ID A0A2H5BAY6_9ACTN Unreviewed; 608 AA.
AC A0A2H5BAY6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CFP65_6906 {ECO:0000313|EMBL:AUG81530.1};
OS Kitasatospora sp. MMS16-BH015.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=2018025 {ECO:0000313|EMBL:AUG81530.1, ECO:0000313|Proteomes:UP000239175};
RN [1] {ECO:0000313|EMBL:AUG81530.1, ECO:0000313|Proteomes:UP000239175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS16-BH015 {ECO:0000313|EMBL:AUG81530.1,
RC ECO:0000313|Proteomes:UP000239175};
RA Kim S.B., Yun B.-R.;
RT "Genome sequence of Kitasatospora sp. MMS16-BH015.";
RL Submitted (NOV-2017) 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; CP025394; AUG81530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5BAY6; -.
DR KEGG; kit:CFP65_6906; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000239175; 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 ECO:0000313|EMBL:AUG81530.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239175};
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 288..427
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 459..598
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 603
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 608 AA; 65430 MW; F0658B2E33B7F65A CRC64;
MCGIVAYIGP KDATTFLLEG LQRLEYRGYD SAGVAVLGKT GGLKVCKVKG RVADLAAAVP
ARFKGTTGIG HTRWATHGEP SDANAHPHTD NSGRIAVVHN GIIENAEELR ARLTAEGVTF
TSETDTEVLA HLIAARAVEG VELEEAVRGA LGHVVGTYGI AVLDSAQPDR IVVARNGSPI
VLGIGEKEMF VASDIAALVR YTRQVVHLED GELATVRADG FRTITEDART VTRQPSTVDW
EVASYDTAGY EHYLLKEIHE QPGSVERTLS GRLDEKFATA HLGGLNLDAR ELREIRRVKI
LGCGSAYYAG EMGAQLIEEL ARIPAHSEPA SEFRYRNPVI ERDTLYVAVS QSGETYDTLA
AVQEIKRKGG RVLGVVNTVG SAIARECDGG IYLHAGPEIS VASTKAFTST VVAFALLALH
FGRINDLSPA DGRRIVSALK ALPGQIREIL AQEEEIAKLA AHYADSAGMM FIGRVRGYPV
AREGAQKLKE ISYVHAEAYP ASELKHGPLA LISPELPTVA LVPDDELLDK NLTTLGEIKA
RSGRILAVGH RVPDAKLADH AIVVPKSEPE LDPLLLNIPL QIFAYFAAIA LERDVDKPRN
LAKSVTVE
//
