ID K2NHS1_9BACI Unreviewed; 600 AA.
AC K2NHS1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, 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=BA1_15181 {ECO:0000313|EMBL:EKF34446.1};
OS Bacillus xiamenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1178537 {ECO:0000313|EMBL:EKF34446.1, ECO:0000313|Proteomes:UP000010122};
RN [1] {ECO:0000313|EMBL:EKF34446.1, ECO:0000313|Proteomes:UP000010122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYC-10 {ECO:0000313|EMBL:EKF34446.1,
RC ECO:0000313|Proteomes:UP000010122};
RX PubMed=23209239; DOI=10.1128/JB.01920-12;
RA Lai Q., Liu Y., Shao Z.;
RT "Genome Sequence of Bacillus sp. Strain HYC-10, Isolated from Intestinal
RT Tract Contents from a Marine Fish (Mugil cephalus).";
RL J. Bacteriol. 194:6991-6991(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: 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:EKF34446.1}.
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DR EMBL; AMSH01000056; EKF34446.1; -; Genomic_DNA.
DR RefSeq; WP_008360582.1; NZ_LDHZ01000008.1.
DR AlphaFoldDB; K2NHS1; -.
DR GeneID; 69522645; -.
DR KEGG; bxi:BK049_07120; -.
DR PATRIC; fig|1178537.3.peg.3138; -.
DR eggNOG; COG0449; Bacteria.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000010122; Unassembled WGS sequence.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 283..422
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 452..590
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 595
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 600 AA; 65526 MW; 9E16625349FA5106 CRC64;
MCGIVGYIGQ NDAKEILLKG LEKLEYRGYD SAGIAVANEE GVHVFKEKGR IAELREVVDA
NVASSAGIGH TRWATHGVPS HLNAHPHQSA SGRFTLVHNG VIENYVQLTR EYLQDVTLKS
DTDTEVVVQV IEQFVNRGLD TEEAFRQTLL QLKGSYAIAL FDNENKETIY VAKNKSPLLV
GFGEDFNVVA SDAMAMLQVT NEYAELMDKE MVIVTKDEVI IKNLDGDIMT RPSYIAELDA
SDIEKGTYPH YMLKETDEQP LVMRKIIQEY QDENGKLSVA GDIASAVAEA DRIYIVACGT
SYHAGLVGKQ YIEDWAKVPV EVHVASEFSY NMPLLSKKPL FIFLSQSGET ADSRAVLVQV
KELGHKALTI TNVPGSTLSR EADFTLLLHA GPEIAVASTK AYTAQIAVLA ILASVAAELN
GQSLDFDLVK ELGIVANAME ALVDQKDEME QIARDFFTVT RNAFFIGRGL DYYVCLEGSL
KLKEISYIQA EGFAGGELKH GTIALIEEGT PVIALATQEH VNLSIRGNVK EVVARGANPC
VISLKGLEDE GDRFVLPAVH PALAPLASVV PLQLIAYYAA LHRGCDVDKP RNLAKSVTVE
//
