ID J7QQA9_METSZ Unreviewed; 615 AA.
AC J7QQA9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 OrderedLocusNames=BN69_0699 {ECO:0000313|EMBL:CCJ06150.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ06150.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ06150.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ06150.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
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; HE956757; CCJ06150.1; -; Genomic_DNA.
DR AlphaFoldDB; J7QQA9; -.
DR STRING; 187303.BN69_0699; -.
DR KEGG; msc:BN69_0699; -.
DR PATRIC; fig|187303.17.peg.765; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_5; -.
DR Proteomes; UP000005263; 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 7
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 8..223
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 288..429
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 462..605
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 8
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 610
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 615 AA; 65711 MW; 0AC7B99968CF43F6 CRC64;
MLLEVVMCGI VGIIGTAPVA GKIVDALKRL EYRGYDSAGI ATLENGRLTR LRASGKLRNL
EEKLAAAPLS GAIGIGHTRW ATHGRPTENN AHPHANDRVA VVHNGIIENF RELRAELTAK
GHIFSSETDS EAVAHLVADA LGDGATPEQA VASALKRLKG AFALVFLFEG ENDLLIGARR
GSPLAVGWSD EGAYLGSDAL ALAPFATSIA YLDEGDWVTL TRDAARFHDA SDALVERRFQ
PLTAGSFLVD KGNYRHFMAK EIHEQPEVVG RTLAHYLDLA EGVVRLPFDL TFDPRTLSRV
TISACGTAYY AGLVARYWLE RFAALSVEID IASEFRYREA PLPENGLTIL VSQSGETADT
LAALRYAREQ GQHILSIVNV ETSTIARESD TVAQTLAGPE IGVASTKAFT CQLAVFACLA
LALGRARGVL SKERERELVA ELVATPGQMA QALAREAQIE PVARDVARAS SVLYLGRGPA
FPLALEGALK LKELSYIHAE GYAAGELKHG PIALIDFAMP VIVLAPPDAS LEKTVSNLQE
VAARGGHLIL IGSPHARDAA AAELAGFVEM PESVAGPFAV LVYAVPAQLL AYHVATFMGK
DVDQPRNLAK SVTVE
//
