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Database: UniProt
Entry: D3HB40_STRM6
LinkDB: D3HB40_STRM6
Original site: D3HB40_STRM6 
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
//
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