ID A0A1E1KZ53_9HELO Unreviewed; 701 AA.
AC A0A1E1KZ53;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=RCO7_06110 {ECO:0000313|EMBL:CZT03522.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT03522.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZT03522.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZT03522.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJUW01000028; CZT03522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1KZ53; -.
DR STRING; 914237.A0A1E1KZ53; -.
DR InParanoid; A0A1E1KZ53; -.
DR OrthoDB; 1705390at2759; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000178129; 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; 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 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 ECO:0000313|EMBL:CZT03522.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CZT03522.1}.
FT DOMAIN 2..306
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 378..517
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 550..691
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 701 AA; 77693 MW; FD31124C048BB877 CRC64;
MCGIFGYINY LVEKDRKTII ETLVNGLSRL EYRGYDSAGL AVDGDKKNEV FAYKEVGKVI
KLKELIAAES PDMSKIFDSH AGIAHTRWAT HGPPSRINCH PHRSDPTWEF SVVHNGIITN
YKELKTLLTT KGFKFETETD TECIAKLAKY LYDQHPTIGF TDLAKAVIKE LQGAFGLLMK
SVHYPHEVIA ARKGSPLVIG VRTEKRMKVD FVDVEYTEDG PLPAETASQN VALKKSNVGN
FLSAGNLLAP ADKSLLHRSQ SRAFMTDDGA PMPTEFFLSS DPSAIVEHTK KVMYLEDDDI
AHIHEGSLNI HRLTKADGSS NVRTIQTLEL ELQEIMKGKF DHFMQKEIFE QPESVVNTMR
GRLDVENKVV TLGGLRSYIA TIRRCRRIIF IACGTSYHSC MAVRGAFEEL TEIPIAVELA
SDFLDRSAPV FRDDTCIFVS QSGETADSLM ALRYCLERGA LTVGIVNVVG SSISLLTHCG
VHVNAGPEIG VASTKAYTSQ FIAMIMFALS LSEDRASKQK RREDIMEGLG KISEQIKEIL
KLDQPIKELC ARTFKGQKSL LLLGRGSQFS TALEGALKIK EISYLHCEAV MSGELKHGVL
ALVDENLPII MILTRDDIFA KSLNAYQQVI ARSGKPIVIC NPNDEEFKAG QAEKIEIPKT
VDCLQGLLNV IPLQLMAYWL AVAEGLNVDF PRNLAKSVTV E
//