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Database: UniProt
Entry: A6VF26_PSEA7
LinkDB: A6VF26_PSEA7
Original site: A6VF26_PSEA7 
ID   A6VF26_PSEA7            Unreviewed;       611 AA.
AC   A6VF26;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 102.
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   ECO:0000313|EMBL:ABR86308.1};
GN   OrderedLocusNames=PSPA7_6350 {ECO:0000313|EMBL:ABR86308.1};
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754 {ECO:0000313|EMBL:ABR86308.1, ECO:0000313|Proteomes:UP000001582};
RN   [1] {ECO:0000313|EMBL:ABR86308.1, ECO:0000313|Proteomes:UP000001582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7 {ECO:0000313|EMBL:ABR86308.1,
RC   ECO:0000313|Proteomes:UP000001582};
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR86308.1, ECO:0000313|Proteomes:UP000001582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7 {ECO:0000313|EMBL:ABR86308.1,
RC   ECO:0000313|Proteomes:UP000001582};
RX   PubMed=20107499; DOI=10.1371/journal.pone.0008842;
RA   Roy P.H., Tetu S.G., Larouche A., Elbourne L., Tremblay S., Ren Q.,
RA   Dodson R., Harkins D., Shay R., Watkins K., Mahamoud Y., Paulsen I.T.;
RT   "Complete genome sequence of the multiresistant taxonomic outlier
RT   Pseudomonas aeruginosa PA7.";
RL   PLoS ONE 5:E8842-E8842(2010).
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}.
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DR   EMBL; CP000744; ABR86308.1; -; Genomic_DNA.
DR   RefSeq; WP_012078093.1; NC_009656.1.
DR   AlphaFoldDB; A6VF26; -.
DR   KEGG; pap:PSPA7_6350; -.
DR   HOGENOM; CLU_012520_5_2_6; -.
DR   OMA; TSYYSGC; -.
DR   Proteomes; UP000001582; 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 {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   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          287..427
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          460..601
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        606
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   611 AA;  66332 MW;  9863CF806022BF18 CRC64;
     MCGIVGAIAE RNITPILIEG LKRLEYRGYD SAGVAVFDNE GRLHRCRRVG KVASLEEGLA
     GTPLLGRLGI AHTRWATHGA PTEGNAHPHF SSDELAVVHN GIIENHEPLR ERLKGLGYVF
     TSQTDTEVIV HLLHHKLQSI GDLTLALKEA VKELHGAYGL AVISAAQPDR IVAARSGSPL
     VIGLGLGENF LASDQLALRQ VTDRFIYLEE GDIAEIRRDS VRLWDVQGND VQRETVQYHE
     GAEAADKGEY RHFMLKEIHE QPSVVQRTLE GRLGQNQVLV ESFGPQAAEL FAKVRNVQIV
     ACGTSYHAGM VARYWLESLT GIPCQVEVAS EFRYRKVAVQ PDCLFVTISQ SGETADTLAA
     LRNAKELGFL SSVAICNVAT SSLVRESDLS LLTQAGPEIG VASTKAFTTQ LVALLLLTLG
     IGQVQKRLAE GVEAELVDEL RRLPTRLGEA LAMNRTVEKV SELFAEKHHT LFLGRGAQFP
     VALEGALKLK EISYIHAEAY PAGELKHGPL ALVDSDMPVV TVAPNNELVE KLKSNLQEVR
     ARGGELVVFA DEGAGIEAGE GTHVVGMPHI GDVLSPILYT IPLQLLSYHV AVLKGTDVDQ
     PRNLAKSVTV E
//
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