BC012853; AAH12853.1; -; mRNA.
DR EMBL; BC020769; AAH20769.1; -; mRNA.
DR EMBL; BC022322; AAH22322.1; -; mRNA.
DR RefSeq; NP_005462.1; NM_005471.4.
DR RefSeq; XP_005268406.1; XM_005268349.1.
DR RefSeq; XP_005268407.1; XM_005268350.1.
DR RefSeq; XP_005268408.1; XM_005268351.1.
DR UniGene; Hs.633853; -.
DR PDB; 1NE7; X-ray; 1.75 A; A/B/C/D/E/F=1-289.
DR PDBsum; 1NE7; -.
DR ProteinModelPortal; P46926; -.
DR SMR; P46926; 1-281.
DR IntAct; P46926; 1.
DR STRING; 9606.ENSP00000311876; -.
DR PhosphoSite; P46926; -.
DR DMDM; 1171639; -.
DR PaxDb; P46926; -.
DR PeptideAtlas; P46926; -.
DR PRIDE; P46926; -.
DR DNASU; 10007; -.
DR Ensembl; ENST00000311337; ENSP00000311876; ENSG00000113552.
DR Ensembl; ENST00000500692; ENSP00000424275; ENSG00000113552.
DR Ensembl; ENST00000503794; ENSP00000423485; ENSG00000113552.
DR Ensembl; ENST00000508177; ENSP00000423674; ENSG00000113552.
DR GeneID; 10007; -.
DR KEGG; hsa:10007; -.
DR UCSC; uc003lmf.4; human.
DR CTD; 10007; -.
DR GeneCards; GC05M141360; -.
DR HGNC; HGNC:4417; GNPDA1.
DR HPA; HPA000499; -.
DR MIM; 601798; gene.
DR neXtProt; NX_P46926; -.
DR PharmGKB; PA28796; -.
DR eggNOG; COG0363; -.
DR HOGENOM; HOG000064979; -.
DR HOVERGEN; HBG002546; -.
DR InParanoid; P46926; -.
DR KO; K02564; -.
DR PhylomeDB; P46926; -.
DR SABIO-RK; P46926; -.
DR EvolutionaryTrace; P46926; -.
DR GeneWiki; GNPDA1; -.
DR GenomeRNAi; 10007; -.
DR NextBio; 37805; -.
DR PRO; PR:P46926; -.
DR ArrayExpress; P46926; -.
DR Bgee; P46926; -.
DR CleanEx; HS_GNPDA1; -.
DR Genevestigator; P46926; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IMP:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB.
DR GO; GO:0006043; P:glucosamine catabolic process; IMP:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR GO; GO:0007338; P:single fertilization; TAS:ProtInc.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1 289 Glucosamine-6-phosphate isomerase 1.
FT /FTId=PRO_0000160122.
FT ACT_SITE 72 72 Proton acceptor; for enolization step (By
FT similarity).
FT ACT_SITE 141 141 For ring-opening step (By similarity).
FT ACT_SITE 143 143 Proton acceptor; for ring-opening step
FT (By similarity).
FT ACT_SITE 148 148 For ring-opening step (By similarity).
FT MOD_RES 64 64 N6-acetyllysine.
FT STRAND 2 8
FT HELIX 9 27
FT STRAND 35 39
FT HELIX 43 57
FT STRAND 66 74
FT HELIX 85 92
FT HELIX 94 96
FT HELIX 101 103
FT HELIX 114 127
FT STRAND 132 136
FT STRAND 157 161
FT HELIX 164 170
FT HELIX 171 173
FT TURN 174 176
FT HELIX 178 180
FT STRAND 183 187
FT HELIX 190 194
FT STRAND 199 203
FT HELIX 206 208
FT HELIX 209 216
FT HELIX 225 231
FT STRAND 233 240
FT HELIX 241 244
FT HELIX 249 257
FT HELIX 259 262
FT HELIX 263 265
SQ SEQUENCE 289 AA; 32669 MW; 4111F655D574F74F CRC64;
MKLIILEHYS QASEWAAKYI RNRIIQFNPG PEKYFTLGLP TGSTPLGCYK KLIEYYKNGD
LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH PENTHILDGN AVDLQAECDA
FEEKIKAAGG IELFVGGIGP DGHIAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGELTK
VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD
EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKETEKS QSSKKPYSD
//
ID GNPI1_HUMAN Reviewed; 289 AA.
