ID F4R5Y4_MELLP Unreviewed; 704 AA.
AC F4R5Y4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=MELLADRAFT_70720 {ECO:0000313|EMBL:EGG12173.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883091; EGG12173.1; -; Genomic_DNA.
DR RefSeq; XP_007404548.1; XM_007404486.1.
DR AlphaFoldDB; F4R5Y4; -.
DR STRING; 747676.F4R5Y4; -.
DR EnsemblFungi; EGG12173; EGG12173; MELLADRAFT_70720.
DR GeneID; 18931616; -.
DR KEGG; mlr:MELLADRAFT_70720; -.
DR VEuPathDB; FungiDB:MELLADRAFT_70720; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_0_1; -.
DR InParanoid; F4R5Y4; -.
DR OrthoDB; 1705390at2759; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000001072; 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:UP000001072};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..309
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 381..521
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 552..694
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 223..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 78099 MW; C45AA02DEB05BD7B CRC64;
MCGIFAYASF LVEKDRRYII ETLLNGLQRL EYRGYDSAGI EVDGDKPGEV FIFKQVGKVK
LLRAHTEQAT VDFDKQFLIQ SSMAHTRWAT HGQPSSLNCH PHRSDATNEF TVVHNGIITN
YKELRLVLEK RGYEFETETD TEVAAKLCKF LFDNSKGKNL TFTTLIKGVI KELEGAFAFV
FKSVHFPDEI VVCRRGSPVL IGVKTEKKLK VDFVDVEVAG PNEGEVESLS SPTDAASQTK
SGLLAPPTEG GLKPGGAKLI RSQSRAFVSD DGVPQPIEFF IASDASAIVE HTKRVLYLED
DDIAHIAEGE FHIHRLRRND GVSSVRAIET LEMELAAIMK GNFDHFMQKE IYEQPESVVN
TMRGRVNFDT GRINLGGLKA YLPTIRRCRR IVFVACGTSF HSCLATRAIF EELTEIPVSI
ELASDFLDRR TPIFRDDTCI FVSQSGETAD TILAMRYCLE RGALNVGVVN VVGSTISRET
HCGIHINAGP EIGVASTKAY TSQYIALVMM AIQLSEDRMS LTERRNQIID GLHELPRQIR
EILTQDKEIQ QLAGTISKER SLLIMGRGYQ HATCLEAALK VKELTYMHSE GILAGELKHG
PLALIDENMP VIIIMTKDSL YPKVQSALQQ VTARKGSPIV IANEGDTGLT AADSTRILRV
PQTVDCLQGL LAIIPMQLLS YHIAILRGVD VDFPRNLAKS VTVE
//