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Database: UniProt
Entry: C0N9Y2_9GAMM
LinkDB: C0N9Y2_9GAMM
Original site: C0N9Y2_9GAMM 
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
//
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