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Database: UniProt
Entry: A0A061H2W9_9BASI
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ID   A0A061H2W9_9BASI        Unreviewed;       700 AA.
AC   A0A061H2W9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, 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=PFL1_05458 {ECO:0000313|EMBL:EPQ26823.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26823.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ26823.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26823.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
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; KE361642; EPQ26823.1; -; Genomic_DNA.
DR   RefSeq; XP_007881186.1; XM_007882995.1.
DR   AlphaFoldDB; A0A061H2W9; -.
DR   GeneID; 19319549; -.
DR   KEGG; pfp:PFL1_05458; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   HOGENOM; CLU_012520_5_2_1; -.
DR   OrthoDB; 1705390at2759; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000053664; 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   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
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..690
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   700 AA;  77270 MW;  4A2CF1CC525D9BE7 CRC64;
     MCGIFAYVNH LVEKDRRQVI DILVNGLARL EYRGYDSAGL AVDGDNESDT LIFKQVGKVA
     ALRKHIDEAP VDFNKTFISQ MGMAHTRWAT HGQPTPINCH PHRSDVKNEF TVVHNGIITN
     YRELKLVLEK RGFQFETETD TEAVAKLCKY LYDSATSRKP DFTSLVKSVV KELEGAFSFV
     FKSVHFPGEV VVARRGSPLL IGVKTEKKLK VDFVDVELGG AVDSSGFGDA GLLAPPGGKN
     PSGPGSLSVP NANNKLLRSQ SRAFLSEDGL PQPIEYFVAS DASAIIEHTK RVLYLEDDDI
     AHIAEGELHI HRLRRNDGLS SMRSIETLEM ELAEIMKGQF DHFMQKEIYE QPESVVNTMR
     GRVDFDSRKV TLGGLSAFLN TIRRCRRIVF VACGTSYHSC LATRAIFEEL TEIPVSIELA
     SDFLDRKTPI FRDDVCVFVS QSGETADTIL AMRYCLERGA LCVGVVNTVG STISRETHCG
     VHINAGPEIG VASTKAYTSQ YIALITMAVQ LSEDRISMTE RRNAIIDGLH ALPEQIRSIL
     EQDKALQALA HSTLAKEKSL LIMGRGYQHA TCLEGALKIK EVCYMHSEGI LAGELKHGPL
     ALIDESMPVI LIMTKDSLYP KVQTALMQVT ARKGQPIIIC NDDDQDIQPG SRTIRVPRTV
     DCLQGLLTVI PLQLLSYHLA TAAGVDVDFP RNLAKSVTVE
//
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