ID B0TCS2_HELMI Unreviewed; 655 AA.
AC B0TCS2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 89.
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:ABZ84098.1};
GN ORFNames=HM1_1526 {ECO:0000313|EMBL:ABZ84098.1};
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761 {ECO:0000313|EMBL:ABZ84098.1, ECO:0000313|Proteomes:UP000008550};
RN [1] {ECO:0000313|EMBL:ABZ84098.1, ECO:0000313|Proteomes:UP000008550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1 {ECO:0000313|Proteomes:UP000008550};
RX PubMed=18441057; DOI=10.1128/JB.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ84098.1; -; Genomic_DNA.
DR AlphaFoldDB; B0TCS2; -.
DR STRING; 498761.HM1_1526; -.
DR KEGG; hmo:HM1_1526; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_9; -.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000008550; 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 Reference proteome {ECO:0000313|Proteomes:UP000008550};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 48
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 49..264
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 331..471
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 504..645
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 49
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 650
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 655 AA; 71362 MW; 12AB2497FD0C1351 CRC64;
MPFGRQHFRE KKHESGGFFA PIFRVELFLV KGRHSIRPMI EERRNHPMCG IVGYIGGKAA
APILVEGLKK LEYRGYDSAG VAVMEAGKIE VRKAKGKLAV LEGRLSYCSF GAQTGIGHTR
WATHGKPADE NAHPHQDCRG DFAVVHNGII ENFQTLKEDL IAQGHAFTSE TDTEVLAHLV
ENFYQGDLEA AVRKVVSVIE GSYAMAFLCR HEPEKIVAVR KDSPLVVGLG DGEYFLASDI
PAILAHTRRT FILDDGEMAV LTPQGAVIKT AAAGELVDKA VFEVNWDAVA AEKGGYDHFM
IKEIYEQPKA LRDTILGRVN GDGVNLSEIK IDLELLKKTN KVTIVACGTA YHAGLVGKYV
IEDLARVPVE VDIASEFRYR DPIVDENTLV IVVSQSGETA DTLAAMREAR SKGAKVLAVT
NVVGSTISRE ADSVLYTWAG PEIAVASTKA YTTQLAAMNC IALALAQVRG TQSAETIKAI
ADAIREIPAQ VEKVLAQAET VKAISEQIKT WDDVFFIGRS VDYAVALEGS LKLKEISYIH
AEAYAAGELK HGTLALITDN IPVIALATQE QVFDKTISNI QEVKARDAFV IAVAQEGNRE
IAKFAEYVLT IPRTHPALAP ILAVVPLQML SYYTAVAREC DVDKPRNLAK SVTVE
//