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Database: UniProt
Entry: A0A286ZUW0_PIG
LinkDB: A0A286ZUW0_PIG
Original site: A0A286ZUW0_PIG 
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
//
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