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Database: UniProt
Entry: C1H2Q7_PARBA
LinkDB: C1H2Q7_PARBA
Original site: C1H2Q7_PARBA 
ID   C1H2Q7_PARBA            Unreviewed;       504 AA.
AC   C1H2Q7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Trehalose-6-phosphate synthase {ECO:0000256|RuleBase:RU362045};
DE            EC=2.4.1.15 {ECO:0000256|RuleBase:RU362045};
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000256|RuleBase:RU362045};
GN   ORFNames=PAAG_05050 {ECO:0000313|EMBL:EEH34001.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH34001.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH34001.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC         trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001516,
CC         ECO:0000256|RuleBase:RU362045};
CC   -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000256|RuleBase:RU362045}.
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DR   EMBL; KN294004; EEH34001.2; -; Genomic_DNA.
DR   RefSeq; XP_015699683.1; XM_015845457.1.
DR   AlphaFoldDB; C1H2Q7; -.
DR   STRING; 502779.C1H2Q7; -.
DR   GeneID; 9096156; -.
DR   KEGG; pbl:PAAG_05050; -.
DR   VEuPathDB; FungiDB:PAAG_05050; -.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_7_2_1; -.
DR   OMA; RTIWPLF; -.
DR   OrthoDB; 1023at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR012766; Trehalose_OtsA.
DR   NCBIfam; TIGR02400; trehalose_OtsA; 1.
DR   PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU362045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
FT   REGION          481..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  56539 MW;  52057992FF09BAE0 CRC64;
     MMPGCSLFPN RLPITIKRSD DGKYEFSMSS GGLVSGLSGL SKSTTFQWYG WPGLQVPEDE
     ILLLKKRLAE EYDAVPVLID DNLADKHYNG FSNSILWPLF HYHPGEITFD ESAWFAYRDA
     NRLFAKAIAN DVKDGDLVWV HDYHLMLLPA MLREEIGTSK KNVKIGFFLH TPFPSSEIYR
     ILPVRNELLL GVLHCDLIGF HTYDYARHFL SSCSRILGLS TTPNGVEFQG KVIAVGAFPI
     GIDPDKFSEG LKKEKVQKRI AALEQKFQGV KLMVGVDRLD YIKGVPQKLH ALEVFLTDHP
     EWIGKVVLVQ VAVPSRQDVE EYQNLRAVVN ELVGRINGKF GTVEFMPIHF MHKSVNFDEL
     IALYAVSDVC VVSSTRDGMN LVSYEYIATQ KKRHGCLVLS EFAGAAQSLN GSIIVNPWNT
     EELANAFQEA VTMSDEQRAL NFSKLDKYVS KYTSAFWGQS FVSELTRISA HGEKKLRLRN
     TSAIPSDLSH GKENDIPPAT PDGN
//
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