ID A0A0P0N5I0_9CREN Unreviewed; 613 AA.
AC A0A0P0N5I0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN ORFNames=Pdsh_04930 {ECO:0000313|EMBL:OWJ55039.1}, Pyrde_1696
GN {ECO:0000313|EMBL:ALL01739.1};
OS Pyrodictium delaneyi.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL01739.1, ECO:0000313|Proteomes:UP000058613};
RN [1] {ECO:0000313|EMBL:ALL01739.1, ECO:0000313|Proteomes:UP000058613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Su06 {ECO:0000313|EMBL:ALL01739.1,
RC ECO:0000313|Proteomes:UP000058613};
RA Jung J.-H., Lin J., Holden J.F., Park C.-S.;
RT "Complete genome sequence of hyperthermophilic archaeon Pyrodictium
RT delaneyi Su06.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OWJ55039.1, ECO:0000313|Proteomes:UP000196694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hulk {ECO:0000313|EMBL:OWJ55039.1,
RC ECO:0000313|Proteomes:UP000196694};
RA Demey L.M., Miller C., Manzella M., Reguera G., Kashefi K.;
RT "The draft genome of the hyperthermophilic archaeon 'Pyrodictium delaneyi
RT strain Hulk', an iron and nitrate reducer, reveals the capacity for sulfate
RT reduction.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000256|HAMAP-Rule:MF_00164}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
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DR EMBL; CP013011; ALL01739.1; -; Genomic_DNA.
DR EMBL; NCQP01000002; OWJ55039.1; -; Genomic_DNA.
DR RefSeq; WP_055409930.1; NZ_NCQP01000002.1.
DR AlphaFoldDB; A0A0P0N5I0; -.
DR STRING; 1273541.Pyrde_1696; -.
DR GeneID; 26100036; -.
DR KEGG; pdl:Pyrde_1696; -.
DR PATRIC; fig|1273541.4.peg.1807; -.
DR OrthoDB; 372195at2157; -.
DR Proteomes; UP000058613; Chromosome.
DR Proteomes; UP000196694; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 HAMAP; MF_00164; GlmS; 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 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..225
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 288..427
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 461..603
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 608
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 613 AA; 67750 MW; 8E3FA055D722AEA1 CRC64;
MCGIVGIVAD PDIIGNVAPI LVQGLKRLEY RGYDSAGFAL IECSSNKLLI FKDKGRIDKV
VEEYSVHKYC AVCGIAHTRW ATHGEPNTVN AHPHVDCRNE IAVVHNGIIK NFAELRQLLE
ERGHKFKSET DTEVIAHLLE EYLENGDSMW EAFKKLVKVI EGAYAIAVVY AYEPNRIYFA
RKVSPLVIGL GEGFNMIASD IPSMLQYTKR FVALNDGEYG YIEPYRLYLE KSGTPVEWHH
RVMTVTWSIE DAEKGGYPHY MLKEIMEQPR VLYETYTGLM SSRELEKAAE ILASADHIFV
TGAGTSYHAG LVFAYFMARI ARRPVITFIS SEYLAYRSLD HSNSALVAIS QSGETIDTLQ
AVRSFKSSGG RVVAVSNVVG STIPRESDTT VYTRAGPEIG VAATKTFLTQ VLALTSIALA
LAVHTGSLTK AEYTEAMREL RNASHAASSG IDRSIRLVEL LASSLRSKNN IYVLGRGLGV
PLAYEAALKI KEVSYIHAEA YPAGESKHGP IALVEEEFPV IFVGVPPEDE LLEKLQSNVM
EMKARGASTI VIGTSSYREL EGVDFYIDVG NYSEILAPYA VVPPFQLLAY KLAVMLNRDP
DKPRNLAKTV TVE
//
