GT-CORE (public beta v1)

Glycosyltransferase Curated Online Resource for Enzymology

Family-organised sequence, structure, mechanism and substrate-specificity records for the CAZy glycosyltransferases

pmt

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) · Polyprenol-phosphate-mannose--protein mannosyltransferase (EC 2.4.1.-)

GT39Non-model organism · annotation 4–5Fold GT-CInverting

External resources

Identification and annotation

CAZy familyGT39 · CAZy entry
Gene symbolpmt
Synonyms / alternate names
  • MtPMT
  • PMTub
  • Protein O-mannosyltransferase
UniProt accessionP9WN05
NCBI Gene ID887882
Source speciesMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic domainBacteria
UniProt annotation level5

Function and localisation

Enzyme functionPolyprenol-phosphate-mannose--protein mannosyltransferase (EC 2.4.1.-)
Subcellular locationnot curated

Structure and mechanism

Fold typeGT-C
Catalytic mechanismInverting
Cation dependenceNo
Oligomeric statenot curated
PDB structuresnot curated

Donor and acceptor specificity

Sugar nucleotide donornot curated
Donor CCD code(s)not curated
Acceptor substrate(s)not curated
Acceptor CCD / GlycoCTnot curated

Protein sequences

Full protein sequence

522 aa
MTARPPESCVLAKDRPEEPVVPVVSPGPLVPVADFGPLDRLRGWIVTGLITLLATVTRFLNLGSLTDAGTPIFDEKHYAPQAWQVLNNHGVEDNPGYGLVVHPPVGKQLIAIGEAIFGYNGFGWRFTGALLGVVLVALVVRIVRRISRSTLVGAIAGVLLICDGVSFVTARTALLDGFLTFFVVAAFGALIVDRDQVRERMHIALLAGRSAATVWGPRVGVRWWRFGAGVLLGLACATKWSGVYFVLFFGAMALAFDVAARRQYQVQRPWLGTVRRDVLPSGYALGLIPFAVYLATYAPWFASETAIDRHAVGQAVGRNSVVPLPDAVRSLWHYTAKAFHFHAGLTNSAGNYHPWESKPWTWPMSLRPVLYAIDQQDVAGCGAQSCVKAEMLVGTPAMWWLAVPVLAYAGWRMFVRRDWRYAVVLVGYCAGWLPWFADIDRQMYFFYAATMAPFLVMGISLVLGDILYHPGQGSERRTLGLIVVCCYVALVVTNFAWLYPVLTGLPISQQTWNLEIWLPSWR

Catalytic domain sequence

193 aa
RSLWHYTAKAFHFHAGLTNSAGNYHPWESKPWTWPMSLRPVLYAIDQQDVAGCGAQSCVKAEMLVGTPAMWWLAVPVLAYAGWRMFVRRDWRYAVVLVGYCAGWLPWFADIDRQMYFFYAATMAPFLVMGISLVLGDILYHPGQGSERRTLGLIVVCCYVALVVTNFAWLYPVLTGLPISQQTWNLEIWLPSW