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 02-NOV-2016, entry version 40. 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; Spirurida; OC 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., RA Allen J.E., Delcher A.L., Guiliano D.B., Miranda-Saavedra D., RA Angiuoli S.V., Creasy T., Amedeo P., Haas B., El-Sayed N.M., RA Wortman J.R., Feldblyum T., Tallon L., Schatz M., Shumway M., Koo H., RA Salzberg S.L., Schobel S., Pertea M., Pop M., White O., Barton G.J., RA Carlow C.K.S., Crawford M.J., Daub J., Dimmic M.W., Estes C.F., RA Foster J.M., Ganatra M., Gregory W.F., Johnson N.M., Jin J., RA Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W., Li W., RA 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, RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ENZYME REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF RP ASP-213; ASP-215; TYR-221; SER-329; GLN-332; LYS-334; ASP-336; ARG-337 RP 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., RA Carlow C.K., 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 CC of trehalose 6-phosphate. {ECO:0000269|PubMed:24992307}. CC -!- CATALYTIC ACTIVITY: Trehalose 6-phosphate + H(2)O = trehalose + CC phosphate. {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. CC {ECO:0000269|PubMed:24992307}; CC -!- ENZYME 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 CC {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 SMR; A8NS89; -. DR EnsemblMetazoa; Bm4641; Bm4641; WBGene00224902. DR GeneID; 6096670; -. DR KEGG; bmy:Bm1_08695; -. DR WBParaSite; Bm4641; Bm4641; WBGene00224902. DR CTD; 6096670; -. DR InParanoid; A8NS89; -. DR OMA; YATNLQP; -. DR OrthoDB; EOG091G08RD; -. 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 Gene3D; 3.40.50.1000; -; 3. DR InterPro; IPR023214; HAD-like_dom. DR SUPFAM; SSF56784; SSF56784; 3. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 492 Trehalose-phosphatase. FT /FTId=PRO_0000385170. FT REGION 332 334 Substrate binding. FT {ECO:0000303|PubMed:24992307}. FT ACT_SITE 215 215 Proton donor/acceptor. FT {ECO:0000303|PubMed:24992307}. FT METAL 213 213 Magnesium. {ECO:0000269|PubMed:24992307}. FT METAL 215 215 Magnesium; via carbonyl oxygen. FT {ECO:0000269|PubMed:24992307}. FT METAL 424 424 Magnesium. {ECO:0000269|PubMed:24992307}. FT MUTAGEN 213 213 D->A: Loss of catalytic activity. FT {ECO:0000269|PubMed:24992307}. FT MUTAGEN 215 215 D->A: Loss of catalytic activity. FT {ECO:0000269|PubMed:24992307}. FT MUTAGEN 221 221 Y->A: Reduces catalytic activity. FT {ECO:0000269|PubMed:24992307}. FT MUTAGEN 329 329 S->A: Reduces catalytic activity. FT {ECO:0000269|PubMed:24992307}. FT MUTAGEN 332 332 Q->A: Strongly reduces catalytic FT activity. {ECO:0000269|PubMed:24992307}. FT MUTAGEN 334 334 K->A: Strongly reduces catalytic FT activity. {ECO:0000269|PubMed:24992307}. FT MUTAGEN 336 336 D->A: Strongly reduces catalytic FT activity. {ECO:0000269|PubMed:24992307}. FT MUTAGEN 337 337 R->A: Strongly reduces catalytic FT activity. {ECO:0000269|PubMed:24992307}. FT MUTAGEN 386 386 E->A: Reduces catalytic activity. FT {ECO:0000269|PubMed:24992307}. FT HELIX 65 87 {ECO:0000244|PDB:4OFZ}. FT HELIX 94 107 {ECO:0000244|PDB:4OFZ}. FT STRAND 118 120 {ECO:0000244|PDB:4OFZ}. FT STRAND 125 127 {ECO:0000244|PDB:4OFZ}. FT HELIX 131 151 {ECO:0000244|PDB:4OFZ}. FT STRAND 152 154 {ECO:0000244|PDB:4OFZ}. FT HELIX 159 165 {ECO:0000244|PDB:4OFZ}. FT HELIX 168 172 {ECO:0000244|PDB:4OFZ}. FT HELIX 173 175 {ECO:0000244|PDB:5E0O}. FT HELIX 180 204 {ECO:0000244|PDB:4OFZ}. FT STRAND 209 213 {ECO:0000244|PDB:4OFZ}. FT TURN 216 218 {ECO:0000244|PDB:4OFZ}. FT STRAND 223 225 {ECO:0000244|PDB:4OFZ}. FT HELIX 232 245 {ECO:0000244|PDB:4OFZ}. FT STRAND 247 252 {ECO:0000244|PDB:4OFZ}. FT STRAND 257 261 {ECO:0000244|PDB:4OFZ}. FT HELIX 262 265 {ECO:0000244|PDB:4OFZ}. FT STRAND 270 278 {ECO:0000244|PDB:4OFZ}. FT HELIX 279 281 {ECO:0000244|PDB:4OFZ}. FT STRAND 283 286 {ECO:0000244|PDB:4OFZ}. FT STRAND 289 292 {ECO:0000244|PDB:4OFZ}. FT HELIX 300 316 {ECO:0000244|PDB:4OFZ}. FT STRAND 327 329 {ECO:0000244|PDB:4OFZ}. FT STRAND 331 334 {ECO:0000244|PDB:5E0O}. FT STRAND 335 341 {ECO:0000244|PDB:4OFZ}. FT STRAND 345 347 {ECO:0000244|PDB:4OFZ}. FT HELIX 351 364 {ECO:0000244|PDB:4OFZ}. FT STRAND 376 378 {ECO:0000244|PDB:4OFZ}. FT STRAND 381 388 {ECO:0000244|PDB:4OFZ}. FT STRAND 391 393 {ECO:0000244|PDB:5E0O}. FT HELIX 398 408 {ECO:0000244|PDB:4OFZ}. FT STRAND 415 417 {ECO:0000244|PDB:4OFZ}. FT STRAND 419 425 {ECO:0000244|PDB:4OFZ}. FT HELIX 426 428 {ECO:0000244|PDB:4OFZ}. FT HELIX 429 438 {ECO:0000244|PDB:4OFZ}. FT STRAND 440 442 {ECO:0000244|PDB:4OFZ}. FT STRAND 444 449 {ECO:0000244|PDB:4OFZ}. FT HELIX 452 461 {ECO:0000244|PDB:4OFZ}. FT STRAND 465 473 {ECO:0000244|PDB:4OFZ}. FT HELIX 474 490 {ECO:0000244|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 //