ID   TPSA_DICDI              Reviewed;         733 AA.
AC   Q54K57;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] A;
DE            EC=2.4.1.15;
DE   AltName: Full=Trehalose-6-phosphate synthase A;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase A;
GN   Name=tpsA; ORFNames=DDB_G0287657;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=159657; DOI=10.1016/0003-9861(79)90558-7;
RA   Killick K.A.;
RT   "Trehalose 6-phosphate synthase from Dictyostelium discoideum: partial
RT   purification and characterization of the enzyme from young sorocarps.";
RL   Arch. Biochem. Biophys. 196:121-133(1979).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=NC-4;
RX   PubMed=11553701; DOI=10.1091/mbc.12.9.2590;
RA   Iranfar N., Fuller D., Sasik R., Hwa T., Laub M., Loomis W.F.;
RT   "Expression patterns of cell-type-specific genes in Dictyostelium.";
RL   Mol. Biol. Cell 12:2590-2600(2001).
CC   -!- FUNCTION: Synthesizes trehalose 6-phosphate, the precursor for the
CC       production of trehalose, the main carbohydrate storage reserve of the
CC       dormant spore. Trehalose accumulates in both prestalk and prespore
CC       cells and then is rapidly metabolized during terminal differentiation
CC       of stalk cells, while being stored in spores, where it serves as the
CC       principal energy and carbon source for germination.
CC       {ECO:0000269|PubMed:159657}.
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   -!- DEVELOPMENTAL STAGE: Expressed during aggregation, reaching a peak at
CC       12-16 hours. Accumulates in prestalk cells and, to a lesser extent, in
CC       prespore cells as well. {ECO:0000269|PubMed:11553701}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 20 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; AAFI02000103; EAL63637.1; -; Genomic_DNA.
DR   RefSeq; XP_637107.1; XM_632015.1.
DR   AlphaFoldDB; Q54K57; -.
DR   SMR; Q54K57; -.
DR   STRING; 44689.DDB0231979; -.
DR   PaxDb; Q54K57; -.
DR   EnsemblProtists; EAL63637; EAL63637; DDB_G0287657.
DR   GeneID; 8626202; -.
DR   KEGG; ddi:DDB_G0287657; -.
DR   dictyBase; DDB_G0287657; tpsA.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_3_3_1; -.
DR   InParanoid; Q54K57; -.
DR   OMA; WINGMNT; -.
DR   PhylomeDB; Q54K57; -.
DR   PRO; PR:Q54K57; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IBA:GO_Central.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProt.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR012766; Trehalose_OtsA.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   PANTHER; PTHR10788; PTHR10788; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
DR   TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..733
FT                   /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT                   forming] A"
FT                   /id="PRO_0000328410"
SQ   SEQUENCE   733 AA;  83717 MW;  C15766757DE3E081 CRC64;
     MNENDNNLEN ETGFSGRLIV VSNRLPVSIK KESNGKWSCK MSSGGLVAAL SGLKSNFIWV
     GWIGAEIEED DRKEIKELLW KDYSCIPVFL SEKVANEHYN GFSNGVLWPL FHYLPGDLDY
     DDRIWNSYVE ANEQFSSVVA EILKPNDLVW VHDYHMMLLP EILKQKKPDA RIGFFLHIPF
     PSSEIFRVLP CRKEILLGIL NCCLIGFHTY DYARHFLKSC TRIVGLETAP NGVYFKDRFV
     QVGVFPVGID PDKFFESLKT TQVQNRIKEL KESFEGTKVL IGIDRLDYIK GIPQKLQAIE
     RLFQKYPEWK GKLVLIQVAV PSRQDVEEYQ KLKKEVEELV GRINGLYGSI GYSPIHYLFQ
     SVDPSELTAL YNISDAALIT SIRDGMNLVA QEYIVCQTEN NGVLILSEFT GAAQSLSGAV
     MINPWNTEEV ADSIHNSLLM PPEEREEKHQ MLLKYVTKHT ASHWGLGFVK ELNKASSNTD
     KMVTIQKLDI EKVVDIYKQS KRRLLIFAYD GTLIPYNNVP QLSRPSQELL NSFDILSNDP
     KTDVYILSGR DKKTLSEWFL GIQIGLSAEY GCFFKLPEST EWEQQVPSMD LSWKETIRPL
     FKYFTLRTPG SFFEEKEMLF TWHYRNADPI FGSIQARELH LHLDNLPLDV IVGDKTLGVR
     SYNINPLSSM KKVITDTIPK GLDLILLIGD THIHPSELPT FDGKIFNISV GKKSVKDSYH
     LSDPAEVNYL IIN