GLMS_STRA5
ID GLMS_STRA5 Reviewed; 604 AA.
AC Q8DZZ7;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; OrderedLocusNames=SAG0944;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
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DR EMBL; AE009948; AAM99828.1; -; Genomic_DNA.
DR RefSeq; NP_687956.1; NC_004116.1.
DR RefSeq; WP_000334314.1; NC_004116.1.
DR AlphaFoldDB; Q8DZZ7; -.
DR SMR; Q8DZZ7; -.
DR STRING; 208435.SAG0944; -.
DR MEROPS; C44.A08; -.
DR EnsemblBacteria; AAM99828; AAM99828; SAG0944.
DR KEGG; sag:SAG0944; -.
DR PATRIC; fig|208435.3.peg.949; -.
DR HOGENOM; CLU_012520_7_1_9; -.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000000821; 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; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Glutamine amidotransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT CHAIN 2..604
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135388"
FT DOMAIN 2..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 284..423
FT /note="SIS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 456..594
FT /note="SIS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT ACT_SITE 599
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ SEQUENCE 604 AA; 65636 MW; 65DD68D81B4741E0 CRC64;
MCGIVGVVGN TNATDILIQG LEKLEYRGYD SAGIFVVGDN KSQLVKSVGR IAEIQAKVGD
SVSGTTGIGH TRWATHGKPT EGNAHPHTSG SGRFVLVHNG VIENYLQIKE TYLTKHNLKG
ETDTEIAIHL VEHFVEEDNL SVLEAFKKAL HIIEGSYAFA LIDSQDADTI YVAKNKSPLL
IGLGNGYNMV CSDAMAMIRE TSEYMEIHDK ELVIVKKDSV EVQDYDGNVI ERGSYTAELD
LSDIGKGTYP FYMLKEIDEQ PTVMRKLIST YANESGDMNV DSDIIKSVQE ADRLYILAAG
TSYHAGFAAK TMIEKLTDTP VELGVSSEWG YNMPLLSKKP MFILLSQSGE TADSRQVLVK
ANEMGIPSLT ITNVPGSTLS REATYTMLIH AGPEIAVAST KAYTAQVATL AFLAKAVGEA
NGKAEAKDFD LVHELSIVAQ SIEATLSEKD VISEKVEQLL ISTRNAFYIG RGNDYYVTME
AALKLKEISY IQTEGFAAGE LKHGTISLIE DNTPVIALIS ADSTIAAHTR GNIQEVVSRG
ANALIIVEEG LEREGDDIIV NKVHPFLSAI SMVIPTQLIA YYASLQRGLD VDKPRNLAKA
VTVE
