ID B0DAQ7_LACBS Unreviewed; 703 AA.
AC B0DAQ7;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|ARBA:ARBA00033302};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|ARBA:ARBA00029805};
GN ORFNames=LACBIDRAFT_291192 {ECO:0000313|EMBL:EDR08254.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR08254.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC supplies the amino sugars of asparagine-linked oligosaccharides of
CC glycoproteins). {ECO:0000256|ARBA:ARBA00003267}.
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};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004775}.
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DR EMBL; DS547102; EDR08254.1; -; Genomic_DNA.
DR RefSeq; XP_001881324.1; XM_001881289.1.
DR AlphaFoldDB; B0DAQ7; -.
DR STRING; 486041.B0DAQ7; -.
DR GeneID; 6076789; -.
DR KEGG; lbc:LACBIDRAFT_291192; -.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; B0DAQ7; -.
DR OrthoDB; 1705390at2759; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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 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 4: Predicted;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..299
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 378..521
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 553..693
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 703 AA; 77772 MW; 42F97A5D64AED75A CRC64;
MCGIFGYCSF LKEKSRKDVL EVLCSGLARQ EYRGYDSAGL CIDGDKPGQV IYFKEVGKVA
GLRKKIALSS VNVEKTTVSQ VSIAHTRWAT HGPPSEINCH PIRSDLNSEF IVVHNGIVTN
SAELRLVLQK RGYKFETETD TEAVAILTKY IYDSHNDKRP SFTDLIKSVL KELEGSFAFV
FKSFHYPNEV VTARRGSPLL VGVKTDKKLK VDFVDVEFAG QDVNDTRVDA LQPNSPSALL
AVPSANPKVL RTQSRAFMSE DGLPQPIEFF IASDAAAIVE HTKRVLYLED DDIAHIAEGE
LHIHRLRRKE EGDQSPNQIA ATRTIETLEL EIAAIMKGKF DTFMQKEIYE QPESVVNTMR
GRVNFDEYRI TLGGLRAYLP IMRRGRRIVF IACGTSYHSC LATRAIFEEL TEIPVSVELA
SDFLDRKTPI FRDDVCVFLS QSGETADTIL ALRYCMDRGA LCVGVVNTVG STLSRETHCG
VHINAGPEVG VASTKAGLHA YTSQYVALLM IALQLSEDRI SFTERRNQII DGLHALPAQI
KKVLEQDSSL EQLAMTVAAN KSLLLMGRGY QHATCLEGAL KIKEISYMHS EGILAGELKH
GPLALIDENM PVIIIMTQDS LYPKVQSAFA QITARKAQPI VLCNEGDDGI PANAKTIRVP
KTVDCLQGLL NIIPLQLLAY HLAVKNGCDV DFPRNLAKSV TVE
//