GLMS_METTH
ID GLMS_METTH Reviewed; 590 AA.
AC O26273;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 131.
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=MTH_171;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB84677.1; -; Genomic_DNA.
DR PIR; G69095; G69095.
DR RefSeq; WP_010875810.1; NC_000916.1.
DR AlphaFoldDB; O26273; -.
DR SMR; O26273; -.
DR STRING; 187420.MTH_171; -.
DR EnsemblBacteria; AAB84677; AAB84677; MTH_171.
DR GeneID; 1470132; -.
DR KEGG; mth:MTH_171; -.
DR PATRIC; fig|187420.15.peg.144; -.
DR HOGENOM; CLU_012520_5_2_2; -.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000005223; 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; 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..590
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135427"
FT DOMAIN 2..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 277..415
FT /note="SIS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 438..580
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 585
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ SEQUENCE 590 AA; 63995 MW; 7CE10DAB33103FE2 CRC64;
MCGIVACILK DGSAAPVLLE CVRRLEYRGY DSVGIATSDP MIRIKKDSGK IDEVDAELDL
ADLPGTMGIA HVRWATHGLP TAENAHPHTD CSGEIAVVHN GIIENYLEVK EELESEGHIF
RSETDTEVIP HLIEKYMDEG MDLEAATATA LRKLRGAYAI AAVSSREPGR IVGARKESPL
IVGVGEGEYF LASDVPAILN HTSRVIYLDD GEMVILDGDL RVTDMEGNTV EKEVHSIDWS
ADMAEKGGYD HFMLKEIHEE PSAVRDTLTE WDEVLGVVEE IGEVERICFV ACGTSYHASL
VGKYLFESLL GIPTDVILAS EFRYSAGALN DRTLAIFISQ SGETADTLNA LRAANSRAKT
LAIVNVLGSS ATREAQHVLY TRAGPEIGVA ATKTYVSQLT VIYMLVAAMG APELMDRLER
VPEFMERALE DEDGIKELAA TCSDVSDFFF IGRGFAYPTA LEGALKLKEI TYIHGEGYAA
GELKHGPLAL IDNGVPVVAI SPPGPCHDKT LSNVEEVRAR GARVIGVGSI SDESLRKEAD
DFIGLDPEVD DVISPLVYIV PLQLLSYHVS VERGLDPDKP KNLAKCVTVE
