ID A0A0B8T1S4_9SPHI Unreviewed; 613 AA.
AC A0A0B8T1S4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=DI53_1110 {ECO:0000313|EMBL:KGE15112.1};
OS Sphingobacterium deserti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE15112.1, ECO:0000313|Proteomes:UP000031802};
RN [1] {ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA Zhang W.;
RT "Whole-Genome optical mapping and complete genome sequence of
RT Sphingobacterium deserti sp. nov., a new spaces isolated from desert in the
RT west of China.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE15112.1, ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX PubMed=25830331;
RA Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA Zhang W., Lin M.;
RT "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT Sphingobacterium deserti sp. nov., a New Species Isolated from the Western
RT Desert of China.";
RL PLoS ONE 10:E0122254-E0122254(2015).
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:KGE15112.1}.
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DR EMBL; JJMU01000019; KGE15112.1; -; Genomic_DNA.
DR RefSeq; WP_037496395.1; NZ_JJMU01000019.1.
DR AlphaFoldDB; A0A0B8T1S4; -.
DR STRING; 1229276.DI53_1110; -.
DR PATRIC; fig|1229276.3.peg.1148; -.
DR eggNOG; COG0449; Bacteria.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000031802; 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 Reference proteome {ECO:0000313|Proteomes:UP000031802};
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 289..428
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 462..603
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 608
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 613 AA; 67240 MW; 631CB65BC1E67BAC CRC64;
MCGIVGYVGS NLAYPILIDG LKKLEYRGYD SAGVALHTGK ALEVYKKEGK VAALEDYVYG
KNIQATVGIG HTRWATHGVP SDRNAHPHYS NSGNIAMIHN GIIENYAQLK SELVQKGYTF
ASDTDSEVLL NFIEDIKINN DCSLEEAVRI ALKRVVGAYV ILLIDQDLPD TIIAARKGSP
LVIGIGNNAH YLGSDASPML AYTKEVVYIN DYELAIVRPD ELILKNLGNE RITPFVQKLD
IELAAIEKGG YDHFMLKEIF EQPQTIFDSL RGRLDAEHQH ITLSGVDKIK EKLIHANRVI
IVACGTSWHA GLLAEYVIEE LCRINVEVEY ASEFRYRNPI ITDKDVIIAV SQSGETADTL
VAIENAKKQG ATIFGLVNVV GSSIARMSDA GAYTHAGPEI GVASTKAFTA QLAVLYLIAL
KVAYEKQTID KTLFNKLLGD LAKVPQYVQD ILEEQDAAIK EIANKYADAR DFLYLGRGFN
FPIALEGALK LKEISYIHAE GYPAAEMKHG PIALVDENLP VVFVATKDSY HEKIVSNIQE
IKARKGQVIA VVSQGDNVVA GLADDVMVVP QIHEILAPIL SVVPLQLLSY YIGINRGLDV
DKPRNLAKSV TVE
//
