GFPT2_BOVIN
ID GFPT2_BOVIN Reviewed; 682 AA.
AC Q08DQ2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 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=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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; BC123624; AAI23625.1; -; mRNA.
DR RefSeq; NP_001070351.1; NM_001076883.1.
DR AlphaFoldDB; Q08DQ2; -.
DR SMR; Q08DQ2; -.
DR STRING; 9913.ENSBTAP00000002867; -.
DR MEROPS; C44.975; -.
DR PaxDb; Q08DQ2; -.
DR PRIDE; Q08DQ2; -.
DR GeneID; 530101; -.
DR KEGG; bta:530101; -.
DR CTD; 9945; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; Q08DQ2; -.
DR OrthoDB; 262871at2759; -.
DR TreeFam; TF300864; -.
DR SABIO-RK; Q08DQ2; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000009136; Unplaced.
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: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 2: Evidence at transcript 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_0000287357"
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; 77081 MW; 773A71B230746130 CRC64;
MCGIFAYMNY RVPRTRKEIF ETLIKGLQRL EYRGYDSAGV AIDGNNNEVK ERHIQLVKKR
GNVKALDEEL YKQDSMDLKV EFETHFGIAH TRWATHGVPS AVNSHPQRSD KGNEFVVIHN
GIITNYKDLR KFLESKGYEF ESETDTETIA KLIKYVFDNR ETEDITFSTL VERVIQQLEG
AFALVFKSIH YPGEAVATRR GSPLLIGVRS KYKLSTEQIP VLYRTRNIEN VKNICKTRMK
RLDSSTCLHA VGNKAVEFFF ASDASAIIEH TNRVIFLEDD DIAAVADGKL SIHRVKRLAS
DDPSRAIQTL QMELQQIMKG NFSAFMQKEI FEQPESVFNT MRGRVNFETN TVLLGGLKDH
LKEIRRCRRL IVIGCGTSYH AAVATRQVLE ELTELPVMVE LASDFLDRNT PVFRDDVCFF
ISQSGETADT LLALRYCKDR RALTVGVTNT VGSSISRETD CGVHINAGPE IGVASTKAYT
SQFISLVMFG LMMSEDRISL QNRRREIIHG LKSLPELIKE VLSLDEKIHD LALELYTQRS
LLVMGRGYNY ATCLEGALKI KEITYMHSEG ILAGELKHGP LALIDKQMPV IMVIMKDPCF
AKCQNALQQV TARQGRPIIL CSKDDTESSK FAYKTIELPH TVDCLQGILS VIPLQLLSFH
LAVLRGYDVD FPRNLAKSVT VE
