ID A0A226BZS3_9FIRM Unreviewed; 607 AA.
AC A0A226BZS3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:OWZ84445.1};
GN ORFNames=CDO51_02770 {ECO:0000313|EMBL:OWZ84445.1};
OS Natranaerobius trueperi.
OC Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=759412 {ECO:0000313|EMBL:OWZ84445.1, ECO:0000313|Proteomes:UP000214588};
RN [1] {ECO:0000313|EMBL:OWZ84445.1, ECO:0000313|Proteomes:UP000214588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18760 {ECO:0000313|EMBL:OWZ84445.1,
RC ECO:0000313|Proteomes:UP000214588};
RA Zhao B.;
RT "Draft Genome Sequence of Natranaerobius trueperi halophilic,
RT alkalithermophilic bacteria from soda lakes.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWZ84445.1}.
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DR EMBL; NIQC01000004; OWZ84445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226BZS3; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000214588; Unassembled WGS sequence.
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:UP000214588};
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 284..423
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 456..597
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 602
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 607 AA; 67187 MW; F8F8DD0B8E910039 CRC64;
MCGIVGYIGY KKAVDVLQKG LKKLEYRGYD SAGISVIEED NLKTVKTKGR LYDLTDILEK
ENFTSSIGIG HTRWATHGKP SDANSHPHQD CSNNISIVHN GIIENYQSLK AQLQEKGHTF
NSETDTEVIA HLIEENYDGD ILKTVINIQE KLEGSYALGV LHQKEPDKIV CTRKDSPLIV
GVGENENVIA SDIPAILDYT REAIILDDGE TGLVKQDEVT IYDENAKEVT KETMEINWNT
EEAEKGGYDH FMLKEIHEQP KAVKETVRGR VQKDSVDLEE LSLTKEEISS FNKIDIVACG
TAYHAGLIGK SLFESLARVP VEVSIASEFR YRDPLLSNNN LVIVISQSGE TADTLAALRE
SQKRGAKVLA ITNVVGSSVS READEVIYTW AGPEIAVAST KAYVTQLVAL SLLATYFAQT
KKTITSERLD QLVTTINSLP EHVERIFEYE DEILDIAKKV SKYENAFFIG RSLDWAVAEE
AALKLKEISY IHAEAYAAGE LKHGTLALIV DNVPVISLAT QPHVYEKTIS NLQEVKARGA
QCITVVNEDD TEINNESDQI IRIPNIDPLL SPILSVIPLQ LLSYYAAVAR GTDVDKPRNL
AKSVTVE
//
