ID A0A286ZUW0_PIG Unreviewed; 704 AA.
AC A0A286ZUW0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN Name=GFPT1 {ECO:0000313|Ensembl:ENSSSCP00000035420.2,
GN ECO:0000313|VGNC:VGNC:88426};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000035420.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000035420.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000035420.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000035420.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001031};
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DR AlphaFoldDB; A0A286ZUW0; -.
DR SMR; A0A286ZUW0; -.
DR STRING; 9823.ENSSSCP00000035420; -.
DR Ensembl; ENSSSCT00000053007.3; ENSSSCP00000035420.2; ENSSSCG00000008339.5.
DR VGNC; VGNC:88426; GFPT1.
DR GeneTree; ENSGT00940000158488; -.
DR InParanoid; A0A286ZUW0; -.
DR Reactome; R-SSC-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000008339; Expressed in duodenum and 45 other cell types or tissues.
DR ExpressionAtlas; A0A286ZUW0; baseline and differential.
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:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF12; GLUTAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMERIZING] 1; 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZUW0};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..305
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 377..516
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 548..690
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 704 AA; 79292 MW; A2B82BD43EEAD7EA CRC64;
FAGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GVDGGNDKDW EANACKIQLI
KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPNPVNSHPQ RSDKNNEFIV
IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNRESQDTSF TTLVERVIQQ
LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSKFTRW
GSQGERGKDK KGSCNLSRVD STTCLFPVEE KAVEYYFASD ASAVIEHTNR VIFLEDDDVA
AVVDGRLSIH RIKRTAGDHP GRAVQTLQME LQQIMKGNFS SFMQKEIFEQ PESVVNTMRG
RVNFDDYTVN LGGLKDHIKE IQRCRRLILI ACGTSYHAGV ATRQVLEELT ELPVMVELAS
DFLDRNTPVF RDDVCFFISQ SGETADTLMG LRYCKERGAL TVGITNTVGS SISRETDCGV
HINAGPEIGV ASTKAYTSQF VSLVMFALMM CDDRISMQER RKEIMLGLKR LPDLIKEVLS
MDDEIQKLAT ELYHQKSVLI MGRGYHYATC LEGALKIKEI TYMHSEGILA GELKHGPLAL
VDKLMPVIMI IMRDHTYAKC QNALQQVVAR QGRPVVICDK EDTETIKNTK RTIKVPHSVD
CLQGILSVIP LQLLAFHLAV LRGYDVSDGP LGKSWAFDSF HLSF
//