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
//