ID A0A4D6HF60_9EURY Unreviewed; 596 AA.
AC A0A4D6HF60;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ECO:0000313|EMBL:QCC51692.1};
GN ORFNames=DV733_10795 {ECO:0000313|EMBL:QCC51692.1};
OS Halapricum salinum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halapricum.
OX NCBI_TaxID=1457250 {ECO:0000313|EMBL:QCC51692.1, ECO:0000313|Proteomes:UP000296706};
RN [1] {ECO:0000313|EMBL:QCC51692.1, ECO:0000313|Proteomes:UP000296706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1105 {ECO:0000313|EMBL:QCC51692.1,
RC ECO:0000313|Proteomes:UP000296706};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
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; CP031310; QCC51692.1; -; Genomic_DNA.
DR RefSeq; WP_049994695.1; NZ_CP031310.1.
DR AlphaFoldDB; A0A4D6HF60; -.
DR STRING; 1457250.GCA_000755225_00735; -.
DR GeneID; 39848356; -.
DR KEGG; hsn:DV733_10795; -.
DR OrthoDB; 372195at2157; -.
DR Proteomes; UP000296706; Chromosome.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000296706};
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..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 281..419
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 445..586
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 591
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 596 AA; 63405 MW; FF7E9E0D5EA5B7E4 CRC64;
MCGIIGAVGR GSDTLDVLVH GLSKLEYRGY DSAGVALASD SIDVCKKAGE LDELRTALEG
RSVAGSVGIG HTRWSTHGPP TDANAHPHQD CSGDVAVVHN GIIENYQELR DELASAGHTF
RSDTDTEVVP HLVEDELRGG ADPEAAVRAA LSRLEGSYAV AVVIAGVERI FAARNDSPLV
LGISDDAYYL ASDVPAFRDH TDRVVYMNDG EFAALDAGGW TVTTLDGEPV EKPVDTVDWD
PEETGKSGYD HYMLKEIHEQ PRSLRQCLSE RVDELAGTVD IDDLADLNPR GVQFVACGTS
YHAALYGAEL FQQAGIPAQA FLASEYASSP PPIGDALVIG VTQSGETADT LSALREADRR
GARTLGVTNV VGSTVARECD HVFYIRAGPE IGVAATKTFA SQLAALNLLA LGMAGGDDTR
ELIGALRDLP GQVQEVLDES GARAVAETYL ESDAYFFIGR GLNFPVALEG ALKMKEITYK
HAEGFAAGEL KHGPLALVTD QTPVFAVVTG DGEQARKTIG NVKEVEARDA PVIAVTDGQS
DVERYADHVL RVPETHPRTA AVLANVQLQL VSYHTAAELG RSIDKPRNLA KSVTVE
//
