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 29-OCT-2014, entry version 25. 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: 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 PDBsum; 4OFZ; -. DR EnsemblMetazoa; Bm4641; Bm4641; Bm4641. DR GeneID; 6096670; -. DR KEGG; bmy:Bm1_08695; -. DR CTD; 6096670; -. DR InParanoid; A8NS89; -. 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}. 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 //