(data stored in ACNUC7421 zone)

SWISSPROT: Q47TF2_THEFY

ID   Q47TF2_THEFY            Unreviewed;       291 AA.
AC   Q47TF2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Trehalose 6-phosphate phosphatase {ECO:0000256|RuleBase:RU361117};
DE            EC=3.1.3.12 {ECO:0000256|RuleBase:RU361117};
GN   OrderedLocusNames=Tfu_0224 {ECO:0000313|EMBL:AAZ54262.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54262.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to
CC       produce free trehalose. {ECO:0000256|RuleBase:RU361117}.
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;
CC         EC=3.1.3.12; Evidence={ECO:0000256|RuleBase:RU361117};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361117};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|RuleBase:RU361117}.
CC   -!- SIMILARITY: Belongs to the trehalose phosphatase family.
CC       {ECO:0000256|RuleBase:RU361117}.
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DR   EMBL; CP000088; AAZ54262.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0224; -.
DR   EnsemblBacteria; AAZ54262; AAZ54262; Tfu_0224.
DR   KEGG; tfu:Tfu_0224; -.
DR   eggNOG; ENOG4107X44; Bacteria.
DR   eggNOG; COG1877; LUCA.
DR   HOGENOM; HOG000239290; -.
DR   KO; K01087; -.
DR   OMA; HYGAERW; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TF2.
DR   SWISS-2DPAGE; Q47TF2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Hydrolase {ECO:0000256|RuleBase:RU361117,
KW   ECO:0000313|EMBL:AAZ54262.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361117};
KW   Metal-binding {ECO:0000256|RuleBase:RU361117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
SQ   SEQUENCE   291 AA;  30370 MW;  BBB09B1FDF1D9A1E CRC64;
     MRAVSGIPPA FSPPSGKPSM SLLQSTTQSG KVALDRIRDM PDRAVCAFDF DGTLAPIVPD
     PRDSRAHPGA VPALRALAGR VRAVAVITGR PAQTAVDYGG LDAVPGITVL GHYGRERWED
     GKLTVPEPPP GVAMVREALP GLLDEVGAPE GTWIEDKKHA LAVHTRRTAD PEAALELLRA
     PLADLAKRAE LAVEPGRMVI ELRPPGVDKG AALTDLVTRL GAEAVLYAGD DLGDLAAYDA
     VERLREQGVA GFKLCSGSAE VTELARRADA VVPGPEGVVA FLEELVAAVG G
//

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