ID C6S9N2_NEIML Unreviewed; 612 AA.
AC C6S9N2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
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:CBA08675.1};
GN OrderedLocusNames=NMO_1975 {ECO:0000313|EMBL:CBA08675.1};
OS Neisseria meningitidis (strain alpha14).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=662598 {ECO:0000313|EMBL:CBA08675.1, ECO:0000313|Proteomes:UP000002054};
RN [1] {ECO:0000313|EMBL:CBA08675.1, ECO:0000313|Proteomes:UP000002054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alpha14 {ECO:0000313|Proteomes:UP000002054};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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; AM889136; CBA08675.1; -; Genomic_DNA.
DR RefSeq; WP_002250460.1; NC_013016.1.
DR AlphaFoldDB; C6S9N2; -.
DR KEGG; nmi:NMO_1975; -.
DR HOGENOM; CLU_012520_5_2_4; -.
DR Proteomes; UP000002054; 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 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..428
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 461..602
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 607
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 612 AA; 66572 MW; 62B6BD21B8004034 CRC64;
MCGIVGAIRA HHNVVDFLTD GLKRLEYRGY DSSGIAVNTD GKIKRVRRVG RVQLMEDAAR
EKGISGGIGI GHTRWATHGG VTEPNAHPHI SGGMIAVVHN GIIENFESER KRLEGLGYRF
ESQTDTEVIA HSINHEYAQN GGRLFEAVQE AVKRFHGAYA IAVIAQDKPD ELVVARMGCP
LLVALGDDET FIASDVSAVI AFTRRVAYLE DGDIALLASD GIKRLTDKNG LPAERKVKVS
ELSLASLELG PYSHFMQKEI HEQPRAIADT AEVFLDGGFI PENFGKDAKS VFESIRSVKI
LACGTSYYAA LTAKYWLESI AKIPTDVEIA SEYRYRSVIA DPDQLVITIS QSGETLDTME
ALKYAKSLGH RHSLSICNVM ESALPRESSL VLYTRAGAEI GVASTKAFTT QLVALFGLAV
TLAKVRGLVS GEDEARYTEE LRQLPGSVQH ALNLEPQIAA WAQQFAKKTS ALFLGRGIHY
PIALEGALKL KEITYIHAEA YPAGELKHGP LALVDENMPV VVIAPNDSLL DKVKANMQEV
GARGGELFVF ADLDSNFNAT EGVHVIRAPR HVGELSPVVH TIPVQLLSYH TALARGTDVD
KPRNLAKSVT VE
//
