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Database: UniProt
Entry: Q8IJF3_PLAF7
LinkDB: Q8IJF3_PLAF7
Original site: Q8IJF3_PLAF7 
ID   Q8IJF3_PLAF7            Unreviewed;       829 AA.
AC   Q8IJF3;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   ORFNames=PF3D7_1025100 {ECO:0000313|EMBL:CZT98506.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT98506.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|EMBL:CZT98506.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
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   EMBL; LN999944; CZT98506.1; -; Genomic_DNA.
DR   RefSeq; XP_001347529.1; XM_001347493.1.
DR   AlphaFoldDB; Q8IJF3; -.
DR   SMR; Q8IJF3; -.
DR   STRING; 36329.Q8IJF3; -.
DR   PaxDb; 5833-PF10_0245; -.
DR   EnsemblProtists; CZT98506; CZT98506; PF3D7_1025100.
DR   GeneID; 810402; -.
DR   KEGG; pfa:PF3D7_1025100; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1025100; -.
DR   HOGENOM; CLU_012520_7_0_1; -.
DR   InParanoid; Q8IJF3; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 1705390at2759; -.
DR   PhylomeDB; Q8IJF3; -.
DR   Reactome; R-PFA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR   Proteomes; UP000001450; Chromosome 10.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; ISS:GeneDB.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006041; P:glucosamine metabolic process; ISS:GeneDB.
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: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; IPR005855; GFAT.
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   NCBIfam; TIGR01135; glmS; 1.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR   PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 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   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:CZT98506.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CZT98506.1}.
FT   DOMAIN          215..438
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          504..643
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          678..819
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   829 AA;  93659 MW;  5D533F2456126240 CRC64;
     MNFKFKTVIH NLKSKFKHEF VSDKKQLYFC NIMKNKYNVY ENIGFLNYGC SIKKYLFYNR
     KEDQDEEFKG SFKNGTMNGL KIWKYNNISS QKDTYNNISS QKDTYNNISS HKNTYNNISS
     HKNTYNNVSS HKNTYNNISS HKDTYNKYYY ALFNNNIFNQ KKLYIFFMAI CLALNKFLNT
     QEENNENNNS LKKKKKKKIM NSHFFGLSNE TASCCGIMAY MGNRDASKIL IDGIEILQNR
     GYDSCGMSTI SNKNVLKTTK YASNTTCDAI EKLKSNYLNS HKNDHIGIAH TRWATHGCKT
     DENAHPHVDY GERISIVHNG IIENYREIKT FLLKNNIPFK SNTDTEVVAN LIGYFLDKKQ
     SFQDAVLSAI TQLEGTWSFC IIHKNHPDEM ILASNGSPLH IGFKDDEIFI ASEHTALFMF
     TNEYISLKNG EILSISKDKI NDLKLLKKVE NIPEIAIQKT PHPYPHWTIK EIHEQSATLS
     KSLNNGGRFS SGDHLVKLGG LDPYIQDLNK IENLVLVGCG TSYYAALFAK YLMNYLNCFN
     TVQVMDPIDF NISVIPKEKE GVIFISQSGE TRDVIKACKL AEDLNVRKLS VVNSVGSTIA
     NMTGRGVYLN AGREVGVAST KCFTSEVSVL TLIALWFFQH KKNNQSSNKA TSLINSLHRL
     PLYTGVTIKS CENTCKTLSE KFKNTKSMLI IGNGLSYPIA QEGALKIKEL AYIHCEGFTG
     ASLKHGPYAL LGGEDNIPVI MLLFNDNTKN AMINTGEQIK SRGAHIVCLT DDENLVKHFA
     DDIILIPNNG ILTPLLAVIP LQMLAYYTSV NKGINPDKPR CLAKTVTVS
//
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