AC P46926; D3DQE7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Glucosamine-6-phosphate isomerase 1;
DE EC=3.5.99.6;
DE AltName: Full=Glucosamine-6-phosphate deaminase 1;
DE Short=GNPDA 1;
DE Short=GlcN6P deaminase 1;
DE AltName: Full=Oscillin;
GN Name=GNPDA1; Synonyms=GNPI, HLN, KIAA0060;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9438414;
RA Wolosker H., Kline D., Bian Y., Blackshaw S., Cameron A.M.,
RA Fralich T.J., Schnaar R.L., Snyder S.H.;
RT "Molecularly cloned mammalian glucosamine-6-phosphate deaminase
RT localizes to transporting epithelium and lacks oscillin activity.";
RL FASEB J. 12:91-99(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9714720; DOI=10.1016/S0378-1119(98)00335-7;
RA Shevchenko V., Hogben M., Ekong R., Parrington J., Lai F.A.;
RT "The human glucosamine-6-phosphate deaminase gene: cDNA cloning and
RT expression, genomic organization and chromosomal localization.";
RL Gene 216:31-38(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Testis;
RA Hirata S., Koh T., Hoshi K.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT.
RX PubMed=12965206; DOI=10.1016/S0014-5793(03)00896-2;
RA Arreola R., Valderrama B., Morante M.L., Horjales E.;
RT "Two mammalian glucosamine-6-phosphate deaminases: a structural and
RT genetic study.";
RL FEBS Lett. 551:63-70(2003).
CC -!- FUNCTION: Seems to trigger calcium oscillations in mammalian eggs.
CC These oscillations serve as the essential trigger for egg
CC activation and early development of the embryo (By similarity).
CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 6-phosphate + H(2)O = D-
CC fructose 6-phosphate + NH(3).
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06544.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF048826; AAC05123.1; -; mRNA.
DR EMBL; AJ002231; CAA05259.1; -; mRNA.
DR EMBL; AF029914; AAB84217.1; -; mRNA.
DR EMBL; AF035809; AAB88748.1; -; Genomic_DNA.
DR EMBL; AF035804; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035805; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035806; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035807; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; AF035808; AAB88748.1; JOINED; Genomic_DNA.
DR EMBL; D31766; BAA06544.2; ALT_INIT; mRNA.
DR EMBL; AC005740; AAC62119.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61890.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61891.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61892.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61893.1; -; Genomic_DNA.
DR EMBL; BC012853; AAH12853.1; -; mRNA.
DR EMBL; BC020769; AAH20769.1; -; mRNA.
DR EMBL; BC022322; AAH22322.1; -; mRNA.
DR RefSeq; NP_005462.1; NM_005471.4.
DR RefSeq; XP_005268406.1; XM_005268349.1.
DR RefSeq; XP_005268407.1; XM_005268350.1.
DR RefSeq; XP_005268408.1; XM_005268351.1.
DR UniGene; Hs.633853; -.
DR PDB; 1NE7; X-ray; 1.75 A; A/B/C/D/E/F=1-289.
DR PDBsum; 1NE7; -.
DR ProteinModelPortal; P46926; -.
DR SMR; P46926; 1-281.
DR IntAct; P46926; 1.
DR STRING; 9606.ENSP00000311876; -.
DR PhosphoSite; P46926; -.
DR DMDM; 1171639; -.
DR PaxDb; P46926; -.
DR PeptideAtlas; P46926; -.
DR PRIDE; P46926; -.
DR DNASU; 10007; -.
DR Ensembl; ENST00000311337; ENSP00000311876; ENSG00000113552.
DR Ensembl; ENST00000500692; ENSP00000424275; ENSG00000113552.
DR Ensembl; ENST00000503794; ENSP00000423485; ENSG00000113552.
DR Ensembl; ENST00000508177; ENSP00000423674; ENSG00000113552.
DR GeneID; 10007; -.
DR KEGG; hsa:10007; -.
DR UCSC; uc003lmf.4; human.
DR CTD; 10007; -.
DR GeneCards; GC05M141360; -.
DR HGNC; HGNC:4417; GNPDA1.
DR HPA; HPA000499; -.
DR MIM; 601798; gene.
DR neXtProt; NX_P46926; -.
