ID GOB1_BRUMA Reviewed; 492 AA. AC A8NS89; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 25-MAY-2022, entry version 64. DE RecName: Full=Trehalose-phosphatase; DE EC=3.1.3.12 {ECO:0000269|PubMed:24992307}; DE AltName: Full=Trehalose-6-phosphate phosphatase {ECO:0000303|PubMed:24992307}; DE Short=TPP; GN ORFNames=Bm1_08695; OS Brugia malayi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17885136; DOI=10.1126/science.1145406; RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E., RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T., RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L., RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M., RA Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J., RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F., RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W., RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M., RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J., RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E., RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G., RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B., RA Blaxter M.L., Scott A.L.; RT "Draft genome of the filarial nematode parasite Brugia malayi."; RL Science 317:1756-1760(2007). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, CATALYTIC RP ACTIVITY, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF ASP-213; ASP-215; TYR-221; RP SER-329; GLN-332; LYS-334; ASP-336; ARG-337 AND GLU-386. RX PubMed=24992307; DOI=10.1371/journal.ppat.1004245; RA Farelli J.D., Galvin B.D., Li Z., Liu C., Aono M., Garland M., RA Hallett O.E., Causey T.B., Ali-Reynolds A., Saltzberg D.J., Carlow C.K., RA Dunaway-Mariano D., Allen K.N.; RT "Structure of the trehalose-6-phosphate phosphatase from Brugia malayi RT reveals key design principles for anthelmintic drugs."; RL PLoS Pathog. 10:E1004245-E1004245(2014). CC -!- FUNCTION: Catalyzes the hydrolysis of trehalose 6-phosphate to CC trehalose and phosphate; prevents the accumulation of toxic levels of CC trehalose 6-phosphate. {ECO:0000269|PubMed:24992307}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha- CC trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12; CC Evidence={ECO:0000269|PubMed:24992307}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:24992307}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24992307}; CC -!- ACTIVITY REGULATION: Inhibited by trehalose 6-sulfate. CC {ECO:0000269|PubMed:24992307}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=360 uM for trehalose 6-phosphate {ECO:0000269|PubMed:24992307}; CC Note=kcat is 24 sec(-1) for trehalose 6-phosphate. CC {ECO:0000269|PubMed:24992307}; CC -!- SIMILARITY: Belongs to the gob-1 trehalose phosphatase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS237867; EDP37955.1; -; Genomic_DNA. DR RefSeq; XP_001893209.1; XM_001893174.1. DR PDB; 4OFZ; X-ray; 3.00 A; A=1-492. DR PDB; 5E0O; X-ray; 3.00 A; A=1-492. DR PDBsum; 4OFZ; -. DR PDBsum; 5E0O; -. DR AlphaFoldDB; A8NS89; -. DR SMR; A8NS89; -. DR STRING; 6279.A8NS89; -. DR BindingDB; A8NS89; -. DR ChEMBL; CHEMBL4105873; -. DR EnsemblMetazoa; Bm4641; Bm4641; WBGene00224902. DR GeneID; 6096670; -. DR KEGG; bmy:BM_BM4641; -. DR CTD; 6096670; -. DR WormBase; Bm4641; BM04374; WBGene00224902; Bma-gob-1. DR HOGENOM; CLU_033472_0_0_1; -. DR InParanoid; A8NS89; -. DR OMA; CGRYRSS; -. DR OrthoDB; 766517at2759; -. DR BRENDA; 3.1.3.12; 997. DR Proteomes; UP000006672; Unassembled WGS sequence. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:UniProtKB. DR GO; GO:1901136; P:carbohydrate derivative catabolic process; IDA:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB. DR GO; GO:0005992; P:trehalose biosynthetic process; IDA:UniProtKB. 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; PF18572; T6PP_N; 1. DR SUPFAM; SSF56784; SSF56784; 1. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Reference proteome. FT CHAIN 1..492 FT /note="Trehalose-phosphatase" FT /id="PRO_0000385170" FT REGION 1..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 332..334 FT /note="Substrate binding" FT /evidence="ECO:0000303|PubMed:24992307" FT COMPBIAS 13..39 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..55 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 215 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000303|PubMed:24992307" FT METAL 213 FT /note="Magnesium" FT /evidence="ECO:0000269|PubMed:24992307" FT METAL 215 FT /note="Magnesium; via carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:24992307" FT METAL 424 FT /note="Magnesium" FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 213 FT /note="D->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 215 FT /note="D->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 221 FT /note="Y->A: Reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 329 FT /note="S->A: Reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 332 FT /note="Q->A: Strongly reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 334 FT /note="K->A: Strongly reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 336 FT /note="D->A: Strongly reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 337 FT /note="R->A: Strongly reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT MUTAGEN 386 FT /note="E->A: Reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:24992307" FT HELIX 65..87 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 94..107 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 131..151 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 159..165 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 168..172 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:5E0O" FT HELIX 180..204 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:4OFZ" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 232..245 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 247..252 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 257..261 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 270..278 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 289..292 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 300..316 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:5E0O" FT STRAND 335..341 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 351..364 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 376..378 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 381..388 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:5E0O" FT HELIX 398..408 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 419..425 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 426..428 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 429..438 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 440..442 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 444..449 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 452..461 FT /evidence="ECO:0007829|PDB:4OFZ" FT STRAND 465..473 FT /evidence="ECO:0007829|PDB:4OFZ" FT HELIX 474..490 FT /evidence="ECO:0007829|PDB:4OFZ" SQ SEQUENCE 492 AA; 55119 MW; A07618B5C47178E5 CRC64; MTETVTDQGK QRSSKLQKNE AAKDEQVEGK GKETLESGTD KSAEQNSSLL VGQPDVIDND NVQTVDDFKN LMYKMQETRR AIVFALLNEK DLTKDDVEIL KRAYEKLTDN QTHSFQREMC TLTTKLSVNI GDETRGLEKD LKYLDALMNI RREEPNLLWP IIMSRVDLFS ILANYHPKGK ETFLKEYEDT VKFLKTFISS EAITGKKPIF ITDWDGTMKD YCSQYATNLQ PVYSAVGMTR FAASFTRISA VLTAGPLRGP GILDLTAMPI DGPVMFSGSW GREWWLSGKR VVHQDGITDE GFNALQRLDD EMKDLLHTSD YAPFALVGSG VQRKVDRLTL GVQTVCHHVT SELSNRYQMA VKERMHRVDP NSQILVFDPS TELEVEVVAH NSGIIWNKGN GVERLIKSLG DSLQSPGKIL ICGDTLSDIP MVRQAVKQNP DGVLAIFVGA KMSLREEVKQ VIGDESRCCF VSCPDVIHAA MSQILNEHCI GK //