ID M1SJP3_9PROT Unreviewed; 610 AA.
AC M1SJP3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=D521_1993 {ECO:0000313|EMBL:AGG34559.1};
OS beta proteobacterium CB.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=543913 {ECO:0000313|EMBL:AGG34559.1, ECO:0000313|Proteomes:UP000011764};
RN [1] {ECO:0000313|EMBL:AGG34559.1, ECO:0000313|Proteomes:UP000011764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB {ECO:0000313|EMBL:AGG34559.1,
RC ECO:0000313|Proteomes:UP000011764};
RX PubMed=23599288;
RA Hao Z., Li L., Liu J., Ren Y., Wang L., Bartlam M., Egli T., Wang Y.;
RT "Genome Sequence of a Freshwater Low-Nucleic-Acid-Content Bacterium,
RT Betaproteobacterium Strain CB.";
RL Genome Announc. 1:e0013513-13(2013).
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; CP004348; AGG34559.1; -; Genomic_DNA.
DR AlphaFoldDB; M1SJP3; -.
DR STRING; 543913.D521_1993; -.
DR KEGG; bprc:D521_1993; -.
DR PATRIC; fig|543913.3.peg.1969; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_4; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000011764; 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 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..222
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 278..426
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; 66424 MW; 90CA09FFEBBB9190 CRC64;
MCGIVGAASR KNIVEVLIEG LRRLEYRGYD SCGFAVINGD DAKHPIERAR TTARVSELAE
QGKDFHGTLG IAHTRWATHG KPDTQNAHPH ISDGLIAVVH NGIIENYESL RTELKSAGYV
FTSETDTEVI AHLIHQAYVS SKQVDLVASV RSVLPRLHGA YAIGVIAQDR PDILVGARVG
SPLVVALGEN ENFLASDALA LAGRAHSMMY LEEGDVAILK AESVEIIDQA GKTVQREQKS
MPAQADSVDL GPYQHYMQKE IFEQPRAIGD TLANIASFGP ELFNADPEQW KKFDQILILA
CGTSYYSACV AKYWLEDLAG IPTQVEIASE YRYRTTVPNP STLIVVVSQS GETADTLAAL
RHAQALGHQY TLAICNVASS AMVRETNWNF LTKAGTEIGV ASTKAFTTQL VALYLLAVSL
AKRAGKVSPE GEKELLRDLR HLPKALHAVL ALEPQIMAWS TAFAKCENAL FLGRGMHYPI
ALEGALKLKE ISYIHAEAYP AGELKHGPLA LVTEKMPVVT VAPKDDLLEK LKSNMQEVKA
RGGKLYVFAD QDTEITSSEG INVIRLPEHY GNLSPILHVV PLQLLAYHTA CALGTDVDKP
RNLAKSVTVE
//
