GFPT1_RAT
ID GFPT1_RAT Reviewed; 681 AA.
AC P82808; Q5XI08;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1;
DE EC=2.6.1.16 {ECO:0000269|PubMed:10898949};
DE AltName: Full=D-fructose-6-phosphate amidotransferase 1;
DE AltName: Full=Glutamine:fructose-6-phosphate amidotransferase 1;
DE Short=GFAT 1;
DE Short=GFAT1;
DE AltName: Full=Hexosephosphate aminotransferase 1;
GN Name=Gfpt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-14, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=Sprague-Dawley {ECO:0000269|PubMed:10898949};
RC TISSUE=Liver {ECO:0000269|PubMed:10898949};
RX PubMed=10898949; DOI=10.1006/abbi.2000.1895;
RA Huynh Q.K., Gulve E.A., Dian T.;
RT "Purification and characterization of glutamine:fructose 6-phosphate
RT amidotransferase from rat liver.";
RL Arch. Biochem. Biophys. 379:307-313(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Controls the flux of glucose into the hexosamine pathway.
CC Most likely involved in regulating the availability of precursors for
CC N- and O-linked glycosylation of proteins. Regulates the circadian
CC expression of clock genes ARNTL/BMAL1 and CRY1 (PubMed:10898949). Has a
CC role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc
CC and its effects on hyaluronan synthesis that occur during tissue
CC remodeling (By similarity). {ECO:0000250|UniProtKB:Q06210,
CC ECO:0000269|PubMed:10898949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC Evidence={ECO:0000269|PubMed:10898949};
CC -!- ACTIVITY REGULATION: Inhibited by 4,4'-dithiodipyridine.
CC {ECO:0000269|PubMed:10898949}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5.;
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:0000305|PubMed:10898949}.
CC -!- SUBUNIT: Homotetramer, may also exist as homodimers. {ECO:0000250}.
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DR EMBL; BC083889; AAH83889.1; -; mRNA.
DR RefSeq; NP_001005879.1; NM_001005879.1.
DR AlphaFoldDB; P82808; -.
DR SMR; P82808; -.
DR BioGRID; 255576; 3.
DR IntAct; P82808; 2.
DR STRING; 10116.ENSRNOP00000025070; -.
DR MEROPS; C44.970; -.
DR iPTMnet; P82808; -.
DR PhosphoSitePlus; P82808; -.
DR jPOST; P82808; -.
DR PaxDb; P82808; -.
DR PRIDE; P82808; -.
DR GeneID; 297417; -.
DR KEGG; rno:297417; -.
DR UCSC; RGD:1549703; rat.
DR CTD; 2673; -.
DR RGD; 1549703; Gfpt1.
DR VEuPathDB; HostDB:ENSRNOG00000018507; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; P82808; -.
DR BioCyc; MetaCyc:MON-13170; -.
DR Reactome; R-RNO-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; P82808; -.
DR UniPathway; UPA00113; UER00528.
DR PRO; PR:P82808; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000018507; Expressed in colon and 19 other tissues.
DR ExpressionAtlas; P82808; baseline and differential.
DR GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:RGD.
DR GO; GO:0006042; P:glucosamine biosynthetic process; IDA:RGD.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IMP:RGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0009744; P:response to sucrose; IEP:RGD.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IMP:RGD.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Biological rhythms; Direct protein sequencing; Glutamine amidotransferase;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10898949"
FT CHAIN 2..681
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing] 1"
FT /id="PRO_0000135282"
FT DOMAIN 2..287
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 359..498
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 530..671
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT REGION 295..662
FT /note="Isomerase"
FT /evidence="ECO:0000250"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P14742"
FT BINDING 376..377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 421..423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 426
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 577
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 681 AA; 76827 MW; 230D818CBC920249 CRC64;
MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GLDGGNDKDW EANACKIQLI
KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPSPVNSHPQ RSDKNNEFIV
IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNWESQDVSF TTLVERVIQQ
LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTGK DKKGSCGLSR
VDSTTCLFPV EEKAVEYYFA SDASAVIEHT NRVIFLEDDD VAAVVDGRLS IHRIKRTARD
HPGRAVQTLQ MELQQIMKGN FSSFMQKEIF EQPESVVNTM RGRVNFDDYT VNLGGLKDHI
KEIQRCRRLI LIACGTSYHA GMATRQVLEE LTELPVMVEL ASDFLDRNTP VFRDDVCFFI
SQSGETADTL MGLRYCKERG ALTVGITNTV GSSISRETDC GVHINAGPEI GVASTKAYTS
QFVSLVMFAL MMCDDRISMQ ERRKEIMLGL KRLPDLIKEV LSMDDEIQKL ATELYHQKSV
LIMGRGYHYA TCLEGALKIK EITYMHSEGI LAGELKHGPL ALVDKLMPVI MIIMRDHTYA
KCQNALQQVV ARQGRPVVIC DKEDTETIKN TKRTIKVPHS VDCLQGILSV IPLQLLAFHL
AVLRGYDVDF PRNLAKSVTV E
