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Database: UniProt
Entry: G7VEU7_9CREN
LinkDB: G7VEU7_9CREN
Original site: G7VEU7_9CREN 
ID   G7VEU7_9CREN            Unreviewed;       605 AA.
AC   G7VEU7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {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=P186_1490 {ECO:0000313|EMBL:AET32913.1};
OS   Pyrobaculum ferrireducens.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET32913.1, ECO:0000313|Proteomes:UP000005867};
RN   [1] {ECO:0000313|EMBL:AET32913.1, ECO:0000313|Proteomes:UP000005867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1860 {ECO:0000313|EMBL:AET32913.1,
RC   ECO:0000313|Proteomes:UP000005867};
RX   PubMed=22247528; DOI=10.1128/JB.06465-11;
RA   Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT   pyrobaculum able to grow with various electron acceptors.";
RL   J. Bacteriol. 194:727-728(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: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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00164}.
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DR   EMBL; CP003098; AET32913.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7VEU7; -.
DR   STRING; 1104324.P186_1490; -.
DR   KEGG; pyr:P186_1490; -.
DR   eggNOG; arCOG00057; Archaea.
DR   HOGENOM; CLU_012520_7_0_2; -.
DR   Proteomes; UP000005867; 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   DOMAIN          5..225
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          287..425
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          455..595
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   ACT_SITE        5
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   ACT_SITE        600
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   605 AA;  65680 MW;  25E4B1D519118E76 CRC64;
     MWDVCGIFGV VFAERPGRPL GEILRRGLER LEYRGYDSAG VAVVDRGLVV RKDAGKVAEV
     ARRYGFDALQ GVAGLAHTRW ATHGRPDQVN AHPHVDCGGV IAVVHNGIIE NYAELKEELA
     KRGHVFRSET DTEVVAHLVE EYKRQGLDTF SAFRKAVSRI RGAYAIALID AENPQVIYFA
     RHLSPLIIGV GDGFNIVASD IPTVLDHTKR IIAVRDGEYG YITPTEVYIE ADGVPQDAAS
     RVEEIPWSAE MATKGGYPHF MFKEIYEQPE SLASTAAGLE PARLEAAANA LLAARNVYIV
     GAGTSYHAGL ILAHLLPRLK LTPVPIVASE YAAYEPLFDK DDFAIAVSQS GETIDTIKAV
     RAMRERGVRV AAVTNVVGST LSRESDLVIY TRAGPEIGVA ATKTFTTQVL TLSALYVSAL
     RLLGYDVAER ERELKAAPDL ARRVVEKTAG TAKDLARRLR QKPSAYYLGR GAALPVAMEG
     ALKLKEVAYI HAEAYPAGES KHGPIALVEE DFPVVFVFSD PATREKTLSN VAEMKARGAF
     AIGTVPARSD YAKKLDVAIE VPDAGELTAP IAHVIPLQML AYFAAVERGY DPDKPRNLAK
     TVTVE
//
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