TPSB_DICDI
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 03-AUG-2022, entry version 96.
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 (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).
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.DDB0231987; -.
DR PaxDb; Q54NU9; -.
DR PRIDE; Q54NU9; -.
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; HINPWDM; -.
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: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; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
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; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 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
