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Database: UniProt
Entry: I2K2Y7_DEKBR
LinkDB: I2K2Y7_DEKBR
Original site: I2K2Y7_DEKBR 
ID   I2K2Y7_DEKBR            Unreviewed;       710 AA.
AC   I2K2Y7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=AWRI1499_0466 {ECO:0000313|EMBL:EIF49589.1};
OS   Brettanomyces bruxellensis AWRI1499.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF49589.1, ECO:0000313|Proteomes:UP000004997};
RN   [1] {ECO:0000313|EMBL:EIF49589.1, ECO:0000313|Proteomes:UP000004997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF49589.1,
RC   ECO:0000313|Proteomes:UP000004997};
RX   PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA   Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT   "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT   Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL   PLoS ONE 7:E33840-E33840(2012).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIF49589.1}.
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DR   EMBL; AHIQ01000032; EIF49589.1; -; Genomic_DNA.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000004997; 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   ECO:0000313|EMBL:EIF49589.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004997};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EIF49589.1}.
FT   DOMAIN          2..314
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          386..527
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          557..700
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   710 AA;  78647 MW;  A8504255D2E87B64 CRC64;
     MCGIFGYANY NVDRSRGQII DTLVEGLQKL EYRGYDSAGI GIDGEKDFDE NSPVKEIALY
     RQVGKVSKLK AEIASHHPDT SEIFHKHVGI AHTRWATHGG VTQANCHPQP SDDRNEFIVV
     HNGIITNYRE LKTFLRGLGY TFRSDTDTEV IAKLFKYYYD KDPELEFYEL AKQVLYQLQG
     SYGLLVKSVR YPNEMIATRK GSPLLIGVKT EQKLKVDFVD VEFINDRTGT EKLSAIXGSS
     IDASAIPSRP GGRLTASRPS KNTMTIRKSE SRAILPDFSK PIEFYVSSDA SAVIEHTKKV
     LFLEDDDIAH IDQGELHIHR ARRSAGTSTT RPVHTLEMKL AEIMKGGYDH FMLKEIFEQP
     DSTFNTMRGR VDFKNKTVTL GGVKDYLTTI RRSRRYLMIA CGTSYHSCLA VRPLFEELTG
     EPVTVDLASD FLDREPPVFR DDTCXFVSQS GETADSMLAL RYCKSAGALT LGIVNTVGSS
     ISRETDCGVH INAGPEIGVA STKAYTSQFI ALVMLALQIS SNVLDNKTRH EQIIDGLREV
     PLLISKTLKK SGQVKKICND YLHGKESILV IGRGYQYSSA LEGALKIKEI SYIHAEGVQA
     GELKHGTLAL IDDKMPVIAF ATRDSLSPKV NSAIQQVTAR DGRPIVICSE GDTKIDESKT
     SALFEVPTTV DCLQGLINII PLQLMGYYLS VAAGNNPDRP RNLAKSVTVE
//
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