ID W7CNG6_9LIST Unreviewed; 560 AA.
AC W7CNG6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=BCAMP_08581 {ECO:0000313|EMBL:EUJ38597.1};
OS Brochothrix campestris FSL F6-1037.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ38597.1, ECO:0000313|Proteomes:UP000019243};
RN [1] {ECO:0000313|EMBL:EUJ38597.1, ECO:0000313|Proteomes:UP000019243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ38597.1,
RC ECO:0000313|Proteomes:UP000019243};
RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Novel taxa of Listeriaceae from agricultural environments in the United
RT States.";
RL Submitted (DEC-2012) 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:EUJ38597.1}.
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; AODH01000035; EUJ38597.1; -; Genomic_DNA.
DR AlphaFoldDB; W7CNG6; -.
DR STRING; 1265861.BCAMP_08581; -.
DR PATRIC; fig|1265861.3.peg.1683; -.
DR Proteomes; UP000019243; 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:EUJ38597.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000019243};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EUJ38597.1}.
FT DOMAIN 1..176
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 243..382
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 412..550
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 560 AA; 61030 MW; EC3687B56C7A507D CRC64;
MTTTKTKGRI ADLRAAVTAE QYGTCGIGHT RWATHGVPSE SNAHPHQSHS GRFTLVHNGV
IDNYRQLQAT YLNGVNLKSD TDTEVVVQMM DVFAKDGLST EEIFRAVLNE LAGSYAFGLI
DMQREGELFF AKNKSPLLIG VGNDAMMLAS DAMAVIRQTD QFVEINDREM GVLTAESYHL
FDGDTNEVVV RAPYTAAIDA DDVEKGMYPH YMMKEMDEQP GVIRRIVQKY QAKDGSFTID
ADLMAAINAA DRLYIVACGT SYHAGLIGRK LIEEKAGIPV EVVVASEFGY DMPLLSAKPV
FLFISQSGET ADSRQVLVKI KQLGHTAITL TNVAGSTLSR EASHTLLLHA GPEIAVASTK
AYTAQVAVLS ILAETLGKAN GHTQTNDMVH ELGIVANAMQ TIIDEKEQIQ QLVHDYVATT
RNAFFLGRGV DYFVSLEAAL KLKEISYIQA EGFSSGELKH GTIALIEDNT PVIALITQPH
TQLQIRSNCS EVQSRGAHVA TVVTESLAQP EDTFVIPNTA LELTPLVSVV FTQLFAYYAA
LARDCDVDKP RNLAKSVTVE
//
