ID A0Q566_FRATN Unreviewed; 612 AA.
AC A0Q566;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 116.
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:ABK89381.1};
GN OrderedLocusNames=FTN_0485 {ECO:0000313|EMBL:ABK89381.1};
GN ORFNames=AW25_1544 {ECO:0000313|EMBL:AJI61639.1};
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614 {ECO:0000313|EMBL:ABK89381.1, ECO:0000313|Proteomes:UP000000762};
RN [1] {ECO:0000313|EMBL:ABK89381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=U112 {ECO:0000313|EMBL:ABK89381.1};
RA Brittnacher M., Rohmer L., Zhou Y., Abmayr S., D'Argenio D., Bovee D.,
RA Chang J., Chen J., Drees B., Ernst R., Fong C., Forsman M., Gallagher L.,
RA Gallis B., Gillett W., Goodlett D., Guina T., Guenthner D., Haugen E.,
RA Hayden H., Jacobs M., Kang A., Larson Freeman T., Levy R., Lim R.,
RA Manoil C., Olson M.V., Radey M., Shaffer S., Svensson K., Taylor G.,
RA Wasnick M., Kaul R., Miller S.I.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112 {ECO:0000313|Proteomes:UP000000762};
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
RN [3] {ECO:0000313|EMBL:AJI61639.1, ECO:0000313|Proteomes:UP000031872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112 {ECO:0000313|EMBL:AJI61639.1,
RC ECO:0000313|Proteomes:UP000031872};
RX PubMed=25931589;
RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O.,
RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S.,
RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.;
RT "Genome sequencing of 18 francisella strains to aid in assay development
RT and testing.";
RL Genome Announc. 3:0-0(2015).
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; CP000439; ABK89381.1; -; Genomic_DNA.
DR EMBL; CP009633; AJI61639.1; -; Genomic_DNA.
DR RefSeq; WP_003038501.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q566; -.
DR KEGG; ftn:FTN_0485; -.
DR KEGG; ftx:AW25_1544; -.
DR BioCyc; FTUL401614:G1G75-507-MONOMER; -.
DR Proteomes; UP000000762; Chromosome.
DR Proteomes; UP000031872; 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..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 460..602
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 607
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 612 AA; 67501 MW; B910E6AD2FC1A02B CRC64;
MCGIVGANSR RNVTNILIEG LKKLEYRGYD SAGLAIIDDK NNIDICKEVG KVIELEKSVH
NLANFKGDIG IAHTRWATHG KPSKNNSHPH ASESFCIVHN GVIENFAELK KVLINDGYKF
KSDTDTEVIA HLLQKEWRDN FSIVDNIKHI MTMLKGAYAL AIISQKFSDK IVAVRSGSPL
VIGVGIDENF ISSDALSLLP VTNKFSYLDE GDIAIISKDN VEVFDNNGAA KNLEVEEYNY
SSSSASKDGY KHYMLKEIYE QPEAVSNTIL ASLADGEISL DSFDKRAKEL FEKTKHICIV
ACGTSYNAGM TAKYWIEKYA KVPCSVEIAS EIRYRDNVVV DGSLFVSISQ SGETADTLES
LRKSKKQNYV GSMCICNVPN SSLVRESDIA FMTKAGVEIG VASTKAFTTQ LVALAIFTLV
IAKLKNSLTD QQIAKYTEEL KNIRALVMGA LKLDAEIDQI SEYFSDKEHT IFLGRGLYYP
IAIEGALKLK EISYIHAEAY PSGELKHGPL ALVDKNMPIV AVVPNDELLD KTLSNLQEVH
ARGGKLILFI DKAVKERVNF DNSIVLELDA GHDFSAPVVF TIPLQLLSYH VAIIKGTDVD
QPRNLAKSVT VE
//