DR PharmGKB; PA28796; -.
DR eggNOG; COG0363; -.
DR HOGENOM; HOG000064979; -.
DR HOVERGEN; HBG002546; -.
DR InParanoid; P46926; -.
DR KO; K02564; -.
DR PhylomeDB; P46926; -.
DR SABIO-RK; P46926; -.
DR EvolutionaryTrace; P46926; -.
DR GeneWiki; GNPDA1; -.
DR GenomeRNAi; 10007; -.
DR NextBio; 37805; -.
DR PRO; PR:P46926; -.
DR ArrayExpress; P46926; -.
DR Bgee; P46926; -.
DR CleanEx; HS_GNPDA1; -.
DR Genevestigator; P46926; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IMP:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB.
DR GO; GO:0006043; P:glucosamine catabolic process; IMP:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR GO; GO:0007338; P:single fertilization; TAS:ProtInc.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1 289 Glucosamine-6-phosphate isomerase 1.
FT /FTId=PRO_0000160122.
FT ACT_SITE 72 72 Proton acceptor; for enolization step (By
FT similarity).
FT ACT_SITE 141 141 For ring-opening step (By similarity).
FT ACT_SITE 143 143 Proton acceptor; for ring-opening step
FT (By similarity).
FT ACT_SITE 148 148 For ring-opening step (By similarity).
FT MOD_RES 64 64 N6-acetyllysine.
FT STRAND 2 8
FT HELIX 9 27
FT STRAND 35 39
FT HELIX 43 57
FT STRAND 66 74
FT HELIX 85 92
FT HELIX 94 96
FT HELIX 101 103
FT HELIX 114 127
FT STRAND 132 136
FT STRAND 157 161
FT HELIX 164 170
FT HELIX 171 173
FT TURN 174 176
FT HELIX 178 180
FT STRAND 183 187
FT HELIX 190 194
FT STRAND 199 203
FT HELIX 206 208
FT HELIX 209 216
FT HELIX 225 231
FT STRAND 233 240
FT HELIX 241 244
FT HELIX 249 257
FT HELIX 259 262
FT HELIX 263 265
SQ SEQUENCE 289 AA; 32669 MW; 4111F655D574F74F CRC64;
MKLIILEHYS QASEWAAKYI RNRIIQFNPG PEKYFTLGLP TGSTPLGCYK KLIEYYKNGD
LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH PENTHILDGN AVDLQAECDA
FEEKIKAAGG IELFVGGIGP DGHIAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGELTK
VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD
EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKETEKS QSSKKPYSD
//
MIM
601798
*RECORD*
*FIELD* NO
601798
*FIELD* TI
*601798 GLUCOSAMINE-6-PHOSPHATE DEAMINASE 1; GNPDA1
;;GNP1;;
GNPI;;
OSCILLIN, HAMSTER, HOMOLOG OF;;
read moreKIAA0060
*FIELD* TX
DESCRIPTION
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).
CLONING
By sequencing clones obtained from the KG-1 immature myeloid cell line,
Nomura et al. (1994) cloned GNPDA1, which they designated KIAA0060. The
deduced protein contains 289 amino acids. Northern blot analysis
detected GNPDA1 expression in all human tissues and cell lines examined,
with highest expression in ovary and colon and in KG-1 and HeLa cell
lines.
The hamster sperm oscillin protein is responsible for oocyte calcium
oscillations. By screening a testis cDNA library for a homolog of
hamster oscillin, Shevchenko et al. (1998) obtained a cDNA encoding
GNPI. The deduced 289-amino acid protein is 96% identical to the hamster
sequence. SDS-PAGE and Western blot analysis showed that GNPI was
expressed as a 33-kD cytosolic protein in various cell lines.
By screening a mouse EST database for sequences similar to hamster
oscillin, followed by screening human BAC genomic libraries by PCR,
Nakamura et al. (2000) identified the GNPI gene. Northern and dot blot
analyses revealed ubiquitous expression that was highest in spleen,
ovary, kidney, uterus, and testis. Promoter analysis indicated that GNPI
is most likely a housekeeping gene.
