Detail Information for IndEnz0005001202
IED ID IndEnz0005001202
Enzyme Type ID lipase001202
Protein Name GPI inositol-deacylase
EC 3.1.-.-
Gene Name BST1 SNOG_05858
Organism Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Phaeosphaeriaceae Parastagonospora Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum) Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Enzyme Sequence MVREKAQVTMGSTTMDMLEDEVVKAQDRRWRLRLRNPWACSAYTLVTTALGFAAFFLMLQSFLTKQLDTKGCEMVYMRPMYSKFDDFDTEHTRFASKYSLYLYREWGIDEEFTVKGAPVLFIPGNAGSYKQVRSLAAESAYHYHNSVQHESNAGKGERRPLDFFAVDFNEDFTAFHGQTVLDQAEYLNDAITFILSLYHTPGRSRRDPHLPDPTSVIIVGHSMGGVVARTLFTMPNYQANSINTIVTIAAPHARPPVSFDGDIVRTQNAVNSYWRSAYAQDSAKDNPLQHVTLVSIAGGGLDNIVSSDYASIASIVPETHGFTVFSSSIPNCWTGADHLAITWCDQVRKSIVRALYDVVDVSQAMQTLPVTNRMRFFKKWFLTGLEDIAEKTLPMTTEATLLTVDVDTAILPQEEQLVLRSLGRSSPNIKAFLLPVPPRDRGEKIFTLLTNERLDGPGEHGRLEVLFCSMSSAQSTQSYLTHLDFAGESPTATKLACKNAASDVIILPESTSHSNFPFRPDQAPFSYLQYDVRDLAQHQFVAVLDKVAHHSAGWVVAAFSASSEATVKVNPSLQRLLYTGISLQLPPRRPLTTEISIPALHSSLLAYDVHISRQKCSQGELFAPLLRQYISDLYESKFFVNVEDAMINVHGRGRPTCRAALSSKSPSNGLSLQIWADPTCDSSIDVTLKVDFLGSLGKLWMRYRIVFAAFPLLVVALVLCQQFRTYDATGVFISFAQSLNECMYSSLPLAITALTFLSITLATAQMQSKKLQALGGPASIIGAFFDNDNELLLGSEDPFFWFLVPLFGIMCTAICVMVNYVVLILTYLFATLYALVRSNRLLDASGQRTPDAFAVTSTRRRIINTLILLSLISTAIPYHFAYVVLCIVQLATCIRGFRLAKEAQLDTNYNFYNYAHSIFILMLWILPINLPVLVVWIRNLAIQWLTPFSSHHNVLSITPFILLVETLSTGRMVPRVRPGISLFTNVFLFAIGAYAAVYGVTYAYVLHHLANILCAWLVAIHFDTLGLAFEDSSKGVAVVGGRSEGKKRP
Enzyme Length 1049
Uniprot Accession Number Q0UQV6
Absorption
Active Site ACT_SITE 222; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.-.-
Enzyme Function FUNCTION: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Transmembrane (9)
Keywords Endoplasmic reticulum;Hydrolase;Membrane;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 116,830
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda