ID D8LRB5_ECTSI Unreviewed; 991 AA.
AC D8LRB5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Trehalose 6-phosphate synthase, family GT20 / Trehalose 6-phosphate phosphatase {ECO:0000313|EMBL:CBN75020.1};
DE EC=2.4.1.15 {ECO:0000313|EMBL:CBN75020.1};
GN Name=TPS {ECO:0000313|EMBL:CBN75020.1};
GN ORFNames=Esi_0064_0072 {ECO:0000313|EMBL:CBN75020.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN75020.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN75020.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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; FN648863; CBN75020.1; -; Genomic_DNA.
DR AlphaFoldDB; D8LRB5; -.
DR STRING; 2880.D8LRB5; -.
DR EnsemblProtists; CBN75020; CBN75020; Esi_0064_0072.
DR InParanoid; D8LRB5; -.
DR OrthoDB; 1023at2759; -.
DR Proteomes; UP000002630; Chromosome LG16.
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 CDD; cd01627; HAD_TPP; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
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:SF106; BCDNA.GH08860; 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 Glycosyltransferase {ECO:0000313|EMBL:CBN75020.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Transferase {ECO:0000313|EMBL:CBN75020.1}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 991 AA; 109115 MW; B154B73263B16E17 CRC64;
MAPVEVHSTE HSAHEAPLPP DTRAPTLTSV IAKHAGEREA TDFLASAKAV MPPGGKVPEV
FTHSPEVVGE KEVQTGIEAL DVAEQFHCRL ACTCCSRSLW AMITGNRWFR WDRAGKFWLV
FRSFSGSCGS TRTRRTREMK TGRSRGARSE LDYEESGAEQ SREKSRVVVV SNRLPISAQR
NLETGKWTFK MSSGGLVTAL QGVRHEMDFM WIGWMGVEVE EAERDGDHVW VHDYQLMQVP
YELRKLHPNC RVAWFLHTPF PSSEIYRILP VRKQLLQGLL AADLVGFHTY DYARHFLSAC
RLSAPQEASE LNNRFMSLGV YPIGIDPDHV AKTLRKPWVQ NRIKELSETF AGRKILLGVD
RLDYIKGMPH KLLGLELFLN RYPDWRGKVT LIQVGVPSRT EVAEYRDLGS QVNELVGRIN
GNYGTLEYSP VHYINQSISQ DELFAIYNVA DVCLVTSVRD GMNLVSHEYV AAQSEPRHPL
TVTGDGGAPA TRVNDDGPGV LILSEFAGSA QSLSGALALS RVERELRQHK LYRYVVVHTA
AFWAKSFMHE FREVCDGQQE STRKLPTLPI KEVLEAYKKA KNRLIISDYD GTLTTLQSLP
QLAGPPAVVT NFLDSLCRDY KNRLFIISGR ERRFMDTWLG KLRAGLAAEY GFYYRLPEAT
QWQCSGQDLD LSWKDVVRPI MQYFTERTPG TYIENKESSL TWHYRDADPH FGLWQAKDMQ
IHMEDVLSNL PLEILQGNRM VEVRHQAANK SMVAEEVLKL LSTEQSVRQR GEVDFILCVG
DDRSDEDMFQ TVKRFRDLAK EAPTPVLSED EDGMPFSDGP PGSGEMDQGV GSGSVASSGQ
GMAMVGVNRK MAGNAAVYTV HIGLEHSHAD YYLENLRKLR ELLMKFDEMS TEERGGGGGG
GGGGESTGVP RRASAVGPSG GGGLGLGLGL GLGADNGGDD GGPSAAAPGV KKGDGGGGGG
GGGGGGKGSN LPSPRRNTCP SPSTPAPGAL R
//
