GenomeNet

Database: UniProt
Entry: D7CWW8_TRURR
LinkDB: D7CWW8_TRURR
Original site: D7CWW8_TRURR 
ID   D7CWW8_TRURR            Unreviewed;       610 AA.
AC   D7CWW8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 79.
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   OrderedLocusNames=Trad_1354 {ECO:0000313|EMBL:ADI14476.1};
OS   Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / RQ-24).
OC   Bacteria; Deinococcota; Deinococci; Trueperales; Trueperaceae; Truepera.
OX   NCBI_TaxID=649638 {ECO:0000313|EMBL:ADI14476.1, ECO:0000313|Proteomes:UP000000379};
RN   [1] {ECO:0000313|Proteomes:UP000000379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC   {ECO:0000313|Proteomes:UP000000379};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Truepera radiovictris DSM 17093.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI14476.1, ECO:0000313|Proteomes:UP000000379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC   {ECO:0000313|Proteomes:UP000000379};
RX   PubMed=21475591; DOI=10.4056/sigs.1563919;
RA   Ivanova N., Rohde C., Munk C., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Rohde M.,
RA   Goker M., Tindall B.J., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Truepera radiovictrix type strain (RQ-24).";
RL   Stand. Genomic Sci. 4:91-99(2011).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002049; ADI14476.1; -; Genomic_DNA.
DR   RefSeq; WP_013177846.1; NC_014221.1.
DR   AlphaFoldDB; D7CWW8; -.
DR   STRING; 649638.Trad_1354; -.
DR   KEGG; tra:Trad_1354; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_0; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 106547at2; -.
DR   Proteomes; UP000000379; 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   Reference proteome {ECO:0000313|Proteomes:UP000000379};
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..222
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          287..426
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;  65667 MW;  3F9191BF279A9D52 CRC64;
     MCGIVGYVGH RQAAEVILDG LKRLEYRGYD SAGLVIAPQE QRGALSVVKK SGKLKVLSEA
     LKQGPLVGTL GLGHTRWATH GKPNDVNAHP HLSEDGRLAV IHNGIIENYL SLKAKLVESG
     HVFSSETDTE VIVHLIEEHY ARLEGDLVAA VRSALKEVSG AYALVVSHVD HELIVAARAT
     SPMVLGLGEG ENFVASDVPA LLPYTREVIF LHDGDMALIA KDSLTVTDFD GRVLARPVTT
     IEWDAEAAEK AGFEHFMLKE IYEQPTVLQH TLGGRFAGNG TDVQLELGLD PLAVDRVVIS
     ACGTAFYSGL VGEYLIERLA RLPVEVEIAS EFRYREPVLD ERTLCVVVSQ SGETIDTLEA
     LREAKRQGAR TLAVLNAKGS SISREADDVL YIHAGPEIGV ASTKAYTAMV AAFELLAIFL
     GRARGVLSGE AAAELIRALR ALPGLVEETL GARPEIAAVA EAFKDKRDYL FLGRGANYPT
     ALEGALKLKE ISYIHAEAYA TGEMKHGPIA LIDADMPVVA VATASALYDK TISNLQEVRA
     RDGVVIALAS RGDEAIRAHA DHVIYVPRTL ELVSPIVNVV ALQLLAYETA ARLGRDVDQP
     RNLAKSVTVE
//
DBGET integrated database retrieval system