ID F2Y1G4_9PHYC Unreviewed; 594 AA.
AC F2Y1G4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=162322568 {ECO:0000313|EMBL:ADX05956.1};
OS Organic Lake phycodnavirus 1.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; environmental samples.
OX NCBI_TaxID=938081 {ECO:0000313|EMBL:ADX05956.1};
RN [1] {ECO:0000313|EMBL:ADX05956.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21444812; DOI=10.1073/pnas.1018221108;
RA Yau S., Lauro F.M., DeMaere M.Z., Brown M.V., Thomas T., Raftery M.J.,
RA Andrews-Pfannkoch C., Lewis M., Hoffman J.M., Gibson J.A., Cavicchioli R.;
RT "Virophage control of antarctic algal host-virus dynamics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6163-6168(2011).
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; HQ704802; ADX05956.1; -; Genomic_DNA.
DR MEROPS; C44.A08; -.
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:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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; 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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 283..420
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 447..584
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 594 AA; 67804 MW; 6B62B26BC53595C5 CRC64;
MCGIIACMGK DASTYIINGL KQLQNRGYDS AGISLMYQGQ WTIRKYASHD SIQRLSNIVY
PPSTNGIGHT RWATHGAKTQ QNSHPHQSYN GVFTLVHNGI IENYKILKDF LMKQGCVFYS
QTDSEVIVNL LEYYYTKDYN VINAIQCATQ KMEGTWGLCI QCLNEDNTLY CLRRGSPLLI
SNNDDFALVS SEYSGFCGIM NHYIELNPND ICKIEYVKDK IRMTTKHNYV LNEIHKEICS
YTYEPYMNWT QKEIYEQPET IENVTNHGSR YHSDGTIHLG GLNKDLLKNI EHIILLGCGT
SYFSACIGCK YMKTWCDFTS VQCFDGGEFT TYDIPKGKCA FLFVSQSGET KDLHKCIELL
QDHIKIGVIN KVDSIIAREV DFGCYLNAGR EVGVASTKSF VSQVVLLSMI ALWFAQLQKG
LRPNHKKVIH DLTHLSEHIN QALTIDVKPY LQMFSKGNCF ILGKDYDEYS SKEASLKIKE
LAYIHAEGYS TSSLKHGPFA LLDKDFPVIL LSPRDKHWQK NENAYEELKS RTNYILTITN
EELDREHSIM VPTNKTYQCI LNMIPLQLLA YELSLIRGYN PDKPRNLAKV VTVE
//
