ID A0A3E2GTJ3_SCYLI Unreviewed; 1585 AA.
AC A0A3E2GTJ3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
DE Flags: Fragment;
GN ORFNames=B7463_g11842 {ECO:0000313|EMBL:RFU24494.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU24494.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU24494.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU24494.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) 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}.
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:RFU24494.1}.
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DR EMBL; NCSJ02000439; RFU24494.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2GTJ3; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0140535; C:intracellular protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; cd11069; CYP_FUM15-like; 1.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
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; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF00067; p450; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR Pfam; PF01380; SIS; 2.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 4: Predicted;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 887..1190
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 1262..1401
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 1434..1575
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT COILED 517..551
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU24494.1"
FT NON_TER 1585
FT /evidence="ECO:0000313|EMBL:RFU24494.1"
SQ SEQUENCE 1585 AA; 175906 MW; 3C425A771363804A CRC64;
LPEPTGNSWW NGQYARISGE PTGVPMTDWV NSIPNDGVIR YLGILNSERV LITSPKAMSE
VLTTKSYEFI KPSQVVRGLS RLLGVGILLA EGDEHKIQRK NLMPAFAFRH IKDLYPVFWE
LSREAVTAMT EDINTQSANG VASNDVEESA ATASKGGAII EAGSWASRAT LDIIGVAGMG
QKFGAIRDPQ TPLNKTYRKV FTPNRQAQIL AMLNLFLPTW FVRNLPIKRN GEVEAAAAVI
KSTCRGLIRE KKAKLENNKL TDVDILSVAL ESGGFTEENL VNQMMTFLAA GHETTASSMI
WAIYMLCLNP EVQIKLREEV RDRLPSADDD TKVTNLEIDH MPYLNAVCSE VLRYNSPVPL
TLREAAHDTT IAGHYIPKGS RIVLAPAATN KDENLWGPDA RTFNPDRWLS KDGQTYIASG
GASSNYAFMT FLHGPRGCIG QAFAKAEFAC LLAAWIGRFE FELKNKEEMD EKKVLIKGGV
TSKPAKGLWV KGLFDMSGID DERVNALASF KTKLLESREW EAKLKALRLE IKDLQKEFDH
TEDNIKALQS VGQIIGEVLK QLDDERFIVK ASSGPRYVVG CRSKVDKVKL KQGTRVALDM
TTLTIMRMLP REVDPLVYNM SLEDPGQVSF AGIGGLNDQI RELREVIELP LKNPELFMRV
GIKPPKGVLL YGPPGTGKTL LARAVASGLE TNFLKVVSSA IVDKYIGESA RLIREMFGYA
KEHEPCIIFM DEIDAIGGRR FSEGTSADRE IQRTLMELLN QLDGFDYLGK TKIIMATNRP
DTLDPALLRA GRLDRKIEIP LPNEVGRLEI MKIHAAGVIT EGNIDFESVV KMSDGLNGAD
LRNVVTEAGL FAIKDYRDAV SQDDFNKAVR KVAESKKLEV LHDIFGIGIF GYINYLVERD
RKYILDTLVN GLSRLEYRGY DSAGLAVDGD KKNEVFAFKE VGKVAKLKQL IEDEKPDLTK
VFDSHAGIAH TRWATHGTPS RLNCHPHRSD PTWKFAVVHN GIITNYKELK TLLTGKGLKF
ETETDTECIA KLAWYLYQQQ PTISFTDLAK AVIKELEGAF GLLMKSVYYP HEVIAARKGS
PLVIGVRTQK RMKVDFVDVE YTEEGGALPA EQASQNVALK KSSEFLSVGG ALAPPDKSLL
HRSQSRAFMT DDGAPMPAEF YLSSDPSAIV EHTKKVMYLE DDDIAHIHEG SLNIHRLTKA
DGSSNVRTIQ TLEMELQEIM KGKFDHFMQK EIFEQPESVI NTMRGRLDIE NKKVTLGGLR
SYISTIRRCR RIIFVACGTS YHSCMAVRGA FEELTEIPIS VELASDFLDR QAPVFRDDTC
VFVSQSGETA DSLMALRYCL ERGALTVGIV NVVGSSISLL THCGVHVNAG PEIGVASTKA
YTSQFIAMIM FALSLSEDRA SKQKRREDIM EGLGKISEQI KEVLKLDKTI KDLCARTFKH
QKSLLLLGRG SQYSTALEGA LKIKEISYLH CEAVMSGELK HGVLALVDED LPIIMIMTRD
EIFAKSLNAY QQVIARGGKP IVICNPADPE FKEGQAEKIE IPKTVDCLQG LLNVIPLQLM
AYWLAVAEGL NVDFPRNLAK SVTVE
//
