ID   TPS1_CAEBR              Reviewed;        1374 AA.
AC   A8WRG3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1;
DE            EC=2.4.1.15;
DE   AltName: Full=Trehalose-6-phosphate synthase 1;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase 1;
GN   Name=tps-1; ORFNames=CBG01861;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Catalyzes the production of trehalose from glucose-6-
CC       phosphate and UDP-alpha-D-glucose in a 2 step process. {ECO:0000250}.
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 gob-1 trehalose
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; HE601451; CAP23071.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8WRG3; -.
DR   SMR; A8WRG3; -.
DR   STRING; 6238.CBG01861; -.
DR   WormBase; CBG01861a; CBP40035; WBGene00025041; Cbr-tps-1.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_007752_0_0_1; -.
DR   InParanoid; A8WRG3; -.
DR   OMA; HYLAMDI; -.
DR   OrthoDB; 772297at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
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; IPR041064; T6PP_helical.
DR   PANTHER; PTHR10788; PTHR10788; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF18572; T6PP_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1374
FT                   /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT                   forming] 1"
FT                   /id="PRO_0000385175"
FT   REGION          28..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1352..1374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1374 AA;  155650 MW;  9409B98090517A87 CRC64;
     MVQQLQKSMS DGMATTAAAV PMNANGVDTG KVPTAPPDVF FSTENEPEDC TPVKMDPFDR
     PKSDKDPVED AIERLLKVME KIDCPYTPGK EKGVDQDESD DMTESEDHDE MAKDDEGIPA
     NEVRVETRKM DCTTGQLVAP RIYEKVDTLS STSESSAEED ESMMIIKEGI RVCYGVWKKR
     QKNSEMALKG LAIVLELCLT QPSARDEIFS VLLETLGFNT VTYWKAVVPQ VVDSDLTYAT
     QYREALLFSM CLYDVNHSKN RLRELYAAIP GFRQSMLGIR AKQFTERYRH LQMKIARSRQ
     SSRMSSKYGS EDNIQAMVTL ANDVIMDEET APTQMPLVDM SHDKQRVINV SNAPPVSISR
     KTSGSWEIKQ GSGGLVACVD PVMSADKKNI WLSNLGVNMQ EELKEHSTTT NSIGLPLIKQ
     ACAGEVFCVL ERNEKKELTP KQQAVESDMS LLSVLNTYNK HSYQLNPVVV NQDDYDTYYG
     GISNGLLWPA LHNLPQFISP CYNDPEALRE QWCAYVRVNY LFSINAARNS RAQDFIWIHD
     YHLMLCGQIM RSLEGSLDVS SIEEREGKQK ESLQIGFFLH IPFQPPANFM TKYRTVGEPI
     VRALLRFTKV GFQTSRDRET FVKLVADHIK RTKIDYDSRL DRYTIEHDGF ACSLGVFPVS
     IKIADFVNIA KNPQTVIEAE EIRKQIMGKC ADGGQLFFSV ERFDYTKGIA EKLRAWQRYF
     EKYPDRIGKD VLFQVAVTNR RSVESYRQYQ DDVMALAELI NQKFHSEQYP EWKPVIFETD
     GLPRSRLIAH YLAMDIGVVT PSKDGMNLVA KEMLVCNPTA SLVLSTGAGT EVQLSNAQFY
     SEQEGKCYHR VEDIANTEAF ADNFFAAATE SKETRNKHGE KINQFLCVHD IDEWSDQFLD
     PKWTHEVISE CEVKQLGQFY GLMNRTAQVR RQIVECVLKG LPIRPHFKFS LENAKVTRQA
     NDSECTTLTS LETSCPEGTS KLTLEADEES GEEKGFKITY DIHDELSEME KDLAFLSFIQ
     SDEYENAEEF IKTIGSFYEG GPILFSEEVK QAAEMLQRGI HYNTFFTDRD GTLKSYACSY
     PTSVQPAYSA VIQAQFARRC ATFCAIVTTA PLIHTGILEV ATIPEGYYAY GASAGREWYL
     NPAQQFKDRS FSAVDLTLMN KVFELIEELL EKPEFRTFKW IGSGIQKHCG HITIAKQDVN
     GTIPARKVTR LHEQLVKIVN DFDPTGTTLT MRESDLDFKI YVKAKLKGRI FNKGHGIRLV
     KERLKPNMSK GSCLVCGDSE SDIPMLEECL KLAGSKVYTI WVTRDQALQE KVSQLCERYS
     CTNIHYVTCP QVLLGAMAYA TAHTLTNEKN RKADSYYDDS DTPMDQEDTP SKQQ