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
//