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Database: UniProt
Entry: A0A1E5MLI3_9MICO
LinkDB: A0A1E5MLI3_9MICO
Original site: A0A1E5MLI3_9MICO 
ID   A0A1E5MLI3_9MICO        Unreviewed;       721 AA.
AC   A0A1E5MLI3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   ORFNames=Cus16_0092 {ECO:0000313|EMBL:OEI69486.1};
OS   Curtobacterium sp. ER1/6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1891920 {ECO:0000313|EMBL:OEI69486.1, ECO:0000313|Proteomes:UP000095245};
RN   [1] {ECO:0000313|EMBL:OEI69486.1, ECO:0000313|Proteomes:UP000095245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER1/6 {ECO:0000313|EMBL:OEI69486.1,
RC   ECO:0000313|Proteomes:UP000095245};
RA   Garrido L.M., Alves J.M., Oliveira L.S., Gruber A., Padilla G.,
RA   Araujo W.L.;
RT   "Draft genome sequence of Curtobacterium sp. strain ER1/6, an endophytic
RT   strain isolated from Citrus sinensis with potential to be used as a
RT   biocontrol agent.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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};
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:OEI69486.1}.
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DR   EMBL; MJAK01000001; OEI69486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5MLI3; -.
DR   STRING; 1891920.Cus16_0092; -.
DR   PATRIC; fig|1891920.3.peg.96; -.
DR   Proteomes; UP000095245; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
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   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   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000313|EMBL:OEI69486.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095245};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OEI69486.1}.
FT   DOMAIN          113..337
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          399..536
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          570..711
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   721 AA;  74923 MW;  ECCA7C2DBB30A081 CRC64;
     MVGGVRPGAG LRETAPSAAA SHRDGGEPQE RAAGVVATGA PGEASRAPTA VPSPEGQPAP
     RTSGTRTVAP GPSPPDPRTD TTDGPGHAAD PTAVGAAPLD RPRGPHPNGH QMCGIIAARV
     SDDATPFLLD GLERLEYRGY DSVGIAVRTA SGKLETVRSV SRVGDLRALV AARADAAPAS
     DARSGVGIGH TRWATDGAVR EENAHPHADC SGRISIVHNG TIDNADRLRA TLERQGHVFR
     SDVDSEVIAH LVERALGVDP DLLLAVHIAV AQLEGSWAIV VLDARDGRMV AAADRSPLVV
     ARSDRGDFVS SDVGAIAEWC ETFVPLRDGD VVELGEAWSW SSEGVAVPVP FPTASPFAPS
     ALELGDHPDH MAKEIGEQPE VVAALLDRVR RRTADGSTWV GLGLPPFDRL AVVACGTSLH
     AGQVIAGTLR TLGGVPTDIV VASEVDHVVL TPGTLVVAIS QSGETADVLR ALDRLDERHP
     VLALTNNVHS SLARRADAVL DCHAGPEVGV AATKTFTAQV LVGVTAVVSA LVASGRLEAS
     RAAALVDELA ELPERMATAA AVAADRVPLL ATTVRDAPGF LFLGRGPGLP YAAEGALKLE
     VLSYRWAEAY PAGELKHGPL ALVDEGTPVV VVDHGDPRLQ WAVAEVRARG GFVVTVGGEG
     TDLPALPRRT DAADLAWGRS TAPWGPIEAV VPLQMLAREL ALQLGCDVDK PRNLAKWVTV
     E
//
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