ID I0ID38_PHYMF Unreviewed; 660 AA.
AC I0ID38;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:BAM03176.1};
GN OrderedLocusNames=PSMK_10170 {ECO:0000313|EMBL:BAM03176.1};
OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM03176.1, ECO:0000313|Proteomes:UP000007881};
RN [1] {ECO:0000313|EMBL:BAM03176.1, ECO:0000313|Proteomes:UP000007881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC {ECO:0000313|Proteomes:UP000007881};
RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL Submitted (FEB-2012) 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; AP012338; BAM03176.1; -; Genomic_DNA.
DR RefSeq; WP_014436395.1; NC_017080.1.
DR AlphaFoldDB; I0ID38; -.
DR STRING; 1142394.PSMK_10170; -.
DR GeneID; 80847486; -.
DR KEGG; phm:PSMK_10170; -.
DR PATRIC; fig|1142394.8.peg.1048; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_0; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000007881; 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:UP000007881};
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..251
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 338..477
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 509..650
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 655
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 660 AA; 70147 MW; 8FBFD07480478D98 CRC64;
MCGIVAYVGS KPCLPVLLEG LKRLEYRGYD SAGVAVLRPA HAGEAGPGVT TTAREVGRVM
NLENAIAPRT AGFAGTTGIA HTRWATHGKV TRANAHPHAG VTAEGLTLSV VHNGTIENYA
SLRTLLQNKG VTFASETDTE VIAKLIADRY DAEPEGGDQP SPGESLSGFI PSTRLERATK
AALRRVTGAY AVAVVCDANP HELVAARKGS PLIVGIADNG FVVASDGAAI VSHTTAAVTL
ADYQVVRLAA GPAGSTDAAG ERHAAAWADP LHTTTLDDEL LTAEVGELEM QLEEIELGGY
PHYMIKEIMG QPESLRTCFR GRVDTRDGRV VLGGLTGLSR ELVRAKRVAL IGQGTAFHAG
LIGEYLFEDL AKIPARAHYA SELRYRNPII EEGTVVVAVS QSGETADTLA AIAEAKDRGA
LALGAVNVVG SSIPRETDAG VYLRVGPEIG VASTKAFVGQ VAVLTMMALY MGKRRYLSQA
DLDGYLAELE RIPDHVAEIV QQSDHIKEAV EDVVTRDNWL FLGRGYNYPV ALEGALKLKE
ISYIHAEGMP AAEMKHGPIA LIDEGMPVVF VATGGSQYSK VISNIEEVKA RGGRVLAVAD
EGDTQIDRYA DHVFRVPPVS EPLQPLLTVV PLQLLAYHAA VLRGHDVDKP RNLAKSVTVE
//