GENE FUNCTION
In the course of investigating hexosamine catabolism in the human
malaria parasite, Plasmodium falciparum, Weidanz et al. (1995) became
aware of deficiencies in understanding the relevant enzymatic reactions
in the host erythrocyte. For that reason, they undertook studies of
human glucosamine-6-phosphate deaminase using a newly developed
sensitive radiometric assay. They characterized biochemically the
erythrocyte enzyme and reported data on its kinetics, temperature
stability, and chromatographic purification. Weidanz et al. (1995) noted
that the nucleotide sequence of the nagB gene, encoding the deaminase in
E. coli K12, had been determined (Rogers et al., 1988).
Functional analysis by Shevchenko et al. (1998) showed that GNPI had
glucosamine-6-phosphate deaminase activity. However, it did not induce
calcium oscillations in mammalian eggs.
BIOCHEMICAL FEATURES
Arreola et al. (2003) solved the crystal structure of human GNP1 in the
presence of an allosteric activator, a competitive inhibitor, ammonia,
inorganic sulfate, and a cryoprotectant to 1.75-angstrom resolution.
They found that, like E. coli Gnp1, human GNP1 formed a 6-monomer unit.
However, each of the 6 GNP1 monomers showed a different conformation for
the active-site lid, and all conformations differed from that observed
in the E. coli enzyme. Moreover, all human GNP1 monomers differed from
E. coli Gnp1 in the phosphate-binding loop.
GENE STRUCTURE
Shevchenko et al. (1998) determined that the single-copy GNPI gene
contains 8 exons.
Nakamura et al. (2000) found that the GNPI gene spans approximately 12.4
kb and contains 8 exons.
Arreola et al. (2003) determined that the GNPDA1 gene contains 6 exons.
MAPPING
Using FISH, Shevchenko et al. (1998) mapped the GNPI gene to chromosome
5q31.
*FIELD* RF
1. Arreola, R.; Valderrama, B.; Morante, M. L.; Horjales, E.: Two
mammalian glucosamine-6-phosphate deaminases: a structural and genetic
study. FEBS Lett. 551: 63-70, 2003.
2. Nakamura, Y.; Miura, K.; Fujino, Y.; Iwao, H.; Ogita, S.; Yamanaka,
S.: Evolution, structure, and expression of GNPI/oscillin orthologous
genes. Genomics 68: 179-186, 2000.
3. 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. 1: 223-229, 1994.
4. Rogers, M. J.; Ohgi, T.; Plumbridge, J.; Soll, D.: Nucleotide
sequences of the E. coli nagE and nagB genes: the structural genes
for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate:
sugar phosphotransferase system and for glucosamine 6-phosphate deaminase. Gene 62:
197-207, 1988.
5. Shevchenko, V.; Hogben, M.; Ekong, R.; Parrington, J.; Lai, F.
A.: The human glucosamine-6-phosphate deaminase gene: cDNA cloning
and expression, genomic organization and chromosomal localization. Gene 216:
31-38, 1998.
6. Weidanz, J. A.; Campbell, P.; DeLucas, L. J.; Jin, J.; Moore, D.;
Roden, L.; Yu, H.; Heilmann, E.; Vezza, A. C.: Glucosamine 6-phosphate
deaminase in normal human erythrocytes. Brit. J. Haemat. 91: 72-79,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 1/14/2010
Paul J. Converse - updated: 12/4/2000
*FIELD* CD
Victor A. McKusick: 5/13/1997
*FIELD* ED
mgross: 01/14/2010
mgross: 1/14/2010
mgross: 12/5/2000
terry: 12/4/2000
alopez: 9/10/1999
mark: 12/8/1997
jenny: 5/13/1997
*RECORD*
*FIELD* NO
601798
*FIELD* TI
*601798 GLUCOSAMINE-6-PHOSPHATE DEAMINASE 1; GNPDA1
;;GNP1;;
GNPI;;
OSCILLIN, HAMSTER, HOMOLOG OF;;
read moreKIAA0060
*FIELD* TX
DESCRIPTION
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).
CLONING
By sequencing clones obtained from the KG-1 immature myeloid cell line,
Nomura et al. (1994) cloned GNPDA1, which they designated KIAA0060. The
deduced protein contains 289 amino acids. Northern blot analysis
detected GNPDA1 expression in all human tissues and cell lines examined,
with highest expression in ovary and colon and in KG-1 and HeLa cell
lines.
