ID G8YVH1_PICSO Unreviewed; 697 AA.
AC G8YVH1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, 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 Name=Piso0_000453 {ECO:0000313|EMBL:CCE72854.1};
GN ORFNames=GNLVRS01_PISO0A09680g {ECO:0000313|EMBL:CCE72854.1},
GN GNLVRS01_PISO0B09747g {ECO:0000313|EMBL:CCE73415.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE72854.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|EMBL:CCE72854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 7064 {ECO:0000313|EMBL:CCE72854.1};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(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}.
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DR EMBL; FO082059; CCE72854.1; -; Genomic_DNA.
DR EMBL; FO082058; CCE73415.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YVH1; -.
DR STRING; 559304.G8YVH1; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; G8YVH1; -.
DR OMA; ASEYRYA; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000005222; Chromosome A.
DR Proteomes; UP000005222; Chromosome B.
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:UP000005222};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..301
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 373..512
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 545..687
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 697 AA; 77676 MW; 3B68AB276D650866 CRC64;
MCGIFGYVNF LVDKSRGEIV DNLLEGLRRL EYRGYDSTGI SIDGDNRDET LIIKTPGKVS
ALKQKVDSMS LNRDTVFENH VGIAHTRWAT HGQPEYSNCH PHRSDPNCEF VIIHNGIITN
FRELKTLLLS KGMEFESETD SECIAKLFKH VYDTNMKAGI YLDFNELTKQ VLYELEGSYG
LLVKSSHYPG EICGTRKGSP LLVGVRTDRK LKVDFVDVEF RDSAKDGVIS HNTQTQEEMG
LLPVTPSESN LRTSQSRAFL SDDGLPMPVE FFLSSDPASV IQHTKKVLFL EDDDIAHIYD
GELHIHRAKK SAGESTTRQI QTLEMELNEI MKGPYKHFMQ KEIFEQPDST FNTMRGRLDF
ENSRVILGGI KSWLPTIRRC RRIIMIACGT SYHSCLATRS IFEELTEIPV SIELASDFLD
RRSPVFRDDT CLFVSQSGET ADSILALQYC LERGALTVGI VNSVGSSMSR QTHCGVHINA
GPEIGVASTK AYTSQYIALV MFALSLSSDS ISKSERRKEI IEGLKHIPQQ IKTVLSMEDK
IKSLCDSNLN DQRSLLLLGR GYQHATALEG ALKIKEISYM HSEGVLAGEL KHGVLALVDD
KLPIIAFATK DSLFPKVVSA IEQVTAREGR PIIICNEGHE VLAGGKALAT LHVPLTVDCL
QGLLNIIPLQ LMSYWLAVNR GVDVDFPRNL AKSVTVE
//
