ID A0A0S6X7K9_9SPHN Unreviewed; 607 AA.
AC A0A0S6X7K9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 08-NOV-2023, entry version 34.
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=MBENS4_4334 {ECO:0000313|EMBL:GAM07338.1};
OS Novosphingobium sp. MBES04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM07338.1};
RN [1] {ECO:0000313|EMBL:GAM07338.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBES04 {ECO:0000313|EMBL:GAM07338.1};
RA Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A.,
RA Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.;
RT "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated from
RT Sunken Wood from Suruga Bay, Japan.";
RL Genome Announc. 3:e01373-14(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}.
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DR EMBL; DF850489; GAM07338.1; -; Genomic_DNA.
DR RefSeq; WP_039394671.1; NZ_DF850489.1.
DR AlphaFoldDB; A0A0S6X7K9; -.
DR STRING; 1206458.MBENS4_4334; -.
DR HOGENOM; CLU_012520_5_2_5; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000053513; 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..217
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 283..422
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 455..597
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 602
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 607 AA; 65078 MW; E1E890C9C8C35572 CRC64;
MCGIIGIVGK EEVADRLVDG LRRMEYRGYD SAGICTVDAG QLVRRRAEGK LANLVHELAG
NPAPGLIGIA HTRWATHGAP TAANAHPHAT DTLALVHNGI IENFRPLRES LESRGRTFES
QTDTEVVAHL VSEQVEAGLS PQDAVKAALP QLRGAFALAI AFREHPDMLI GARLGSPLVV
GYGEGETYLG SDALALAPLT QRITYLEEGD WVVITRDGAQ IFDAQNHPVE RAVVTSGASA
VAIEKGNYRH FMQKEIFEQP TVVAQTLSSY IRQVSQSVTL PQMDFDLGGI NRITIVACGT
SYYAGMVAKY WIETFARIPV DIDVASEFRY RDPVLEPGGL SLFISQSGET ADTLAALRHC
KAEGQTIAVV VNVPTSTMAR EADLLLPTYA GPEIGVASTK AFTCQLSVLA ALAARLAVLR
GRMDRDEEAQ VVTHLVEAPA RLNAALDHDD EIAQMAHLIA PARDVLYLGR GPDFPLALEG
ALKLKEISYI HAEGYASGEM KHGPIALIDE AVPVIVLAPS GPLFEKTVSN MQEVRARGGK
VVLISDAEGI AEAGEGCIAT IEMPRVHPLI APIVYAVPVQ LLAYHVACAK GTDVDQPRNL
AKSVTVE
//
