ID R8AS90_PLESH Unreviewed; 610 AA.
AC R8AS90;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-NOV-2023, entry version 46.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN ORFNames=PLESHI_06844 {ECO:0000313|EMBL:EON89178.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89178.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON89178.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON89178.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000256|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:0000256|ARBA:ARBA00001031, ECO:0000256|HAMAP-
CC Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EON89178.1}.
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DR EMBL; AQQO01000043; EON89178.1; -; Genomic_DNA.
DR RefSeq; WP_010862993.1; NZ_KB944507.1.
DR AlphaFoldDB; R8AS90; -.
DR STRING; 703.SAMEA2665130_00007; -.
DR PATRIC; fig|1315976.3.peg.1342; -.
DR HOGENOM; CLU_012520_5_2_6; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000014012; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000014012};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 286..427
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 459..600
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 605
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 610 AA; 66702 MW; D5A25DA9DB02237D CRC64;
MCGIVGAVAQ RDVAEILLEG LRRLEYRGYD SAGIAVVNAE GQMQRLRRLG KVQVLAEAVE
QHPLQGGTGI AHTRWATHGE PSEANAHPHV SDFIAVVHNG IIENHEPLRN VLRERGYEFR
SQTDTEVIAH LVHWELTQNG GPLLAAVQRT LRQLDGAYGT VVIDARDPER MIAARSGSPL
VIGRGLGENF LASDQLALLP VTRRFIFLEE GDVAEITRRS VAIFDVDGQP VQRAEIESNL
QHDAGDKGQF RHYMQKEIYE QPVAIKNTLE GRIAHGSVQL SELGEAADQL LEQVQHVQIV
ACGTSYHAGA VARYWFESIA GVACNVEIAS EFRYRKSVRR PGSLLITLSQ SGETADTLAA
LRLSKTLGYL GSLTVCNVPG SSLVRESDLA LMTKAGAEIG VASTKAFTTQ LTALLLLVAR
IGRLHGMSAE REQALVHALQ ALPNRIDQML ALDKTIEKLA VDFNEKNHAL FLGRGDQYPI
AMEGALKLKE ISYIHAEAYA AGELKHGPLA LIDADMPVIV VAPNNELLEK LKSNIEEVRA
RGGQLYVFAA QDAGFRDEEG MKIIPLPLVE EDVAPIFYTI PLQLLSYHVA VNKGTDVDQP
RNLAKSVTVE
//
