ID C0N9Y2_9GAMM Unreviewed; 631 AA.
AC C0N9Y2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
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 ORFNames=MDMS009_2950 {ECO:0000313|EMBL:EEF78406.1};
OS Methylophaga thiooxydans DMS010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF78406.1, ECO:0000313|Proteomes:UP000004679};
RN [1] {ECO:0000313|EMBL:EEF78406.1, ECO:0000313|Proteomes:UP000004679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF78406.1,
RC ECO:0000313|Proteomes:UP000004679};
RX PubMed=21478352; DOI=10.1128/JB.00388-11;
RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., Schafer H.;
RT "Draft genome sequence of the chemolithoheterotrophic, halophilic
RT methylotroph Methylophaga thiooxydans DMS010.";
RL J. Bacteriol. 193:3154-3155(2011).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00164}.
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DR EMBL; GG657907; EEF78406.1; -; Genomic_DNA.
DR AlphaFoldDB; C0N9Y2; -.
DR HOGENOM; CLU_012520_5_2_6; -.
DR Proteomes; UP000004679; 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; 3.
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:UP000004679};
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 1..204
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 272..446
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 479..621
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 358..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 626
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 631 AA; 69080 MW; 8AB2849EECE7A8A6 CRC64;
MEGLRRLEYR GYDSSGMALL DADANLHRVR AIGKIKQLEN KVDALDEPFT GQIGIAHTRW
ATHGIPSENN AHPHICNNKV AVVHNGIIEN YQTLKHKQLA AGYKFTSETD TEVVAHEIFD
NLTESDDLLD AVMQSLKSFE GAYALGVMAT DNPDTLVAAR KGSPLVIGVG IGEHFIASDV
SALLPVTQNF IFLEDGDVAC LSRDRIEIFS VLTGERVERP IKHSNLNITA VELGKHRHYM
HKEIFEQPQA VIDTLEGRIT QDQILVSSFG PTAEAIFASV NRIHIIACGT SYHAGMVAKY
WTEDIVGIPC QVEVASEFRY RNPVIENHTL FVTISQSGET ADTLAALQQI NAMRQNKTAG
LRSRRASDTQ SDHQDNSTLS STSSDALNLP TLSICNVAES SLTREADLVF LTHAGPEIGV
ASTKAFTTQL VALALLLTSI GKVQNRLDDG REAMIAGGLQ KLPNLITMAL GHEDEIRRIS
EDFADKQHAL FLGRGTMYPI ALEGALKLKE ISYIHAEAYP AGELKHGPLA LIDETMPVIA
IAPLDDLLEK LKSNLQEVKA RGGQMIVFED ERSDISSENS FKVVKATTNV GRITAPITYN
ILLQLLSYHV ALIKGTDVDQ PRNLAKSVTV E
//