GNPI2_BOVIN
ID GNPI2_BOVIN Reviewed; 276 AA.
AC Q17QL1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glucosamine-6-phosphate isomerase 2;
DE EC=3.5.99.6 {ECO:0000250|UniProtKB:Q8TDQ7};
DE AltName: Full=Glucosamine-6-phosphate deaminase 2;
DE Short=GNPDA 2;
DE Short=GlcN6P deaminase 2;
GN Name=GNPDA2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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. Has a role in fine tuning the
CC metabolic fluctuations of cytosolic UDP-GlcNAc and their effects on
CC hyaluronan synthesis that occur during tissue remodeling.
CC {ECO:0000250|UniProtKB:Q8TDQ7}.
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:Q8TDQ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173;
CC Evidence={ECO:0000250|UniProtKB:Q8TDQ7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174;
CC Evidence={ECO:0000250|UniProtKB:Q8TDQ7};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine-6-
CC phosphate (GlcNAc6P). {ECO:0000250|UniProtKB:Q8TDQ7}.
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:Q8TDQ7}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. {ECO:0000305}.
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DR EMBL; BC118295; AAI18296.1; -; mRNA.
DR RefSeq; NP_001068824.1; NM_001075356.1.
DR AlphaFoldDB; Q17QL1; -.
DR SMR; Q17QL1; -.
DR STRING; 9913.ENSBTAP00000000357; -.
DR PaxDb; Q17QL1; -.
DR PRIDE; Q17QL1; -.
DR GeneID; 508383; -.
DR KEGG; bta:508383; -.
DR CTD; 132789; -.
DR eggNOG; KOG3148; Eukaryota.
DR HOGENOM; CLU_049611_0_1_1; -.
DR InParanoid; Q17QL1; -.
DR OrthoDB; 1425290at2759; -.
DR TreeFam; TF300841; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
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 Carbohydrate metabolism; Coiled coil; Cytoplasm; Hydrolase; Isomerase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..276
FT /note="Glucosamine-6-phosphate isomerase 2"
FT /id="PRO_0000343204"
FT COILED 106..130
FT /evidence="ECO:0000255"
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 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88958"
SQ SEQUENCE 276 AA; 31165 MW; 4916140CD1431E12 CRC64;
MRLVILDNYD LASEWAAKYI CNRIIQFRPG QDRYFTLGLP TGSTPLGCYK KLIEYHKNGD
LSFKYVKTFN MDEYVGLPRN HPESYHSYMW NNFFKHIDID PNNAHILDGN ATDLQAECDA
FEKKIKEAGG IDLFVGGIGP DGHIAFNEPG SSLVSRTRLK TLAMDTILAN AKYFDGDLSK
VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTIFVCD
EDATLELRVK TVKYFKGLMH VHNKLVDPLY SMKEGN
