ID   H6BXD6_EXODN            Unreviewed;       935 AA.
AC   H6BXD6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Alpha,alpha-trehalose-phosphate synthase (UDP-forming) {ECO:0000313|EMBL:EHY55366.1, ECO:0000313|EMBL:EHY55367.1};
GN   ORFNames=HMPREF1120_03506 {ECO:0000313|EMBL:EHY55366.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY55366.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY55366.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY55366.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; JH226132; EHY55366.1; -; Genomic_DNA.
DR   EMBL; JH226132; EHY55367.1; -; Genomic_DNA.
DR   RefSeq; XP_009155827.1; XM_009157579.1.
DR   RefSeq; XP_009155828.1; XM_009157580.1.
DR   STRING; 858893.H6BXD6; -.
DR   GeneID; 20308145; -.
DR   VEuPathDB; FungiDB:HMPREF1120_03506; -.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_3_0_1; -.
DR   OMA; PRSDDWE; -.
DR   OrthoDB; 1023at2759; -.
DR   Proteomes; UP000007304; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   CDD; cd01627; HAD_TPP; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; TIGR00685; T6PP; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR10788:SF123; TREHALOSE-PHOSPHATASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  105149 MW;  57C4703A6E590025 CRC64;
     MPNSPEDVVK SLRQEYQENP PSSTALETAA PTNPSLQRAP TSYFSVPRRE APEKPAEKPP
     APALESPANV VKGADTGKEL LRRLSLVDHK DAEALDVDPR TAYPSLRLSG NVISATFCIP
     YQLTHGPQGE WGLSNRRGTS ALFDSFRHLS SDKTPWNHTL VGWTGEIQTQ PETTTGSILE
     GDGGASTPTQ SAGPTQTNAP INKSAAPYPV DGMPNQQNPH GDHLRISRAE RNRLEKILAH
     HPNGRAVPVW MPDTQSDENG DFIFKDQSRW RKYAEHELYT LFHYRQHGPD DGRAEKTSWA
     DYVQLNQAFA DRILHIYQPG DIVWIHDYHL MLLPSMLRQR IPNIYIGFFL HIPFPSSEYM
     RCLPRRKDVL TGALGATMIG FQAYSFSRHF NSCCKRILGF ESSSAGVDAY GAHVAVDVFP
     IGIDVSAVQK AAFMDPVIEQ KMKALRQLYA GKKIIVGRDR LDTVRGVAQK LMAFEIFLER
     YPEWREKVVL IQVTSPTSVM EEKVDGAHKI EHHISNLVSR INGQYGSLSH APVQHYPQYL
     SSQEYFALLR VADAALITSV RDGMNTTSLE YVICQKDNHG PLILSEFSGT AASLGNAIHI
     NPWDLVGVAR ALKYALEMPE EKKKSDHEKL YNYATTHTVA TWTNNFLKRL LTNLTSFSQN
     DLTPALDRNL MIQQYNKAQK RLFMFDYDGT LTPIVKDPNA AIPSDKVLRT LKALAADPRN
     NVWIISGRDA SFLEEWMGHI TELGLSAEHG CFMRRPGSEQ WENLAASMDM GWQKEVMDIF
     SYYTERTQGS WIEKKRVALT WHYRQADPDF GEFQAKECRK ALEENVMKNW DVEVMAGKAN
     LEVRPQFVNK GYIATRLINE YGYAGGNPPD FVLCLGDDQT DEDMFRALLK TNLPKENVFA
     CTVGASSKRT LATWHLLEPS DVIASIAALI KQENL
//