ID D3HB40_STRM6 Unreviewed; 602 AA.
AC D3HB40;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 83.
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 ECO:0000313|EMBL:CBJ23090.1};
GN OrderedLocusNames=smi_1850 {ECO:0000313|EMBL:CBJ23090.1};
OS Streptococcus mitis (strain B6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ23090.1, ECO:0000313|Proteomes:UP000008563};
RN [1] {ECO:0000313|EMBL:CBJ23090.1, ECO:0000313|Proteomes:UP000008563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:CBJ23090.1,
RC ECO:0000313|Proteomes:UP000008563};
RX PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT "The genome of Streptococcus mitis B6--what is a commensal?";
RL PLoS ONE 5:E9426-E9426(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; FN568063; CBJ23090.1; -; Genomic_DNA.
DR RefSeq; WP_000334313.1; NC_013853.1.
DR RefSeq; YP_003446950.1; NC_013853.1.
DR AlphaFoldDB; D3HB40; -.
DR STRING; 365659.smi_1850; -.
DR KEGG; smb:smi_1850; -.
DR PATRIC; fig|365659.3.peg.1871; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_7_1_9; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000008563; 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..217
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 283..422
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 455..592
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 67..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 597
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 602 AA; 65327 MW; DD8C7739601AB694 CRC64;
MCGIVGVVGN TNATDILIQG LEKLEYRGYD SAGIFVLGGA ESHLVKAVGR IAELSAKTAG
VKGTTGIGHT RWATHGKPTE DNAHPHRSET ERFVLVHNGV IENYLEIKEE YLVGHHFKGQ
TDTEIAVHLI GKFAEEDGLS VLEAFKKALH IIRGSYAFAL VDSQNPEVIY VAKNKSPLLI
GLGEGYNMVC SDAMAMIRET NQYMEIHDQE LVIVKADSVE VQDYDGNSRE RASYTAELDL
SDIGKGTYPY YMLKEIDEQP TVMRKLIQAY TDEAGQVVVD PAIIQAVQDA DRIYILAAGT
SYHAGFASKK MLEELTDTPV ELGISSEWGY GMPLLSKKPL FIFISQSGET ADSRQVLVKA
NEVGISSLTV TNVPGSTLSR EASHTMLLHA GPEIAVASTK AYTAQIAALA FLAKAVGEAN
GNAKAQAFDL VHELSIVAQS IESTLSEKEL IDSKVSELLE TTRNAFYIGR GQDYYVAMEA
SLKLKEISYI QCEGFAAGEL KHGTIALIEE GTPVLALLSD PVLANHTRGN IQEVAARGAK
VLTIAEENVA KETDDIVLMT VHPYLSPISM VVPTQLVAYF ATLHRGLDVD KPRNLAKSVT
VE
//