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Database: UniProt
Entry: A0A0S7BM59_9CHLR
LinkDB: A0A0S7BM59_9CHLR
Original site: A0A0S7BM59_9CHLR 
ID   A0A0S7BM59_9CHLR        Unreviewed;       595 AA.
AC   A0A0S7BM59;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=LARV_02646 {ECO:0000313|EMBL:GAP14869.1};
OS   Longilinea arvoryzae.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Longilinea.
OX   NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP14869.1};
RN   [1] {ECO:0000313|EMBL:GAP14869.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KOME-1 {ECO:0000313|EMBL:GAP14869.1};
RA   Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.;
RT   "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT   caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT   saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously Described as
RT   Members of the Anaerolineaceae (Chloroflexi).";
RL   Submitted (JUL-2015) 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};
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DR   EMBL; DF967972; GAP14869.1; -; Genomic_DNA.
DR   RefSeq; WP_075074093.1; NZ_DF967972.1.
DR   AlphaFoldDB; A0A0S7BM59; -.
DR   STRING; 360412.LARV_02646; -.
DR   OrthoDB; 106547at2; -.
DR   Proteomes; UP000055060; 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; 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; 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   ECO:0000313|EMBL:GAP14869.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055060};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAP14869.1}.
FT   DOMAIN          2..220
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          283..423
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          446..585
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   595 AA;  64775 MW;  69A990AED2ADCF39 CRC64;
     MCGIFGIVTE KEQTLGPILV EAARRLTYRG YDSVGAATIS GDRIDLRKDA GRVDEVARKY
     NFAEMTGQRG ITQLRWATFG APSQLNSQPH LDSDGDIVGA HNGNVVNNVE LREQFMAEGL
     VVRSQNDGES CVHAVERYIN RGKDFIEAIR LAHGDLQGDY SFVIGRINDD KLFAIKKGSG
     LVVGIGDGFT CVSSDLPSIL PLTRKVIRLN DGEIITLWAN RVELHSVKDG ALIERALEII
     TEEMTAVQKG GFAHFMLKEI HEQPQVAREV INLLNNSADV QSILDQLATA RHIYFIGCGT
     SYHACLAGAV YFGQLAKKAV TPVLATQFIP QYLPAVNQED VGIFVSQSGE TKDVLTALQE
     AQNRGMTCFS LANVIGSTLT RGTSACLPLG CGYEISVPAT KTFTNQVITF LYLATRLGGQ
     DLRQLDRLPE LMSQTITMTD PQVKALVPKI NSWNDLYCLG YGATYSMALE GALKLKEITY
     AHCEGMLSTE FKHGPLSAVL KDFPILFVAG PEDVPLIVSG INEVTCRGGR AIAIGEADQR
     LNANATDVIT IPSSNAAFAS LLSVIPLQLL SYYMSVDRGY DPDFPRNLSK TLTVD
//
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