ID A0A0F0KGH0_9MICO Unreviewed; 606 AA.
AC A0A0F0KGH0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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_3 {ECO:0000313|EMBL:KJL19963.1};
GN Synonyms=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN ORFNames=RL72_03009 {ECO:0000313|EMBL:KJL19963.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL19963.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL19963.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL19963.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL19963.1}.
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DR EMBL; JYIT01000083; KJL19963.1; -; Genomic_DNA.
DR RefSeq; WP_045251632.1; NZ_JYIT01000083.1.
DR AlphaFoldDB; A0A0F0KGH0; -.
DR PATRIC; fig|582680.7.peg.3067; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000033448; Unassembled WGS sequence.
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:UP000033448};
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..216
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 284..424
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 456..596
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 601
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 606 AA; 64824 MW; B380A13E554C509B CRC64;
MCGIVGYIGH QAAAPVLVEG LTRLEYRGYD SAGLAVLGAK GTTAIRRVGR VRELEAALPK
RLTGTVGIGH TRWATHGPAV EQNAHPQRSQ DGRISVVHNG IIDNAAALRA QLAQTGVEFS
SDTDTEVVAH LIAQSEAATL EEAVLAALGR ITGTYALAVL DERHPDRIVL ARSGSPLIIG
IGDKEMLVAS DVAALVRHTD RVVHLDDGEL ATVTATGFRT FDRGNSPTSS EPVEISVAAE
DLELSGYQHF MLKEIHEQPD AAAMVLRGRL DERFATARLD GLGLDPRELR GFRRIKILGC
GSAYYVGQLG AQLIEDLARI PADAEAASEF RYRQPIIESD TLYVAVSQSG ETADTAFAVE
EIKRKGGRVI GVVNVVGSTI ARTVDGGIYL HAGPEISVAS TKALTNMALS FALLALHLGR
LHDLSHADGQ RILRGLQRIP EQIREILDGS EAIAAVADDV AKAQSAFYVG RVRGFPVARE
GAQKLKEISY IHAEAYQTSE LKHGPLALID PDMPTVAVIP DDELTDRNLA AAEQILARKG
PLIAITHAGV DLGHLAARTI LVPKNEPELD PILLTIPTQL LAYHAAVLLG HDVDKPRNLA
KSVTVE
//
