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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