The hamster sperm oscillin protein is responsible for oocyte calcium
oscillations. By screening a testis cDNA library for a homolog of
hamster oscillin, Shevchenko et al. (1998) obtained a cDNA encoding
GNPI. The deduced 289-amino acid protein is 96% identical to the hamster
sequence. SDS-PAGE and Western blot analysis showed that GNPI was
expressed as a 33-kD cytosolic protein in various cell lines.
By screening a mouse EST database for sequences similar to hamster
oscillin, followed by screening human BAC genomic libraries by PCR,
Nakamura et al. (2000) identified the GNPI gene. Northern and dot blot
analyses revealed ubiquitous expression that was highest in spleen,
ovary, kidney, uterus, and testis. Promoter analysis indicated that GNPI
is most likely a housekeeping gene.
GENE FUNCTION
In the course of investigating hexosamine catabolism in the human
malaria parasite, Plasmodium falciparum, Weidanz et al. (1995) became
aware of deficiencies in understanding the relevant enzymatic reactions
in the host erythrocyte. For that reason, they undertook studies of
human glucosamine-6-phosphate deaminase using a newly developed
sensitive radiometric assay. They characterized biochemically the
erythrocyte enzyme and reported data on its kinetics, temperature
stability, and chromatographic purification. Weidanz et al. (1995) noted
that the nucleotide sequence of the nagB gene, encoding the deaminase in
E. coli K12, had been determined (Rogers et al., 1988).
Functional analysis by Shevchenko et al. (1998) showed that GNPI had
glucosamine-6-phosphate deaminase activity. However, it did not induce
calcium oscillations in mammalian eggs.
BIOCHEMICAL FEATURES
Arreola et al. (2003) solved the crystal structure of human GNP1 in the
presence of an allosteric activator, a competitive inhibitor, ammonia,
inorganic sulfate, and a cryoprotectant to 1.75-angstrom resolution.
They found that, like E. coli Gnp1, human GNP1 formed a 6-monomer unit.
However, each of the 6 GNP1 monomers showed a different conformation for
the active-site lid, and all conformations differed from that observed
in the E. coli enzyme. Moreover, all human GNP1 monomers differed from
E. coli Gnp1 in the phosphate-binding loop.
GENE STRUCTURE
Shevchenko et al. (1998) determined that the single-copy GNPI gene
contains 8 exons.
Nakamura et al. (2000) found that the GNPI gene spans approximately 12.4
kb and contains 8 exons.
Arreola et al. (2003) determined that the GNPDA1 gene contains 6 exons.
MAPPING
Using FISH, Shevchenko et al. (1998) mapped the GNPI gene to chromosome
5q31.
*FIELD* RF
1. Arreola, R.; Valderrama, B.; Morante, M. L.; Horjales, E.: Two
mammalian glucosamine-6-phosphate deaminases: a structural and genetic
study. FEBS Lett. 551: 63-70, 2003.
2. Nakamura, Y.; Miura, K.; Fujino, Y.; Iwao, H.; Ogita, S.; Yamanaka,
S.: Evolution, structure, and expression of GNPI/oscillin orthologous
genes. Genomics 68: 179-186, 2000.
3. 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. 1: 223-229, 1994.
4. Rogers, M. J.; Ohgi, T.; Plumbridge, J.; Soll, D.: Nucleotide
sequences of the E. coli nagE and nagB genes: the structural genes
for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate:
sugar phosphotransferase system and for glucosamine 6-phosphate deaminase. Gene 62:
197-207, 1988.
5. Shevchenko, V.; Hogben, M.; Ekong, R.; Parrington, J.; Lai, F.
A.: The human glucosamine-6-phosphate deaminase gene: cDNA cloning
and expression, genomic organization and chromosomal localization. Gene 216:
31-38, 1998.
6. Weidanz, J. A.; Campbell, P.; DeLucas, L. J.; Jin, J.; Moore, D.;
Roden, L.; Yu, H.; Heilmann, E.; Vezza, A. C.: Glucosamine 6-phosphate
deaminase in normal human erythrocytes. Brit. J. Haemat. 91: 72-79,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 1/14/2010
Paul J. Converse - updated: 12/4/2000
*FIELD* CD
Victor A. McKusick: 5/13/1997
*FIELD* ED
mgross: 01/14/2010
mgross: 1/14/2010
mgross: 12/5/2000
terry: 12/4/2000
alopez: 9/10/1999
mark: 12/8/1997
jenny: 5/13/1997