GNPI1_BOVIN
ID GNPI1_BOVIN Reviewed; 289 AA.
AC A4FV08;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Glucosamine-6-phosphate isomerase 1;
DE EC=3.5.99.6 {ECO:0000269|PubMed:9774701};
DE AltName: Full=Glucosamine-6-phosphate deaminase 1;
DE Short=GNPDA 1;
DE Short=GlcN6P deaminase 1;
DE AltName: Full=Oscillin;
GN Name=GNPDA1;
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 lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-42, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=9774701; DOI=10.1016/s0167-4838(98)00141-1;
RA Lara-Lemus R., Calcagno M.L.;
RT "Glucosamine-6-phosphate deaminase from beef kidney is an allosteric system
RT of the V-type.";
RL Biochim. Biophys. Acta 1388:1-9(1998).
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 (PubMed:9774701). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P46926, ECO:0000250|UniProtKB:Q64422,
CC ECO:0000269|PubMed:9774701}.
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:0000269|PubMed:9774701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173;
CC Evidence={ECO:0000305|PubMed:9774701};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174;
CC Evidence={ECO:0000305|PubMed:9774701};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine-6-
CC phosphate (GlcNAc6P). {ECO:0000269|PubMed:9774701}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.65 mM for alpha-D-glucosamine 6-phosphate (in the absence of
CC GlcNAc6P);
CC KM=5.9 mM for beta-D-fructose 6-phosphate (in the presence of
CC GlcNAc6P) {ECO:0000269|PubMed:9774701};
CC KM=3.7 mM for NH4(+) (in the presence of GlcNAc6P)
CC {ECO:0000269|PubMed:9774701};
CC Note=kcat is 61.6 sec(-1) for conversion of alpha-D-glucosamine 6-
CC phosphate into beta-D-fructose 6-phosphate (in the presence of
CC GlcNAc6P). kcat is 0.37 sec(-1) for conversion of alpha-D-glucosamine
CC 6-phosphate into beta-D-fructose 6-phosphate (in the absence of
CC GlcNAc6P). kcat is 5.8 sec(-1) for conversion of beta-D-fructose 6-
CC phosphate into alpha-D-glucosamine 6-phosphate (in the presence of
CC GlcNAc6P).;
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:0000269|PubMed:9774701}.
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; BC123566; AAI23567.1; -; mRNA.
DR RefSeq; NP_001073756.2; NM_001080287.3.
DR AlphaFoldDB; A4FV08; -.
DR SMR; A4FV08; -.
DR STRING; 9913.ENSBTAP00000010347; -.
DR PaxDb; A4FV08; -.
DR PRIDE; A4FV08; -.
DR Ensembl; ENSBTAT00000010347; ENSBTAP00000010347; ENSBTAG00000007865.
DR GeneID; 522919; -.
DR KEGG; bta:522919; -.
DR CTD; 10007; -.
DR VEuPathDB; HostDB:ENSBTAG00000007865; -.
DR VGNC; VGNC:29476; GNPDA1.
DR eggNOG; KOG3148; Eukaryota.
DR GeneTree; ENSGT00390000014316; -.
DR HOGENOM; CLU_049611_0_1_1; -.
DR InParanoid; A4FV08; -.
DR OMA; FNEPCSS; -.
DR OrthoDB; 1425290at2759; -.
DR TreeFam; TF300841; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000007865; Expressed in corpus epididymis and 106 other tissues.
DR ExpressionAtlas; A4FV08; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IDA: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:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl.
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 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..289
FT /note="Glucosamine-6-phosphate isomerase 1"
FT /id="PRO_0000343209"
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; 32580 MW; 297DBD6AB27ED6B0 CRC64;
MKLIILDHYS QASEWAAKYI RNRIIQFNPG PDKYFTLGLP TGSTPLGCYK KLIEYYKNGD
LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH PENTHILDGN AADLQAECDA
FEEKIKAAGG IELFVGGIGP DGHIAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGDLAK
VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD
EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKEIEKS QSSKKPYSD
