ID   TPS2_CAEEL              Reviewed;        1229 AA.
AC   O45380; Q7YZT5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 3.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 2;
DE            EC=2.4.1.15;
DE   AltName: Full=Trehalose-6-phosphate synthase 2;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase 2;
GN   Name=tps-2; Synonyms=tps2; ORFNames=F19H8.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Bristol N2;
RX   PubMed=13678635; DOI=10.1016/s0020-7519(03)00173-5;
RA   Pellerone F.I., Archer S.K., Behm C.A., Grant W.N., Lacey M.J.,
RA   Somerville A.C.;
RT   "Trehalose metabolism genes in Caenorhabditis elegans and filarial
RT   nematodes.";
RL   Int. J. Parasitol. 33:1195-1206(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=15935281; DOI=10.1016/j.biochi.2005.01.010;
RA   Goyal K., Browne J.A., Burnell A.M., Tunnacliffe A.;
RT   "Dehydration-induced tps gene transcripts from an anhydrobiotic nematode
RT   contain novel spliced leaders and encode atypical GT-20 family proteins.";
RL   Biochimie 87:565-574(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the production of trehalose from glucose-6-
CC       phosphate and UDP-alpha-D-glucose in a 2 step process.
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 in all development stages.
CC       {ECO:0000269|PubMed:13678635}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:13678635}.
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 gob-1 trehalose
CC       phosphatase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD54507.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ512333; CAD54507.2; ALT_FRAME; mRNA.
DR   EMBL; AJ811574; CAH18872.1; -; mRNA.
DR   EMBL; Z93378; CAB07584.3; -; Genomic_DNA.
DR   PIR; T21127; T21127.
DR   RefSeq; NP_497035.3; NM_064634.5.
DR   AlphaFoldDB; O45380; -.
DR   SMR; O45380; -.
DR   BioGRID; 532368; 1.
DR   STRING; 6239.F19H8.1a.1; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   EPD; O45380; -.
DR   PaxDb; 6239-F19H8-1a; -.
DR   PeptideAtlas; O45380; -.
DR   EnsemblMetazoa; F19H8.1a.1; F19H8.1a.1; WBGene00006603.
DR   GeneID; 3565050; -.
DR   KEGG; cel:CELE_F19H8.1; -.
DR   UCSC; F19H8.1; c. elegans.
DR   AGR; WB:WBGene00006603; -.
DR   WormBase; F19H8.1a; CE37507; WBGene00006603; tps-2.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_007752_0_0_1; -.
DR   InParanoid; O45380; -.
DR   OMA; ANDIERW; -.
DR   OrthoDB; 1023at2759; -.
DR   PRO; PR:O45380; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006603; Expressed in larva and 3 other cell types or tissues.
DR   ExpressionAtlas; O45380; baseline and differential.
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   Gene3D; 1.20.58.1800; -; 1.
DR   Gene3D; 3.30.70.3080; -; 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; IPR023214; HAD_sf.
DR   InterPro; IPR049063; T6PP_C.
DR   InterPro; IPR041064; T6PP_helical.
DR   PANTHER; PTHR10788:SF110; ALPHA,ALPHA-TREHALOSE-PHOSPHATE SYNTHASE [UDP-FORMING] 2; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF21141; T6PP_C; 1.
DR   Pfam; PF18572; T6PP_N; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1229
FT                   /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT                   forming] 2"
FT                   /id="PRO_0000385177"
FT   REGION          196..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1229 AA;  139911 MW;  707A48DA05E6383D CRC64;
     MGSEPPPSEK KVREPFSRAM KDVQISDEQR LKELWHLLDL LEIEYKKTAD LHTLISSVSE
     SLTMVWKRRD PKSELALKGL LLILEYCLSH VFDGHAVFEI FVSSLGFNTV IFWKHCAGYI
     FDSDLGRGTK FRDALLFSLT LYDVNTGKNR LRELYAAVPG IRKSLLGVNA KQFGERYHHL
     QKRLARYGSH TSLCSVSSDS EGEEAIHNVR SGTHTESESE EDPKAPRSGL ATSHFQQRVI
     NVSNAPPVSL KREKTGDWEI KQGSGGLVAC VDPVMSKDHE NLWLANLGMN INDKKQKRPG
     SVASIPESFP STNTLGLPLI KQTIAEVFFH VLADDDMDAP KNEKQKKARE EMSLLGVLNN
     YNRGNYKLNP VVVQEDDYNV YYGGISNGLL WPALHNLPEY IVSEYDDEKI LRAHWCAYVR
     VNYQFAIDAV RNSRPQDFIW IHDYHLMLVG MIMQSLDQHL EVGFFLHIPF QPPGEFFSKY
     STVGFAVLRG LLRFTKVGFQ THRDRTKYIE LVQHYFGTAK IVYDNKMDIY SITNEGWTCS
     LGVFPVSIKN DDFLKFVDLP ETIKLKNDLR KRVMGDTPAP DGRFFFSVER FDYTKGIMEK
     LQAYKRYFER HPDRIGKDVL FQIAVTNRRS VDTYRVYQDE CIDLADKINE IFKDPNNPTW
     KPLVFQTDGL PRSELVAAYL AMDIGVVTPK KDGMNLVAKE MLVCNPKAGL VLSTGAGSEI
     QFTTAGLYSD KEKNYHRISN VFDPDSYCDA FYSAALEPED VRAEHGKRLH EFIMANDIER
     WSCAFLDPSW THEVIRPTQV ETLDDFFSLM MKTRNVRRQI VGRVLKGIPI RSHFAISLRN
     AKESLEQICK PGTHTAEFKS GPDSKEVAHF EIDNELQEFE RDLSFIDYVQ SDDADNVEQF
     VDTLISSHPI SVETYKKEVE NAVELLYSAD HFHYFFTDRD GTLKSYSCSY PSSIQPAYSG
     VIQAQFARRC AQTCVILTTA PLMHIGVLDV STIPNGYYYF GASGGREWFI DNGHNFKDES
     ILKGEKADVL ASAYTRISHL LEEPEFRPFT WVGSGLQKHY GHLTIAFQDV YKTITEAQGK
     QLHEEIEKIV KDVDPHGTRL QLASTEFDIK VYMKTETDGH VFDKGDGLRL LCEKMHCDLT
     EGNVLVCGDS STDIPMLKEC LIRNPKGVYT IWVTVNDKLK EEVRALCASY SNSNVAFVSC
     PEVLLGAMAQ ATIREITITR TRKMSRNIV
//