GLMS_BACTN
ID GLMS_BACTN Reviewed; 614 AA.
AC Q8AAB1;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; OrderedLocusNames=BT_0554;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
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DR EMBL; AE015928; AAO75661.1; -; Genomic_DNA.
DR RefSeq; NP_809467.1; NC_004663.1.
DR RefSeq; WP_008765067.1; NC_004663.1.
DR AlphaFoldDB; Q8AAB1; -.
DR SMR; Q8AAB1; -.
DR STRING; 226186.BT_0554; -.
DR PaxDb; Q8AAB1; -.
DR PRIDE; Q8AAB1; -.
DR EnsemblBacteria; AAO75661; AAO75661; BT_0554.
DR GeneID; 60926511; -.
DR KEGG; bth:BT_0554; -.
DR PATRIC; fig|226186.12.peg.554; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_10; -.
DR InParanoid; Q8AAB1; -.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Glutamine amidotransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT CHAIN 2..614
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135301"
FT DOMAIN 2..221
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 291..430
FT /note="SIS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 463..604
FT /note="SIS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT ACT_SITE 609
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ SEQUENCE 614 AA; 67594 MW; 310FBC0FA736C4BE CRC64;
MCGIVGYIGK RKAYPILIKG LKRLEYRGYD SAGVALISDN QQLNVYKTKG KVSELENFVT
QKDISGTVGI AHTRWATHGE PCSVNAHPHY SSSEKLALIH NGIIENYAVL KEKLQAKGYV
FKSSTDTEVL VQLIEYMKVT NRVDLLTAVQ LALNEVIGAY AIAILDKEHP EEIIAARKSS
PLVVGIGEDE FFLASDATPI VEYTDKVVYL EDGEIAVINR GKELKVVDLS NVEMTPEVKK
VELKLGQLEK GGYPHFMLKE IFEQPDCIHD CMRGRINVEA NNVVLSAVID YKEKLLNAKR
FIIVACGTSW HAGLIGKHLI ESFCRIPVEV EYASEFRYRD PVIDEHDVVI AISQSGETAD
TLAAVELAKS RGAFIYGICN AIGSSIPRAT HTGSYIHVGP EIGVASTKAF TGQVTVLTML
ALTLAREKGT IDETQYLNIV RELNSIPGKM KEVLKLNDKL AELSKTFTYA HNFIYLGRGY
SYPVALEGAL KLKEISYIHA EGYPAAEMKH GPIALIDAEM PVVVIATQNG LYEKVLSNIQ
EIKARKGKVI AFVTKGDTVI SKIADCSIEL PETIECLDPL ITTVPLQLLA YHIAVCKGMD
VDQPRNLAKS VTVE
