ID   GFA1_ENCCU              Reviewed;         699 AA.
AC   Q8SRI2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            Short=GFAT;
DE            EC=2.6.1.16;
DE   AltName: Full=D-fructose-6-phosphate amidotransferase;
DE   AltName: Full=Hexosephosphate aminotransferase;
GN   Name=GFA1; OrderedLocusNames=ECU07_1280;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC       supplies the amino sugars of asparagine-linked oligosaccharides of
CC       glycoproteins). {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   -!- 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.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
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DR   EMBL; AL590447; CAD25661.1; -; Genomic_DNA.
DR   RefSeq; NP_586057.1; NM_001041679.1.
DR   AlphaFoldDB; Q8SRI2; -.
DR   SMR; Q8SRI2; -.
DR   STRING; 284813.Q8SRI2; -.
DR   GeneID; 859487; -.
DR   KEGG; ecu:ECU07_1280; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_1280; -.
DR   HOGENOM; CLU_012520_5_2_1; -.
DR   InParanoid; Q8SRI2; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 262871at2759; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   Aminotransferase; Glutamine amidotransferase; Reference proteome; Repeat;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..699
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000381745"
FT   DOMAIN          2..303
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          377..516
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          544..689
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
SQ   SEQUENCE   699 AA;  77544 MW;  225F2F74C19C6B36 CRC64;
     MCGIFGYANF SKERSKDEIA NIMINGLKRI EYRGYDSAGF CITDNTDRNF ARIRAVGKVN
     SLYEIKNSQT SVDLTRKVLN HVSIAHTRWA THGQPSIENS HPLSSDENNS FLVVHNGIIT
     NYKDLKVYLK KKGFTFESDT DTECAAKLAL YFYREMERKK EETDFVAIVK NVVKHCEGAF
     AFVFASSLFP NELVTVRKSS PVLIGLKPSG KMSFDFFGVN YGDPADDTPT SLLDSPLAFS
     KSDRHGFDQN IDMMTRDVQD CTLHAHNKEP LEVFVASDAS ALIEHTRKVI FLEDNDIVHI
     SNGNISIHRM HSKAKESGPE IREVKTIETE LAAIMKGNYD HYMIKEINEQ EESVVNTMRG
     RINFESLTVS LGGLKDHVSG IRKSQRIIFV ACGTSYHASL ANRALLEELL EIPVSVEIAS
     DFLDRAPPIM RSDCVFFVSQ SGETADSVMA LRYCMSMGAL CVGITNTVGS TISRETACGV
     HINAGPEIGV ASTKAYTSQY IALVLVALQL SDQNLVKQAR RREIMEGLKN ISSQINRVLE
     LSTSVKSLAN GPMKDDASLL LIGRGYQYPT CMEGALKIKE ITYIHAEGLA AGELKHGPIA
     LVDDKLRIIF IATKDLLYDK TRNAMEQIFA RGGRPIVICT EDISGDYAEY DTFVVPKTVD
     CLQGILTVIP LQLLSYHLAV AKGYNADFPR NLAKSVTVE