ID D1BR20_VEIPT Unreviewed; 610 AA.
AC D1BR20;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 90.
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 OrderedLocusNames=Vpar_0299 {ECO:0000313|EMBL:ACZ23983.1};
OS Veillonella parvula (strain ATCC 10790 / DSM 2008 / CCUG 5123 / JCM 12972 /
OS NCTC 11810 / Te3) (Veillonella alcalescens).
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=479436 {ECO:0000313|EMBL:ACZ23983.1, ECO:0000313|Proteomes:UP000007968};
RN [1] {ECO:0000313|Proteomes:UP000007968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10790 / DSM 2008 / CCUG 5123 / JCM 12972 / NCTC 11810 /
RC Te3 {ECO:0000313|Proteomes:UP000007968};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P., Woyke T.,
RA Wu D., Wellnitz S., Schneider S., Gronow S., Klenk H.P., Eisen J.A.;
RT "The complete genome of Veillonella parvula DSM 2008.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ23983.1, ECO:0000313|Proteomes:UP000007968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10790 / DSM 2008 / CCUG 5123 / JCM 12972 / NCTC 11810 /
RC Te3 {ECO:0000313|Proteomes:UP000007968};
RX PubMed=21304678; DOI=10.4056/sigs.521107;
RA Gronow S., Welnitz S., Lapidus A., Nolan M., Ivanova N.,
RA Glavina Del Rio T., Copeland A., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Saunders E., Brettin T., Han C., Detter J.C., Bruce D., Goodwin L.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Pati A., Mavromatis K.,
RA Mikhailova N., Chen A., Palaniappan K., Chain P., Rohde M., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lucas S.;
RT "Complete genome sequence of Veillonella parvula type strain (Te3).";
RL Stand. Genomic Sci. 2:57-65(2010).
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; CP001820; ACZ23983.1; -; Genomic_DNA.
DR RefSeq; WP_012863873.1; NC_013520.1.
DR AlphaFoldDB; D1BR20; -.
DR PaxDb; 479436-Vpar_0299; -.
DR GeneID; 69652837; -.
DR KEGG; vpr:Vpar_0299; -.
DR PATRIC; fig|479436.6.peg.291; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_9; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000007968; Chromosome.
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 287..426
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 459..600
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 605
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 610 AA; 66746 MW; D822D3B838EC985D CRC64;
MCGIVGYIGF NQASDFLLDG MAKLEYRGYD SAGIAVIGPE NVIKIQKKVG RLSNLETIVK
ADPNEGTVGI GHTRWATHGR PSDMNAHPHA SEDGKFAVVH NGIIENYMPL KEELIAKGYH
FKSETDTEVV AHLLEDMYDG DFVGTVRRML NRVDGAYALE IICADEPDKI ICTKKENPLV
IGLGKGENFV ASDIPAIINY TRDTYILSDG ELAIVTRDNV SVFDREGKAV DKEVFHVNWN
AEAAEKGGYE HFMLKEIHDQ PKAVRDTFGT HISEDGKTAI FDELNWTAED VAAFNKILIV
ACGTAYHAGL VTKQYIENLA RIPVDVEIAS EYRYSNPLTD DKTLCIVISQ SGETSDTLAA
LKEAKRLGAK SLAITNVVGS SISREADNKV YTWAGPEISV ASTKAYTTQL VAGLLFAVYL
GQLNGKMNPA VGEEILSGVK NLPSLIHEIF EVDEDMKAFA KHYGFKSDAF FLGRAIDYAV
AMEGALKLKE ISYIHAEAYA GGELKHGTLA LIEEGVPVIA LATQEDVYDK MISNIREVKA
REAIVIGIGM KGDEELSKHV DHTIYVPRAN KFIAPILAVV PLQLLAYYAA ITRGADVDKP
RNLAKSVTVE
//