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Database: UniProt
Entry: A4ZH64_LACHE
LinkDB: A4ZH64_LACHE
Original site: A4ZH64_LACHE 
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
//
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