ID A0A1B1YSE3_9GAMM Unreviewed; 610 AA.
AC A0A1B1YSE3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, 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=PG2T_06060 {ECO:0000313|EMBL:ANX03800.1};
OS Immundisolibacter cernigliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Immundisolibacterales;
OC Immundisolibacteraceae; Immundisolibacter.
OX NCBI_TaxID=1810504 {ECO:0000313|EMBL:ANX03800.1, ECO:0000313|Proteomes:UP000092952};
RN [1] {ECO:0000313|Proteomes:UP000092952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR3.2 {ECO:0000313|Proteomes:UP000092952};
RA Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.;
RT "Complete genome sequence of Solimmundus cernigliae, representing a novel
RT lineage of polycyclic aromatic hydrocarbon degraders within the
RT Gammaproteobacteria.";
RL Submitted (MAR-2016) 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; CP014671; ANX03800.1; -; Genomic_DNA.
DR RefSeq; WP_068803464.1; NZ_CP014671.1.
DR AlphaFoldDB; A0A1B1YSE3; -.
DR STRING; 1810504.PG2T_06060; -.
DR KEGG; gbi:PG2T_06060; -.
DR InParanoid; A0A1B1YSE3; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000092952; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000092952};
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..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 287..427
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 459..600
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 605
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 610 AA; 65514 MW; D3811B660CF99117 CRC64;
MCGIVCGIAR HDIVPDLLEG LRRLEYRGYD SAGIAVRLDD GRLHRVRALG KVMELARRLA
AEPVTSHAGI GHTRWATHGA PSEANAHPHI SRGELAVVHN GIIENHAALR EAQRAAGFEF
TSQTDTEVIG HQIRRHLDAG LDLFDAVRAA AAELHGAFAI GVLSGAEPDR LLAARRGSPL
VVGVAADAVY LASDAAALVP FTQDMVFLQD GDVAEVGIGL LRIVDAHGQP VQRPLRRSSL
SAAATERGAY RHYMQKEIFE QPQAIADTLD GRLGESRVLE AAFGTEAAAI FDRVRELRIV
ACGTSYHAGC VARYWFEALA GVPCQVEIAS EFRYRDSVVP ADALLVAISQ SGETADTLEA
LREARRRGYA HTLAICNVPE SSLTREADLK LMTHAGPEIG VASTKAFTTQ LVSLMLLVLA
LGRRHRLDAA TEASLVDELR RLPAAVQAVL ALDDTIAALA PDFADKHHAL FLGRGVHYPV
ALEGALKLKE ISYIHAEAYA AGELKHGPLA LVDADMPVVA VAPSDPLLEK LKSNMEEVRA
RGGRLLVFAD AGAGFDDTDI ALVEVPTDTI DHLVPVLFTV PLQLLAYHVA LIRGTDVDQP
RNLAKSVTVE
//
