ID   GFAT_MIMIV              Reviewed;         606 AA.
AC   Q7T6X6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Probable 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   OrderedLocusNames=MIMI_L619;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: Controls the flux of glucose into the hexosamine pathway.
CC       Most likely involved in regulating the availability of precursors for
CC       glycosylation of proteins (Potential). {ECO:0000305}.
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.
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DR   EMBL; AY653733; AAQ09584.2; -; Genomic_DNA.
DR   RefSeq; YP_003987136.1; NC_014649.1.
DR   SMR; Q7T6X6; -.
DR   MEROPS; C44.A08; -.
DR   PRIDE; Q7T6X6; -.
DR   GeneID; 9925259; -.
DR   KEGG; vg:9925259; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000001134; Genome.
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   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
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   3: Inferred from homology;
KW   Aminotransferase; Glutamine amidotransferase; Reference proteome; Repeat;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..606
FT                   /note="Probable glutamine--fructose-6-phosphate
FT                   aminotransferase [isomerizing]"
FT                   /id="PRO_0000135286"
FT   DOMAIN          2..224
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          282..427
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          458..596
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   606 AA;  68570 MW;  9C0644BDC1C80CFC CRC64;
     MCGISACLNH TNNSAMTSVV NALTKLQNRG YDSAGICTTS NGKFNFVKSV SDDTNNAIHY
     IKNNPLANHH CSIAIGHTRW ATHGEKTIEN AHPHFDASGR FSLIHNGIIE NYDQIKSMLV
     ESQNYQFYGQ TDTEVAVAYL SYLLSENKTW FDFNESLKGS WAIIALDKFN PEKLYFMRNG
     SPLIIGFNET NTKAMIVSEL SGFDSDISQY CIVGDNDYGY ITNNNDKYII KSQQHYQMIS
     MGKIVMDLTP SPYKHWTQRE IYDQPNAIHS LITERIVDSQ LFFPEFNTIN FTLVEHIVLL
     GCGTSYHAAQ IGRRYIREFR PNITVDVIDG ADFEETDIPK SRNTLLILLS QSGETKDLYR
     ALVIGKQHSL KTIGIINVEN SLIAREVDTV LYLRAGRENA VASTKSFTNQ VLMLFMLALK
     INLSLDNSQL DYYTMSLNNF PIEFKKIIDQ SVNEIPKLLE FFDNQTSCFI LGKFGLEWIA
     KEGSLKIKEI SYVHSEGYSS AALKHGPFAL LHQNIPVVLL ANDDSYFSKI ENANSEIRSR
     KAKVIFITNK LIDNHCTDYL IHINTKSPLF HLLCIVPLQL LAYHLALSKG INPDYPRNLA
     KVVTVE