ID H0K1W6_9PSEU Unreviewed; 620 AA.
AC H0K1W6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=SZMC14600_05152 {ECO:0000313|EMBL:EHK88467.1};
OS Saccharomonospora azurea SZMC 14600.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=1114959 {ECO:0000313|EMBL:EHK88467.1, ECO:0000313|Proteomes:UP000003647};
RN [1] {ECO:0000313|EMBL:EHK88467.1, ECO:0000313|Proteomes:UP000003647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZMC 14600 {ECO:0000313|EMBL:EHK88467.1,
RC ECO:0000313|Proteomes:UP000003647};
RA Csepregi K., Valasek A., Penzes A., Kiss E.I., Kerepesi I., Horvath B.,
RA Nagy I., Fekete C.;
RL Submitted (DEC-2011) 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:EHK88467.1}.
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DR EMBL; AHBX01000061; EHK88467.1; -; Genomic_DNA.
DR RefSeq; WP_005443355.1; NZ_AHBX01000061.1.
DR AlphaFoldDB; H0K1W6; -.
DR STRING; 1114959.SZMC14600_05152; -.
DR PATRIC; fig|1114959.3.peg.1008; -.
DR eggNOG; COG0449; Bacteria.
DR Proteomes; UP000003647; 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 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..226
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 293..432
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 465..610
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 615
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 620 AA; 66905 MW; 6E0C46FD46803D34 CRC64;
MCGIVGYVGH RQALDVVLGG LRRMEYRGYD SAGVAVLTDG KDLVVERKAG RLANLEAALD
TVGRDAFAGT AGMGHTRWAT HGAPVDRNSH PHRDSTGRVA VVHNGIIENF AALRSELEDA
GVELTSDTDT ETTAHLIARA YDHGDTAGDL PASVRAVCRR LEGAFTLVVT HADQPDLVVA
ARRSSPLVVG VGDGETFVAS DVAAFIEHTR EAVELGQDQL VVIDRDGYRV TDFHGEPAEG
KPFTVDWDLS AAEKGGHEYF MLKEIEEQPD ALANTLRGHF ESGRIVLDEQ RMSDQDLRDV
DKVFVVACGS AYHSGLVAKY AIEHWTRLPV EVELASEFRY RDPVLDRDTL VVAVSQSGET
ADTLEAVRHA REQKARVLAV CNTNGAQIPR ESDAVLYTHA GPEIGVASTK AFLAQVAANY
LVGLALAQAR GTKYPDEVAR EFAELEAMPS AVKSVLSTVD QVRDLGRRMS DSRAVLFLGR
HVGFPVALEG ALKLKELAYM HAEGFAAGEL KHGPIALIEE GLPVVVVMPS PKGRAVLHAK
MVSNISEIQA RGARTIVIAE EGDERVKPFA DELVEVPAVP TLLQPLVSTV PLQVLAAEIA
RSRGYDVDKP RNLAKSVTVE
//