ID G3BD71_CANTC Unreviewed; 696 AA.
AC G3BD71;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=CANTEDRAFT_111025 {ECO:0000313|EMBL:EGV60256.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV60256.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(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; GL996528; EGV60256.1; -; Genomic_DNA.
DR RefSeq; XP_006689470.1; XM_006689407.1.
DR AlphaFoldDB; G3BD71; -.
DR STRING; 590646.G3BD71; -.
DR GeneID; 18246245; -.
DR KEGG; cten:CANTEDRAFT_111025; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_2_1; -.
DR OrthoDB; 1705390at2759; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000000707; 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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..300
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 372..511
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 544..686
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 696 AA; 77122 MW; 1C8E9242F916C13E CRC64;
MCGIFGYVNF LVDKTRGEIV DTLIDGLQKL EYRGYDSAGI AIDGDKKGET LIVKTAGKVK
ALKDKLDNSN IERSTIFDSH VGIAHTRWAT HGQPMESNCH PHRSDPEAEF VVVHNGIITN
YRELKTLLVS KGYKFESETD TECIAKLFKH IYDTNLKANI EVDFNELVKQ VLYELEGSYG
LLVKSSHYPG EAVGTRKGSP LLVGVKTEKK LKVDFVDVEF PEQNQEVPVG SAKNGELNGF
IPLSGAEASL RTSQSRAFLA DDGLPMPAEF FFSSDPASVV QHTKKVLYLE DDDIAHVYDG
ELHIHRAKKN AGDSTTRPIQ TLEMELNEIM KGPYTHFMQK EIFEQPDSTF NTMRGRIDFE
NHQINLGGLK AFLPAIRRSR RIIMIACGTS YHSCLATRSI FEELNEIPVT VELASDFLDR
RSPVFRDDTC VFVSQSGETA DSILALQYCL ERGALSVGIV NSVGSSMSRQ THCGVHINAG
PEIGVASTKA YTSQYIALVM FALSLSNDSI SQQQRHREII DGLQKIPEQI KTVLKLENKI
KTLCTEHLND QRSLLLLGRG YQFATALEGA LKIKEISYMH SEGVLAGELK HGVLALVDDK
LPIIAFATRD SLFPKVLNAI NQVVSRDGRP IVICDEGDTV LSSSQTTATL HVPTTVDCLQ
GLLNVIPLQL MSYWLAVNRG IDVDFPRNLA KSVTVE
//
