GOB1_BRUMA
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 03-AUG-2022, entry version 65.
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}.
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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 PRIDE; A8NS89; -.
DR EnsemblMetazoa; Bm4641.1; Bm4641.1; WBGene00224902.
DR GeneID; 6096670; -.
DR KEGG; bmy:BM_BM4641; -.
DR WBParaSite; Bm4641.1; Bm4641.1; WBGene00224902.
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 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 BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24992307"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24992307"
FT BINDING 332..334
FT /ligand="substrate"
FT /evidence="ECO:0000303|PubMed:24992307"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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
