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Database: UniProt
Entry: A0A0D2H757_9EURO
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ID   A0A0D2H757_9EURO        Unreviewed;       701 AA.
AC   A0A0D2H757;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=Z517_07060 {ECO:0000313|EMBL:KIW80444.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW80444.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW80444.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW80444.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846972; KIW80444.1; -; Genomic_DNA.
DR   RefSeq; XP_013284252.1; XM_013428798.1.
DR   AlphaFoldDB; A0A0D2H757; -.
DR   STRING; 1442368.A0A0D2H757; -.
DR   GeneID; 25306550; -.
DR   VEuPathDB; FungiDB:Z517_07060; -.
DR   HOGENOM; CLU_012520_5_0_1; -.
DR   OrthoDB; 1705390at2759; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000053029; 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:UP000053029};
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..691
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   701 AA;  77883 MW;  68D9480A3286FD41 CRC64;
     MCGIFGYINY LVEKDRRFIL DTLLNGLARL EYRGYDSAGL AVDGDKKNEV FAFKEVGKVA
     KLRELVEKSG VDMTKVFDSH CGIAHTRWAT HGQPSRLNCH PHRSDPKWEF AVVHNGIITN
     YKELKALLEG KGFKFETDTD TECIAKLAKY LYDQHPDIDF TTLGKAIIKE LQGAFGLLMK
     SVHYPHECIA ARKGSPLVVG VKTAKKMKVD FVDVEYSEDG GALSAEIANH NVAVKKSTAG
     LLAPNGMLAP PDKSLLHRSQ SRAFLSDDGM PQPAEFFLSS DASALVEHTK KVLYLEDDDI
     AHIHDGQLNI HRLTKDDGTS NVRAIQTIEL ELQEIMKGKF DHFMQKEIFE QPESVVNTMR
     GRLDVANRTV TLGGLRQYMS TIRRCRRLIF IACGTSYHSC MAVRGAFEEL TEIPISVELA
     SDFLDRQAPV FRDDTCVFVS QSGETADSLM ALRYCLERGA LTVGIVNVVG SSISMLTHCG
     VHINAGPEIG VASTKAYTSQ FVAMIMFALS LSEDRLSKAQ RRHEIIDGLA KVSEQFREIL
     KLNDSIKEMC AKFLQNQKSL LLLGRGSQYS TALEGALKIK EISYLHCEAV MSGELKHGVL
     ALVDENLPII MILTRDDIFP KSLNAYQQVI ARGGRPIVIC NKDDPEFPPS KTERIEVPKT
     VDCLQGLLNV IPLQLIAYWL AVAEGLNVDF PRNLAKSVTV E
//
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