ID A0A3N4M7T2_9PEZI Unreviewed; 715 AA.
AC A0A3N4M7T2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=L211DRAFT_855076 {ECO:0000313|EMBL:RPB28862.1};
OS Terfezia boudieri ATCC MYA-4762.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pezizaceae; Terfezia.
OX NCBI_TaxID=1051890 {ECO:0000313|EMBL:RPB28862.1, ECO:0000313|Proteomes:UP000267821};
RN [1] {ECO:0000313|EMBL:RPB28862.1, ECO:0000313|Proteomes:UP000267821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4762 {ECO:0000313|EMBL:RPB28862.1,
RC ECO:0000313|Proteomes:UP000267821};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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; ML121528; RPB28862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4M7T2; -.
DR STRING; 1051890.A0A3N4M7T2; -.
DR InParanoid; A0A3N4M7T2; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000267821; 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:RPB28862.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000267821};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RPB28862.1}.
FT DOMAIN 35..320
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 392..531
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 564..705
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 715 AA; 79316 MW; 98CB4EB6710BCF6E CRC64;
MEGFHQLRYP ASAYRAPQET GALYWAYAEH IPKKCPGVGP SLRKSLSRLE YRGYDSAGVA
IDGDKEGEVF TYKEVGKVAK LKKLIDESKP DLDASFTSHA GIAHTRWATH GKPSRLNCHP
HRSDPKFQFT VVHNGIITNY KELKAFLESK GDVFETETDT ECIAKLAKYI YERDTSIDFT
TLAKSVIKEL EGAFGLLLKS VHYSHEVIAA RKGSPLVIGV KTSRKMKVDF VDVEYSDSTT
GPLSAEQASQ TVALKKLKGN TLAPPDKSLL HRSQSRAFLS DDGLPVPAEF FLSSDPSAIV
EHTKKVLYLE DDDIAHIHEG QLNIHRAGKG DGLSAVRSIQ TLELELQEIM KGKFEHFMQK
EIFEQPESVI NTMRGRLDAE NKRVTLGGLR QYLSTIRRCR RIIFIACGTS YHSCMAVRGI
FEELTEIPIA VELASDFLDR QAPVFRDDTC VFVSQSGETA DSLMALRYCL ERGALTVGIV
NVVGSSISLL THCGVHINAG PEIGVASTKA YTSQFIALVM FALSLSEDRA SKAKRREDIM
NGLDKISGQI KKILDQDQAI KKMCQDMLHE QKSLLLLGRG NQFATALEGA LKIKEISYLH
CEAVMSGELK HGVLALVDEN LPIIMILTRD EIFKKSLNAY QQVVARAGKP IVICNEGDEE
FAKEKCVKIE LPQTVDCLQG LLNVIPLQLI AYWLAILGNL NVDFPRNLAK SVTVE
//
