| IED ID | IndEnz0009000329 |
| Enzyme Type ID | chitinase000329 |
| Protein Name |
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 EC 2.4.1.109 |
| Gene Name | PMT1 YDL095W D2390 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSEEKTYKRVEQDDPVPELDIKQGPVRPFIVTDPSAELASLRTMVTLKEKLLVACLAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFDFENIGDSFPSTTPYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSFKKYEMYPANSLNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIHFQSLTLDGDGASFFSPEFRSTLKNNKIPQNVVADVGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGESLTTFQNLTDGTKVRLFHTVTRCRLHSHDHKPPVSESSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFEQQEVTCASSGRHDLTLWYVENNSNPLLPEDTKRISYKPASFISKFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRNVYLLGNAIVWWAVTAFIGIFGLIVITELFSWQLGKPILKDSKVVNFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAYYFGILALGHALDIIVSYVFRSKRQMGYAVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLSGWDYNCNTYFSSLEEYKNQTLTKRESQPAATSTVEEITIEGDGPSYEDLMNEDGKKIFKDTEGNELDPEVVKKMLEEEGANILKVEKRAVLE |
| Enzyme Length | 817 |
| Uniprot Accession Number | P33775 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321; EC=2.4.1.109; Evidence={ECO:0000269|PubMed:10764776, ECO:0000269|PubMed:8367478}; CATALYTIC ACTIVITY: Reaction=dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323; EC=2.4.1.109; Evidence={ECO:0000269|PubMed:10764776, ECO:0000269|PubMed:8367478}; |
| DNA Binding | |
| EC Number | 2.4.1.109 |
| Enzyme Function | FUNCTION: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. Required for incorporation of proteins in the cell wall. {ECO:0000269|PubMed:10764776, ECO:0000269|PubMed:18182384, ECO:0000269|PubMed:8367478, ECO:0000269|PubMed:8543034, ECO:0000269|PubMed:9466258}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}. |
| nucleotide Binding | |
| Features | Beta strand (23); Chain (1); Domain (3); Glycosylation (3); Helix (27); Initiator methionine (1); Modified residue (1); Mutagenesis (7); Topological domain (8); Transmembrane (7); Turn (9) |
| Keywords | 3D-structure;Acetylation;Direct protein sequencing;Endoplasmic reticulum;Glycoprotein;Glycosyltransferase;Membrane;Reference proteome;Repeat;Transferase;Transmembrane;Transmembrane helix |
| Interact With | P31382; P47190 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000303|PubMed:10085156}; Multi-pass membrane protein {ECO:0000269|PubMed:10085156}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22814378 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (2) |
| Cross Reference PDB | 6P25; 6P2R; |
| Mapped Pubmed ID | 11800270; 12776183; 14555493; 16200504; 16554755; 17024709; 17088254; 17397115; 17587671; 17975704; 18323647; 19420743; 19536198; 19633715; 20648385; 21231968; 21810245; 21912684; 22261724; 22533807; 22925677; 22960125; 23135325; 23434682; 23480475; 23484968; 23704572; 23942187; 24519942; 24934559; 25666261; 25936926; 25995378; 26456335; 26474840; 27161930; 27358400; 27768707; 31285605; 31835530; 7772870; 7852348; 7864633; 8472892; 8585318; 9184828; |
| Motif | |
| Gene Encoded By | |
| Mass | 92,675 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17377; RHEA:53396 |
| Cross Reference Brenda | 2.4.1.109; |