ID F7XF16_SINMM Unreviewed; 629 AA.
AC F7XF16;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=nodM {ECO:0000313|EMBL:AEH82141.1};
GN Synonyms=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN OrderedLocusNames=SM11_pC1068 {ECO:0000313|EMBL:AEH82141.1};
OS Sinorhizobium meliloti (strain SM11).
OG Plasmid pSmeSM11c {ECO:0000313|EMBL:AEH82141.1,
OG ECO:0000313|Proteomes:UP000009045}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH82141.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH82141.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH82141.1,
RC ECO:0000313|Proteomes:UP000009045};
RC PLASMID=pSmeSM11c {ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(2011).
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; CP001831; AEH82141.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XF16; -.
DR KEGG; smx:SM11_pC1068; -.
DR PATRIC; fig|707241.3.peg.5019; -.
DR HOGENOM; CLU_012520_5_2_5; -.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000009045; Plasmid pSmeSM11c.
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 Plasmid {ECO:0000313|EMBL:AEH82141.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 22
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 23..238
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 302..443
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 477..619
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 23
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 624
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 629 AA; 68337 MW; AF24C15E813E46BB CRC64;
MKAGERSSVV LLLRLDYFGE NMCGIVGIVG NQPVSERLVE ALKRLEYRGY DSAGVATIDA
GTLQRRRAEG KLVNLESRLR EEPLAGTIGI AHTRWATHGA PTERNAHPHF TEGVAVVHNG
IIENFAELKD ELAAAGAEFQ TETDTEVVAH LLAKYRRDGL GRREAMHAML KRVKGAYALA
VLFEDDPSTI MAARNGPPLA IGHGNGEMFL GSDAIALAPF TNEITYLIDG DWAVIGKTGV
HIFDFDGNVV ERPRQISTAA AFLVDKGNHR HFMEKEIYEQ PEVIAHALGH YVNFIENRVV
PISDAIDFGK VPSLAISACG TAYLAGLIGK YWFERYARLP VEIDVASEFR YREIPLSPQS
AALFISQSGE TADTLASLRY CKEHGLKIGA VVNARESTIA RESDAVFPIL AGPEIGVAST
KAFTCQLAVL AALAVGAGRA RGTISGEEEQ ALVKSLAEMP RIMGQVLNSI QPKIESLSRE
LSKCHDVLYL GRGTSFPLAM EGALKLKEIS YIHAEGYAAG ELKHGPIALI DENMPVIVIA
PHDRFFDKTV SNMQEVAARG GRIILITDEK GAAASKLDTM HTIVLPEVDE IIAPMIFSLP
LQLLAYHTAV FMGTDVDQPR NLAKSVTVE
//