ID J7M1L7_STRP1 Unreviewed; 604 AA.
AC J7M1L7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 55.
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 ECO:0000313|EMBL:BAM30371.1};
GN ORFNames=M1GAS476_1041 {ECO:0000313|EMBL:BAM30371.1};
OS Streptococcus pyogenes M1 476.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1207470 {ECO:0000313|EMBL:BAM30371.1, ECO:0000313|Proteomes:UP000005248};
RN [1] {ECO:0000313|EMBL:BAM30371.1, ECO:0000313|Proteomes:UP000005248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=476 {ECO:0000313|Proteomes:UP000005248};
RX PubMed=22965090; DOI=10.1128/JB.01265-12;
RA Miyoshi-Akiyama T., Watanabe S., Kirikae T.;
RT "Complete Genome Sequence of Streptococcus pyogenes M1 476, Isolated from a
RT Patient with Streptococcal Toxic Shock Syndrome.";
RL J. Bacteriol. 194:5466-5466(2012).
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; AP012491; BAM30371.1; -; Genomic_DNA.
DR RefSeq; WP_011285557.1; NC_020540.2.
DR AlphaFoldDB; J7M1L7; -.
DR KEGG; spym:M1GAS476_1041; -.
DR PATRIC; fig|1207470.4.peg.1040; -.
DR HOGENOM; CLU_012520_7_1_9; -.
DR Proteomes; UP000005248; Chromosome 1.
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..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 284..423
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 456..594
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 599
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 604 AA; 65565 MW; 182F12E99AB3F77D CRC64;
MCGIVGVVGN RNATDILMQG LEKLEYRGYD SAGIFVANAN QTNLIKSVGR IADLRAKIGI
DVAGSTGIGH TRWATHGQST EDNAHPHTSQ TGRFVLVHNG VIENYLHIKT EFLAGHDFKG
QTDTEIAVHL IGKFVEEDKL SVLEAFKKSL SIIEGSYAFA LMDSQATDTI YVAKNKSPLL
IGLGEGYNMV CSDAMAMIRE TSEFMEIHDK ELVILTKDKV TVTDYDGKEL IRDSYTAELD
LSDIGKGTYP FYMLKEIDEQ PTVMRQLIST YADETGNVQV DPAIITSIQE ADRLYILAAG
TSYHAGFATK NMLEQLTDTP VELGVASEWG YHMPLLSKKP MFILLSQSGE TADSRQVLVK
ANAMGIPSLT VTNVPGSTLS REATYTMLIH AGPEIAVAST KAYTAQIAAL AFLAKAVGEA
NGKQEALDFN LVHELSLVAQ SIEATLSEKD LAAEKVQALL ATTRNAFYIG RGNDYYVAME
AALKLKEISY IQCEGFAAGE LKHGTISLIE EDTPVIALIS SSQLVASHTR GNIQEVAARG
AHVLTVVEEG LDREGDDIIV NKVHPFLAPI AMVIPTQLIA YYASLQRGLD VDKPRNLAKA
VTVE
//
