ID   TPSB_DICDI              Reviewed;         790 AA.
AC   Q54NU9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] B;
DE            EC=2.4.1.15;
DE   AltName: Full=Trehalose-6-phosphate synthase B;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase B;
GN   Name=tpsB; ORFNames=DDB_G0284975;
OS   Dictyostelium discoideum (Social amoeba).
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).
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   -!- 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; AAFI02000073; EAL64951.1; -; Genomic_DNA.
DR   RefSeq; XP_639968.1; XM_634876.1.
DR   AlphaFoldDB; Q54NU9; -.
DR   SMR; Q54NU9; -.
DR   STRING; 44689.Q54NU9; -.
DR   PaxDb; 44689-DDB0231987; -.
DR   EnsemblProtists; EAL64951; EAL64951; DDB_G0284975.
DR   GeneID; 8624879; -.
DR   KEGG; ddi:DDB_G0284975; -.
DR   dictyBase; DDB_G0284975; tpsB.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_3_3_1; -.
DR   InParanoid; Q54NU9; -.
DR   OMA; PRSDDWE; -.
DR   PhylomeDB; Q54NU9; -.
DR   PRO; PR:Q54NU9; -.
DR   Proteomes; UP000002195; Chromosome 4.
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: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   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:SF16; ALPHA,ALPHA-TREHALOSE-PHOSPHATE SYNTHASE [UDP-FORMING] B; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 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   Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..790
FT                   /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT                   forming] B"
FT                   /id="PRO_0000328411"
SQ   SEQUENCE   790 AA;  90775 MW;  EA8E23A53F6DADB7 CRC64;
     MTIIQRSTSL NNIINEKLGK IIVASNTLPI TVTKFNETPL FGSPLSASRE SITSSFGMSE
     PSRDRESKIQ IQINGHPFPT QSALETLKAK DEIEDWLWIG WSHCEVNEDE EPMLNQAIKE
     FSPHFEHVFL NPRQFENYYK GYCKNGLWLL LHYQMNFIRM QSEWWEEYVG VNQMFAEKIA
     SVWRPSDIIW IHDYHLMLVP QMLRQLLPPE ASIGFFFHAP FPSYELFRIL PNRKELLKGI
     LSSNLIGFQS FEYVRHFKSS CARLLDLEVH PKGLEIFEDG STHFTKLQVY PIGVDYNDFA
     KNLNLPEVSS RVESLRKIFK GKKVVVARDR LDQIEGVPRK LEVFEQLLND HPEYIGKLVF
     IQIYEPTVEE GDETDEQKIL HKTVNEMVGR INGKFGKLSF NPIEYINKKI SYEELSALYK
     LADIALITPI RDGMNLTSHE YVVCQKDNFG VLILSEFAGA ARCLGGSIIV NPFSKKEIME
     AIIEALNMSM HDRKLKHQIN YNYVLANTSS FWGKRFLCDL NEATQKEIME TSVPRANFQE
     IEDSYKKAKV RVFFLDYDGT LTPLVRLPSQ AMPSKQLIDV LSKLTEDRRN EVYVISGRDR
     SSLEKWLGHL PIGMSCEHGV FTRQPGENQP WTESPNAEVQ WKDTVLSIMQ DFEDRTPGSM
     TETKQVNITW HYRNADPDFG QFQAKELIAQ LRSVANKYPL DILSGKKAIE VKPIGINKGE
     IVKMILQKID ADFILCIGDD KTDEDMFKAL YNVPSFTIRV CGDLEESTKA RGVVESSSEV
     LTLLNRLSLS
//