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Database: UniProt
Entry: F5VDH1_9LACO
LinkDB: F5VDH1_9LACO
Original site: F5VDH1_9LACO 
ID   F5VDH1_9LACO            Unreviewed;       605 AA.
AC   F5VDH1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=NIAS840_00603 {ECO:0000313|EMBL:EGL98889.1};
OS   Ligilactobacillus salivarius NIAS840.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1029822 {ECO:0000313|EMBL:EGL98889.1, ECO:0000313|Proteomes:UP000006227};
RN   [1] {ECO:0000313|EMBL:EGL98889.1, ECO:0000313|Proteomes:UP000006227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIAS840 {ECO:0000313|EMBL:EGL98889.1,
RC   ECO:0000313|Proteomes:UP000006227};
RX   PubMed=21914873; DOI=10.1128/JB.05688-11;
RA   Ham J.S., Kim H.W., Seol K.H., Jang A., Jeong S.G., Oh M.H., Kim D.H.,
RA   Kang D.K., Kim G.B., Cha C.J.;
RT   "Genome Sequence of Lactobacillus salivarius NIAS840, Isolated from Chicken
RT   Intestine.";
RL   J. Bacteriol. 193:5551-5552(2011).
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:EGL98889.1}.
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DR   EMBL; AFMN01000001; EGL98889.1; -; Genomic_DNA.
DR   RefSeq; WP_003705538.1; NZ_AFMN01000001.1.
DR   AlphaFoldDB; F5VDH1; -.
DR   PATRIC; fig|1029822.3.peg.603; -.
DR   Proteomes; UP000006227; 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..220
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          286..424
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          457..595
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        600
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   605 AA;  65846 MW;  FFD146662FA8D3C0 CRC64;
     MCGIVGVTGN NDATNILLDG LQQLEYRGYD SAGIYVNDQN GKDFLVKEKG RISDLRAEVG
     PEVKGSTGIG HTRWATHGIP SKVNAHPHVS ANGRFFLVHN GVIGNFAQLR DEYLQDVTLV
     SSTDTEVIVQ LIGKFSDEGL DTEAAFKKVL GLVDESSSYS FLLMDKEEPD TLFVAKNKSP
     LLIGVGDGFN VVCSDAIAML SQTHDFIELV DGEIVIVKPD SITIKDPEEN VINREPFHVD
     TDPAAAQKGA YPYYMLKEID EQPGVMRNLV QHYVAEDGSI NIDKELLDAL EKADRLYIVA
     AGTSYHAGLV GKELFEKLAN IPTEVHVASE FAYNPPLLSE KPFFIFLTQS GETADSRQVL
     TQVNTQGYPS LTITNVQNST LDREATYTLL LYAGPEIAVA STKAYTAQIA LEAILVKAYG
     EAKNIDKVKE FDVAAELTKV ANGMQELVDE KGTVEKIAKD MLATTRNAFY IGRGIDYDVA
     QEAALKLKEV SYIQTEGFAS GELKHGTIAL IEEGTPVVAV ITDPKTATHT RSNAQEVLAR
     GANVLFIASR DVAQEGDQVV LPEVTPLLSP LLAIIPAQLL AYYASIQRGY DVDKPRNLAK
     SVTVE
//
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