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Database: UniProt
Entry: S3BXF0_OPHP1
LinkDB: S3BXF0_OPHP1
Original site: S3BXF0_OPHP1 
ID   S3BXF0_OPHP1            Unreviewed;       707 AA.
AC   S3BXF0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=F503_02768 {ECO:0000313|EMBL:EPE05939.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE05939.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE05939.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE05939.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(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; KE148154; EPE05939.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3BXF0; -.
DR   STRING; 1262450.S3BXF0; -.
DR   VEuPathDB; FungiDB:F503_02768; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   HOGENOM; CLU_012520_5_2_1; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 1705390at2759; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000016923; 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   ECO:0000313|EMBL:EPE05939.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPE05939.1}.
FT   DOMAIN          2..312
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          384..523
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          556..697
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   707 AA;  78400 MW;  8D6BEDF15649B41A CRC64;
     MCGIFGYVNY LVEKDRKFIL DTLVNGLSRL EYRGYDSAGL AVDGDKKKEV FAFKEVGKVA
     KLRELIDGSG VDQDKTFDSH CGIAHTRWAT HGPPSRVNCH PHRSDPTWEF SIVHNGIITN
     YKELKTLLES KGFKFETETD TECIAKLTKY IYDQHPNVGF TDLAKAVIHE LEGAYGLLIK
     SVHYPHEVIA ARKGSPLVIG VKTQKRMKVD FVDVEYGDDN NPLPAETASQ NVALKKAGVS
     GDSFLSPASA AGGLAAPDKS LLHRSQSRAF MTDDGMPMPT EFFLSSDPSA IIEHTKKVMY
     LEDDDIAHIH EGSLNIHRLK KADGSSNVRT IQTLELELQE IMKGKFDHFM QKEIFEQPES
     VVNTMRGRLD IENKTITLGG LRSYISTIRR CRRIIFIACG TSYHSCMAVR GAFEELAEIP
     IAVELASDFL DRQAPVFRDD TCVFVSQSGE TADSLMALRY CLERGALTVG IVNVVGSSIS
     LLTHCGVHVN AGPEIGVAST KAYTSQFIAM IMFALSLSED RASKQKRREE IIEGLGKISG
     QIKSILDQNQ YIKDMCESKF KNQKSLLLLG RGSQFSTALE GALKIKEISY LHCEAVMSGE
     LKHGVLALVD ENLPIIMILT RDDLFKKSLN AYQQVIARSG KPIVICNPDD EEFKTSQAQK
     IEIPQTVDVL QGILNVIPLQ LIAYWLAVLE GLNVDFPRNL AKSVTVE
//
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