GNPI1_MESAU
ID GNPI1_MESAU Reviewed; 289 AA.
AC Q64422;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Glucosamine-6-phosphate isomerase 1;
DE EC=3.5.99.6 {ECO:0000250|UniProtKB:P46926};
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;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8552195; DOI=10.1038/379364a0;
RA Parrington J., Swann K., Shevchenko V.I., Sesay A.K., Lai F.A.;
RT "Calcium oscillations in mammalian eggs triggered by a soluble sperm
RT protein.";
RL Nature 379:364-368(1996).
CC -!- FUNCTION: Catalyzes the reversible conversion of alpha-D-glucosamine 6-
CC phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and
CC ammonium ion, a regulatory reaction step in de novo uridine
CC diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via
CC hexosamine pathway. Deamination is coupled to aldo-keto isomerization
CC mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high
CC ammonium level can drive amination and isomerization of Fru-6P toward
CC hexosamines and UDP-GlcNAc synthesis (By similarity). Has a role in
CC fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and
CC their effects on hyaluronan synthesis that occur during tissue
CC remodeling (By similarity). Seems to trigger calcium oscillations in
CC mammalian eggs. These oscillations serve as the essential trigger for
CC egg activation and early development of the embryo (PubMed:8552195).
CC {ECO:0000250|UniProtKB:P46926, ECO:0000269|PubMed:8552195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
CC Evidence={ECO:0000250|UniProtKB:P46926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173;
CC Evidence={ECO:0000250|UniProtKB:P46926};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174;
CC Evidence={ECO:0000250|UniProtKB:P46926};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine-6-
CC phosphate (GlcNAc6P). {ECO:0000250|UniProtKB:P46926}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P46926}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P46926}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: At the equatorial segment of the sperm head.
CC {ECO:0000269|PubMed:8552195}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. {ECO:0000305}.
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DR EMBL; X94699; CAA64360.1; -; mRNA.
DR PIR; S68445; S68445.
DR RefSeq; NP_001268528.1; NM_001281599.1.
DR AlphaFoldDB; Q64422; -.
DR SMR; Q64422; -.
DR STRING; 10036.XP_005069257.1; -.
DR GeneID; 101825394; -.
DR CTD; 10007; -.
DR eggNOG; KOG3148; Eukaryota.
DR OrthoDB; 1425290at2759; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0006043; P:glucosamine catabolic process; ISS:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; ISS:UniProtKB.
DR CDD; cd01399; GlcN6P_deaminase; 1.
DR HAMAP; MF_01241; GlcN6P_deamin; 1.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Carbohydrate metabolism; Cytoplasm; Hydrolase; Isomerase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..289
FT /note="Glucosamine-6-phosphate isomerase 1"
FT /id="PRO_0000160123"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46926"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88958"
SQ SEQUENCE 289 AA; 32607 MW; 27D84551CFAC3C67 CRC64;
MKLIILEHYS QASEWAAKYI RNRIIQFNPG PDKYFTMGLP TGSTPLGCYQ KLIEYYKNGD
LSFKYVKTFN MDEYVGLPRE HPESYHSFMW NNFFKHIDIH PENTHILDGN AADLQAECDA
FEEKIRAAGG IELFVGGIGP DGHVAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGDLAK
VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD
EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKEIQKS QAAKKPYSD
