ID A0A1A9GJG0_9ACTN Unreviewed; 614 AA.
AC A0A1A9GJG0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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_2 {ECO:0000313|EMBL:ANH38394.1};
GN Synonyms=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN ORFNames=I601_1965 {ECO:0000313|EMBL:ANH38394.1};
OS Nocardioides dokdonensis FR1436.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH38394.1, ECO:0000313|Proteomes:UP000077868};
RN [1] {ECO:0000313|EMBL:ANH38394.1, ECO:0000313|Proteomes:UP000077868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FR1436 {ECO:0000313|EMBL:ANH38394.1,
RC ECO:0000313|Proteomes:UP000077868};
RA Kwon S.-K., Kim K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT dokdonensis FR1436.";
RL Submitted (MAR-2016) 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; CP015079; ANH38394.1; -; Genomic_DNA.
DR RefSeq; WP_068108794.1; NZ_CP015079.1.
DR AlphaFoldDB; A0A1A9GJG0; -.
DR STRING; 1300347.I601_1965; -.
DR KEGG; ndk:I601_1965; -.
DR PATRIC; fig|1300347.3.peg.1965; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000077868; 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 Reference proteome {ECO:0000313|Proteomes:UP000077868};
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..220
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 460..604
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 609
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 614 AA; 67025 MW; 015EC26473ADBB8E CRC64;
MCGIVGYVGQ RPSELVVVEG LRRMEYRGYD SAGIAVVADG VLATRKKAGK LANLEQVVDQ
DPLPPSTIGI GHTRWATHGA PNDVNAHPHL GSTGRVAMVH NGIIENFDDL RARLEADGHQ
LHSQTDTEVV AHLLELQVVS GVDLTTAMQR VCSRLEGAFT LVAIEAEDPT RVVAARRNSP
LVVGLGEGEN FLGSDVAAFI EHTREALELD QDQVVTITAD DVSVTGFDGT PTQGRQYHVD
WDLSAAEKDG HDWFMRKEIF EQPRAVADSL LGRRTREGAL HLDEMRLSDQ ELRDVDKIII
IAAGTSFYAG MVAKYAIEHW CRIPVEVELS SEFRYRDPIL DYSTLVVAIS QSGETADTLQ
AIRHARTQRS KVLAICNTNG STIPRESDAV IYTHAGPEIG VASTKGFLTQ LVACYLLALY
LAQVKGTRFG DEIAEVVSQL EEMPAHIETV LSRAEQVYEL AREHVDTRAV LFLGRHAGYP
VALEGALKLK ELAYIHAEGF AAGELKHGPI ALIEQDLPVW CVVPPRGRDQ LHGKMLSGIQ
EVRARGARTI CLAEDGDESI ASYADVLVRL PQVPVLLQPL VAVVPLQLFA CELATAMGHD
VDQPRNLAKS VTVE
//
