ID GLMS_CHLTE Reviewed; 614 AA.
AC Q8KG38;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 121.
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=CT0130;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM71378.1; -; Genomic_DNA.
DR RefSeq; NP_661036.1; NC_002932.3.
DR RefSeq; WP_010931824.1; NC_002932.3.
DR AlphaFoldDB; Q8KG38; -.
DR SMR; Q8KG38; -.
DR STRING; 194439.CT0130; -.
DR EnsemblBacteria; AAM71378; AAM71378; CT0130.
DR KEGG; cte:CT0130; -.
DR PATRIC; fig|194439.7.peg.127; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_10; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000001007; 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; 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_0000135320"
FT DOMAIN 2..223
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 292..431
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; 67577 MW; A9B4195C3DC3F84F CRC64;
MCGIIGYIGR REAAPLLLNG LKRLEYRGYD SAGMAVLNGS MKMLKKKGSV SNLEELLNVS
GTVMLGATVG IAHTRWATHG DPSDRNAHPH MNVSGDIALI HNGIIENYSA LKQELMGEGY
VFESDTDSEV LVHLIDRIWK NDSALGLEGA VRQALRHVEG AYGICVVSSR EPDKIVVARK
GSPLVIGLGD GEFFIASDAA PIVEHTNKVV YLSDGEMAVV TRDSYTVKTI ENVEQQKRVT
ELDFSLEKIE KGGFEHFMLK EIFEQPEVMR DVMRGRVRVE EGRVHLGGIH DYLDRLKQAK
RIMICACGTS WHAGLIGEYL IEEFARIPVE VDYASEFRYR NPIVSSDDVV IVISQSGETA
DTLAALRLAK EKGAMVMGIC NVVGSTIPRE TLCGMYTHAG PEVGVASTKA FTAQVIVLFM
LAMALSKGRT ISQEEIKLNL RELAEVPDKV AWILEQNDAI KEIAVKLKDA RNALYLGRGY
NFPVALEGAL KLKEISYIHA EGYPAAEMKH GPIALIDEDM PVIVIATRDN TYAKILSNIE
EVRSRKGRVI AIASEGDREI ERLTEDVIYI PQASAAVLPL LTVIPLQLLS YHVATLRGCN
VDRPRNLAKS VTVE
//
