GLMS_CHLTR
ID GLMS_CHLTR Reviewed; 606 AA.
AC O84823;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 122.
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=CT_816;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC68413.1; -; Genomic_DNA.
DR PIR; B71467; B71467.
DR RefSeq; NP_220337.1; NC_000117.1.
DR RefSeq; WP_010725356.1; NC_000117.1.
DR AlphaFoldDB; O84823; -.
DR SMR; O84823; -.
DR STRING; 813.O172_04560; -.
DR EnsemblBacteria; AAC68413; AAC68413; CT_816.
DR GeneID; 884625; -.
DR KEGG; ctr:CT_816; -.
DR PATRIC; fig|272561.5.peg.901; -.
DR HOGENOM; CLU_012520_5_2_0; -.
DR InParanoid; O84823; -.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000000431; 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..606
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135321"
FT DOMAIN 2..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 278..424
FT /note="SIS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 448..596
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 601
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ SEQUENCE 606 AA; 67400 MW; 268123FFE5AFF6F0 CRC64;
MCGIFGYLGE KNAVPLVLEG LSKLEYRGYD SAGIATLVEG RLFVEKAVGP VSQLCSAVSS
DIHSQAAIGH TRWATHGEPS RFNAHPHVDM DASCALVHNG IIENFQKLKE ELEEQGVVFS
SDTDTEVIVQ LFARRYKETR DLIQSFSWTL KRLQGSFACA LMHQDHPEVL LCAAHESPLI
LGLGEDEVFI SSDIHAFLKY SGCTQTLASG ELAVLRIGKS IETYNFELAR IQKEVRCIDH
TEDSLDKKGF DYYMLKELYE QPEVFERILH LTCEENGFTE SFLKGFSLDE IQSLHIVACG
SSYHAGYLAK YVIESIASIP VYVETASEFR YRQPYIAEHS LAILISQSGE TADTLAALNE
FRKLSKARVL GICNVRESAL ASRVDHCLFI EAGLEVGVAS TKAFTAQLLL LILLGLRLAN
HRQVIAQEDL AQAIQGLKDL PNLTRLFLDS SIHDWRCRQI EETSFIFLGR RFMYPICMEA
ALKLKEIAYV EANAYPAGEM KHGPIALIRE GTPVIVYCGD RSVYTKTIGA IMEVKARKAY
VIALAPESNR DIAAVSDEQI YIPDSHDLAA PILFTIAGQI MAYTMALQRG TEVDRPRNLA
KSVTVE
