ID A0A395RYU0_FUSSP Unreviewed; 1309 AA.
AC A0A395RYU0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE SubName: Full=Trehalose 6-phosphate synthase {ECO:0000313|EMBL:RGP65326.1};
GN ORFNames=FSPOR_7347 {ECO:0000313|EMBL:RGP65326.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP65326.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP65326.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP65326.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000256|ARBA:ARBA00006330}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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:RGP65326.1}.
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DR EMBL; PXOF01000103; RGP65326.1; -; Genomic_DNA.
DR STRING; 5514.A0A395RYU0; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR CDD; cd01557; BCAT_beta_family; 1.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR NCBIfam; TIGR01123; ilvE_II; 1.
DR NCBIfam; TIGR00685; T6PP; 1.
DR PANTHER; PTHR10788:SF15; TREHALOSE SYNTHASE COMPLEX REGULATORY SUBUNIT TPS3-RELATED; 1.
DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 19..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1309 AA; 145889 MW; 2F780978502AC3DA CRC64;
MTVFVCSLFL PKTIHFTLPG TPPPGVDPAR TSLSGSSNIN LAGDTRASLS GGSAPKGGAA
LPPKPVAPVG GRPAPLNRQP SLFQKDDITP PRTPTEEVDV NLFANEDGIR IPFPKRPGSN
AGSGKPWGSR ANQPKSRASS PPPPALSENN RTMQKARELG RQGVIQPKPL VRSDSHDRVF
ASAGWMVVNA DQGNGGLRNA ADAAARDGKI DEITWVGTLG MPTDALDGTE QKQDIEDTLA
NEHNMLTVFC SDKDFDGHYA HFCKHILWPV FHYQIPDNPK SKAYEDHSWK YYVNVNQAFA
DQIVKNWKRG DVVWIHDYHL LLVPGMVRKK IPEAKIGFFL HVAFPSSEVF RCLAVRKELL
EGMLGANLVG FQIHEYGRHF LQTCSRILNA EATPDGLQLE DRFVDVIHLA IGIDPVSLRE
HLDAPEVAKW LQIMQERYKG KRLIVARDKL DHVRGVRQKL LSYELFLNKN PQWRENTVLI
QVALSSSEKS DLEATVSDIV TRVNSSWANL AYQPVVYLKQ DIDYAQYLAL LTIADALMIT
SQREGMNLTS HEYLFCQDGK LLPEKKHGSL ILSEFTGTSS LFAKNELAVN PWDYRACADA
IKQALEMGEE EKDQRWNNLY GRVIKHTGAH WFTEFLSRLD IVYDEQHKRD QTSVPRLSIP
ALSTKYTKAQ RRLFIIDYED TLVAWGPVNQ IIPISPQRTL DVLNDLLLDE RNTVYVMSGR
RPEELDRVFR RVPNLGLIAE NGCFLKSHGD DSWTEMADLD HVKDWKESVR PIMTYFLERT
PGAEIEERRC SLIFHYKSAE DYETASRQAS DCASHVNDAC ESQRVHAIAL DGCIAVEPID
WTKRTAARKV FETLKEEIHP TKEQKMPVDF LMVIGDGRED EKVFKWANRL QDDGSVENVV
TVSLGNRNTE ATATLTQGVS VSISISSARM TAFPPPPVNT IDWSNVGFKV REVNGHVEAT
YSRSTGKWTP LRFVADPFMR IHGMAPALNY GQQAYEGLKA FRTPNDEAIT IFRPDRNAKR
LQHSAEVVSM PSVPEDLFLS AVRAAVALNA EYVPPHETGA ALYIRPQLYG SSAQLGLSPP
DEYIFAVFVI PTGVYHGAHP VKALILEEFD RAAPHGTGNA KVGGNYAPVL RWSDKARDEG
YGITLHLDSV RHEEIDEFST SGFLGVKVNG DDVTLAVPDS KNVIDSVTSD SIQELGRSYG
WKVEKRAIKY GELQEFSEVF AAGTAAALVP IRSITRRVDG KEEIATYIKE GSEEPGPLFE
KLLKHLKDIQ LGRAEDSFSW RFPVGAKDKE IQGASTGGDG DATTVDQMD
//
