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Database: UniProt
Entry: A0A024FFU7_9FLAO
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ID   A0A024FFU7_9FLAO        Unreviewed;       615 AA.
AC   A0A024FFU7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=WPG_1576 {ECO:0000313|EMBL:BAO75806.1};
OS   Winogradskyella sp. PG-2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO75806.1, ECO:0000313|Proteomes:UP000031636};
RN   [1] {ECO:0000313|EMBL:BAO75806.1, ECO:0000313|Proteomes:UP000031636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-2 {ECO:0000313|EMBL:BAO75806.1,
RC   ECO:0000313|Proteomes:UP000031636};
RX   PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA   Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT   "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT   Proteorhodopsin-Containing Marine Flavobacterium.";
RL   Genome Announc. 2:e00490-14(2014).
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; AP014583; BAO75806.1; -; Genomic_DNA.
DR   RefSeq; WP_045471015.1; NZ_AP014583.1.
DR   AlphaFoldDB; A0A024FFU7; -.
DR   STRING; 754409.WPG_1576; -.
DR   KEGG; win:WPG_1576; -.
DR   HOGENOM; CLU_012520_5_2_10; -.
DR   OrthoDB; 106547at2; -.
DR   Proteomes; UP000031636; 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:UP000031636};
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..221
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          292..431
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          464..605
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        610
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   615 AA;  67862 MW;  E34DB9A10D6C61F0 CRC64;
     MCGIVGYIGH RKAYPIVIKG LQRLEYRGYD SAGIALFDGN NIKLSKTKGK VSDLKERLES
     EISTDGTLGI GHTRWATHGV PNDVNSHPHY SNSGDLVIIH NGIIENYDSL KKELLKRGYT
     FQSDTDTEVL VNLIEDVKKN ENIKLGKAVQ IALNQVVGAY AIAVFDKNKP NEIVVARLGS
     PLAIGIGEDE FFIASDASPF IEYTKNAVYL EDEEMAIIRR GKKIKVRKIN NDSLVDPYIQ
     ELQLNLEQIE KGGYDHFMLK EIYEQPEAIL DTFRGRLLSN EALVKLAGVE DNMKKFLAAD
     RIIVVACGTS WHAGLVSEYI FEDLARIPVE VEYASEFRYR NPVITEKDVV IAISQSGETA
     DTLAAIKLAK SKGAFVFGVC NVVGSSIARE THAGAYTHAG PEIGVASTKA FTTQITVLTL
     IALRLARAKG TISSSEFRHH LIELETIPSK VEKALKSDAY VQTVADIYKD ATNFLYLGRG
     FNFPVALEGA LKLKEISYIH AEGYPAAEMK HGPIALIDEN MPIVVIATKK GHYEKVVSNI
     QEIKSRKGKI IGIVTEGDKS VKELADHVIE VPETIECLTP LLTTIPLQLL SYHIAVMLDK
     NVDQPRNLAK SVTVE
//
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