ID   GFPT2_RAT               Reviewed;         682 AA.
AC   Q4KMC4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2;
DE            EC=2.6.1.16 {ECO:0000250|UniProtKB:P82808};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase 2;
DE   AltName: Full=Glutamine:fructose-6-phosphate amidotransferase 2;
DE            Short=GFAT 2;
DE            Short=GFAT2;
DE   AltName: Full=Hexosephosphate aminotransferase 2;
GN   Name=Gfpt2;
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=Heart;
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]
RP   IDENTIFICATION BY 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.
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:0000250|UniProtKB:P82808};
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:P82808}.
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DR   EMBL; BC098630; AAH98630.1; -; mRNA.
DR   RefSeq; NP_001002819.2; NM_001002819.2.
DR   AlphaFoldDB; Q4KMC4; -.
DR   SMR; Q4KMC4; -.
DR   STRING; 10116.ENSRNOP00000003770; -.
DR   MEROPS; C44.975; -.
DR   jPOST; Q4KMC4; -.
DR   PaxDb; Q4KMC4; -.
DR   PRIDE; Q4KMC4; -.
DR   GeneID; 360518; -.
DR   KEGG; rno:360518; -.
DR   UCSC; RGD:1303097; rat.
DR   CTD; 9945; -.
DR   RGD; 1303097; Gfpt2.
DR   VEuPathDB; HostDB:ENSRNOG00000002810; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   HOGENOM; CLU_012520_5_2_1; -.
DR   InParanoid; Q4KMC4; -.
DR   OMA; TSYYSGC; -.
DR   OrthoDB; 262871at2759; -.
DR   PhylomeDB; Q4KMC4; -.
DR   Reactome; R-RNO-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR   SABIO-RK; Q4KMC4; -.
DR   UniPathway; UPA00113; UER00528.
DR   PRO; PR:Q4KMC4; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000002810; Expressed in esophagus and 20 other tissues.
DR   Genevisible; Q4KMC4; RN.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
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   Aminotransferase; Glutamine amidotransferase; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..682
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing] 2"
FT                   /id="PRO_0000135285"
FT   DOMAIN          2..288
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          360..499
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          531..672
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P14742"
FT   BINDING         377..378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06210"
FT   BINDING         422..424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06210"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06210"
FT   BINDING         578
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06210"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94808"
SQ   SEQUENCE   682 AA;  77010 MW;  E4B4B656999F667A CRC64;
     MCGIFAYMNY RVPKTRKEIF ETLIRGLQRL EYRGYDSAGV AIDGNNHEVK ERHIHLVKKK
     GKVKALDEEL YKQDSMDLKV EFETHFGIAH TRWATHGVPN VVNSHPQRSD KDNEFVVIHN
     GIITNYKDLR KFLESKGYEF ESETDTETIA KLIKYVFDNR ETEDITFSTL VERVIQQLEG
     AFALVFKSIH YPGEAVATRR GSPLLIGVRS KYKLSTEQIP VLYRTCTIEN VKNICKTRLK
     RLDSSTCLHA VGDKAVEFFF ASDASAIIEH TNRVIFLEDD DIAAVADGKL SIHRVKRSAS
     DDPSRAIQTL QMELQQIMKG NFSAFMQKEI FEQPESVFNT MRGRVNFETN TVLLGGLKDH
     LKEIRRCRRL IVIGCGTSYH AAVATRQVLE ELTELPVMVE LASDFLDRNT PVFRDDVCFF
     ISQSGETADT LLALRYCKDR GALTVGITNT VGSSISRETD CGVHINAGPE IGVASTKAYT
     SQFISLVMFG LMMSEDRISL QTRRQEIIRG LRSLPELIKE VLSLDEKIHD LALELYTQRS
     LLVMGRGYNY ATCLEGALKI KEITYMHSEG ILAGELKHGP LALVDKQMPV IMVIMKDPCF
     AKCQNALQQV TARQGRPIIL CSKDDTESSK FAYKTIELPH TVDCLQGILS VIPLQLLSFH
     LAVLRGYDVD FPRNLAKSVT VE