ID A4ZH64_LACHE Unreviewed; 603 AA.
AC A4ZH64;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 08-NOV-2023, entry version 85.
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=glmS1 {ECO:0000313|EMBL:ABH11644.1};
GN Synonyms=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
OS Lactobacillus helveticus CNRZ32.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=326425 {ECO:0000313|EMBL:ABH11644.1};
RN [1] {ECO:0000313|EMBL:ABH11644.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNRZ32 {ECO:0000313|EMBL:ABH11644.1};
RX PubMed=17322329; DOI=10.1128/AEM.00005-07;
RA Smeianov V.V., Wechter P., Broadbent J.R., Hughes J.E., Rodriguez B.T.,
RA Christensen T.K., Ardo Y., Steele J.L.;
RT "Comparative high-density microarray analysis of gene expression during
RT growth of Lactobacillus helveticus in milk versus rich culture medium.";
RL Appl. Environ. Microbiol. 73:2661-2672(2007).
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}.
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DR EMBL; DQ826151; ABH11644.1; -; Genomic_DNA.
DR RefSeq; WP_003626989.1; NC_021744.1.
DR AlphaFoldDB; A4ZH64; -.
DR KEGG; lhv:lhe_0499; -.
DR PATRIC; fig|326425.4.peg.633; -.
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..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 284..423
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 456..593
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 598
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 603 AA; 66100 MW; 727B6D537DCDFA94 CRC64;
MCGIVGVVGK PAREIILSGL TNLEYRGYDS AGIYLNDLNG NEYLTKAVGR ILNLKEKLTP
DEQGLVGIGH TRWATHGKPT VDNAHPHFDE TKRFYLVHNG VIENFAELKE KYLQGVHFHS
DTDTEVVVQL IGKIARDKNL DGFSAFKEAL KLVKGSYAFL LVDNTEPDHV FIAKNKSPMM
LGIGDGFNII ASDAISVMDQ TKTFVDLHDG DVGDITKDSY TIETVDGKKV DREPHVLNID
PNAASKGAYE FYMLKEIDEQ PGVMRHMSQN YLDDNGEPKV DQDILDAISK ADRLYIFAAG
TSYHAGLVGK TIFEHYTGIP TEVGLASEVG YHFPMMSKHP FFIFLTQSGE TADSRVVLKE
VNKRSIPSLT MTNVEGSTLS REATYTMLLG AGPEIAVAST KAYTAQIALQ AVLAKALGEK
LGKQEAKDWN LRQDLAMAAE GIQQIVDGKE KLKKLADDYL IKSRNAFYIG RGIDYAVALE
AALKLKEVSY IQTEGFAAAE LKHGTISLIE KGTPVVALIN DPVTADLTRG NIQEVVSRGA
SVITIVGKDF AREGDDIVLP EINYYMSALL TVVPAQLLAY YASKDKGLDV DKPRNLAKSV
TVE
//