ID D7BS33_STRBB Unreviewed; 615 AA.
AC D7BS33;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
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:ADI09351.1};
GN OrderedLocusNames=SBI_06231 {ECO:0000313|EMBL:ADI09351.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI09351.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI09351.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI09351.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI09351.1; -; Genomic_DNA.
DR RefSeq; WP_014178803.1; NC_016582.1.
DR AlphaFoldDB; D7BS33; -.
DR STRING; 749414.SBI_06231; -.
DR KEGG; sbh:SBI_06231; -.
DR PATRIC; fig|749414.3.peg.6423; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_11; -.
DR Proteomes; UP000000377; 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:UP000000377};
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..605
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 610
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 615 AA; 65845 MW; 6F19E3787D300E85 CRC64;
MCGIVGYVGG QSALDVVLAG LKRLEYRGYD SAGVAVLADG GLAAAKKAGK LANLEKELAD
RPLPSGGTGI GHTRWATHGG PTDANAHPHL DNAGRVSVVH NGIIENFAAL RAELAERGHQ
LASETDTEVV AHLLAESFSS CGDLAESMRQ VCRRLEGAFT LVAVHADAPD VVVGARRNSP
LVVGVGEDEA FLASDVAAFI AHTREAIELG QDQVVEARRD GVTVTDFDGA PADVRAYHVD
WDASAAEKGG YDYFMLKEIA EQPKAVADTL LGRIDVAGNL TLDEVRIPAS VLREVDKVVI
VACGTAYHAG MIAKYAIEHW TRIPCETELA SEFRYRDPIL DPRTLVIAIS QSGETMDTLM
ALRHAREQGA KVLAICNTNG STIPRESDAV LYTHAGPEVA VASTKAFLTQ LVACYLVALY
LGQVRGTKWG DEIQSVIREL SEIGTQVEQV LETMEPVREL ARTLANKNTV LFLGRHVGFP
VALEGALKLK ELAYMHAEGF AAGELKHGPI ALIEEDLPVV VVVPSPRGRS VLHDKIVSNI
QEIRARGART IVIAERGDET VAPYADHLIE IPATPTLLQP LVATVPLQVF ACELATARGN
EVDQPRNLAK SVTVE
//
