ID A0A090W2L6_9FLAO Unreviewed; 615 AA.
AC A0A090W2L6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=JCM19302_3903 {ECO:0000313|EMBL:GAL69714.1}, JCM19538_2215
GN {ECO:0000313|EMBL:GAL87853.1};
OS Jejuia pallidilutea.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Jejuia.
OX NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL69714.1, ECO:0000313|Proteomes:UP000029646};
RN [1] {ECO:0000313|Proteomes:UP000029646, ECO:0000313|Proteomes:UP000030184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19302 {ECO:0000313|EMBL:GAL69714.1}, JCM 19538
RC {ECO:0000313|EMBL:GAL87853.1, ECO:0000313|Proteomes:UP000030184}, and
RC JCM19302 {ECO:0000313|Proteomes:UP000029646};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea Strain
RT 11shimoA1 and Pigmentation Mutants.";
RL Genome Announc. 2:e01236-14(2014).
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:GAL69714.1}.
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DR EMBL; BBNS01000002; GAL69714.1; -; Genomic_DNA.
DR EMBL; BBNY01000001; GAL87853.1; -; Genomic_DNA.
DR RefSeq; WP_042247777.1; NZ_BBNY01000001.1.
DR AlphaFoldDB; A0A090W2L6; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000029646; Unassembled WGS sequence.
DR Proteomes; UP000030184; 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..221
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 292..431
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 464..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; 67745 MW; 1CFF6DC517B5FDD2 CRC64;
MCGIVGYIGH RDAYPIVIEG LKRLEYRGYD SAGIALFDGT SLKVSKTKGK VSDLEACVET
QISKTGNLGI GHTRWATHGV PNDINSHPHV SNSGDLVIIH NGIIENYDSL KQELIKRGYT
FKSDTDTEVL INLIEEVKTK EGVKLGKAVQ IALNQVVGAY AIAVFDKNKP EEVVVARLGS
PLAVGIGDEE FFIASDASPF IEYTKNAIYL EDEEMAIIRF HKGIKVRKIK DDSLVDPYIQ
ELQLNLEQIE KGGYDHFMLK EIHEQPKAIT DTYRGRLLRD EAIIKMAGVE DNMKKFLNAN
RIIIVACGTS WHAGLVAEYI FEDLARIPVE VEYASEFRYR NPVITENDVL IAISQSGETA
DTLAAIKMAK SKGAFVFGVC NVVGSSIARE SDAGAYTHAG PEIGVASTKA FTTQITVLSL
IALRLARAKG TISSSDFRRY LLEMELIPEK VEKALEADAH IKEVSHIYKN AANFLYLGRG
YNFPVALEGA LKLKEISYIH AEGYPAAEMK HGPIALIDEN MPIVVIATKA EHYDKVVSNI
QEIKSRKGKI IGVITEGDTV VRELADHVIE VPETIEALSP LLTTIPLQLL SYHIAVMLGK
NVDQPRNLAK SVTVE
//
