GLMS_PYRAB
ID GLMS_PYRAB Reviewed; 598 AA.
AC Q9V249; G8ZG60;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 125.
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=PYRAB02250;
GN ORFNames=PAB2201;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB49149.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69601.1; -; Genomic_DNA.
DR PIR; F75212; F75212.
DR RefSeq; WP_010867349.1; NC_000868.1.
DR AlphaFoldDB; Q9V249; -.
DR SMR; Q9V249; -.
DR STRING; 272844.PAB2201; -.
DR EnsemblBacteria; CAB49149; CAB49149; PAB2201.
DR GeneID; 1495114; -.
DR KEGG; pab:PAB2201; -.
DR PATRIC; fig|272844.11.peg.241; -.
DR eggNOG; arCOG00057; Archaea.
DR HOGENOM; CLU_012520_5_2_2; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 7487at2157; -.
DR PhylomeDB; Q9V249; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Repeat;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT CHAIN 2..598
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135428"
FT DOMAIN 2..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 280..420
FT /note="SIS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 449..588
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 593
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ SEQUENCE 598 AA; 65874 MW; ACFC93F2E21CEA3C CRC64;
MCGIIGYIGP RKASPIIVEG LKRLEYRGYD SAGIATSHEG RILIKKGAGK IDELAKRLNF
TDLPGNIGIG HTRWATHGIP NDTNAHPHTD CTGKIVVVHN GIIENFQELK EELLRQGHVF
RSDTDTEVIA HLIEENLRIT GNFEDAFRLS LLRLRGSFAL VVMFADDPER LYIARKDSPL
IIGIGNGEMF IASDIPAFLP YTRKAVFLDD GEYGVVSRNG FTVKDIITGK EKRKKVYEIQ
WTLEMAEKGG YDHFMLKEIF EQPRAVKDAI YGNLEEVPKI AGLLSKYDRI IITGMGTSYH
AALVGKYLIQ RFGKIPVLVE EASELRYEYE DILDNKTLLI AITQSGETAD TVAAMKLAKS
KGSKVIGIVN VVGSLATRIA DATLYTHAGP EIGVAATKTY TTQLTVLLLL SLELGKMNGV
DTTQVENTLP KLPELIDAGL KMNEKIKELA KSLNDRRDFF YIGRGISYPT ALEGALKIKE
IAYVHAEGLS AGELKHGPLA LIEEGVPVIG VAPSGKTFEK MLSNIEEAKA RGGFIITVGD
DLRLHQVSNV FIRLPKVPEE VSPITYIVPL QLLAYHLAVL KGHNPDRPRN LAKSVTVE
