fadD22

p-hydroxybenzoic acid--AMP ligase FadD22

705 amino acids

Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. This intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B).

Belongs to the ATP-dependent AMP-binding enzyme family.

75.198 kDa

MRNGNLAGLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQRDDLSASNMTIAGGNDGGATLRERLVALRQERQRLVVDAVCAEAAKMLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHGRLKSAGPVNSGATGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALLGTIAGSEAGLGKLIQAASTPDEIFQLIDSELGK

fadD22

p-hydroxybenzoic acid--AMP ligase FadD22

705 amino acids

Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. Usually, this intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1, but M.tuberculosis lacks Pks15/1 due to a natural frameshift and thus is unable to produce PPOL.

Belongs to the ATP-dependent AMP-binding enzyme family.

75.198 kDa

MRNGNLAGLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQRDDLSASNMTIAGGNDGGATLRERLVALRQERQRLVVDAVCAEAAKMLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHGRLKSAGPVNSGATGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALLGTIAGSEAGLGKLIQAASTPDEIFQLIDSELGK

fadD22

p-hydroxybenzoic acid--AMP ligase FadD22

705 amino acids

Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. Usually, this intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1, but M.tuberculosis lacks Pks15/1 due to a natural frameshift and thus is unable to produce PPOL.

Belongs to the ATP-dependent AMP-binding enzyme family.

75.198 kDa

MRNGNLAGLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQRDDLSASNMTIAGGNDGGATLRERLVALRQERQRLVVDAVCAEAAKMLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHGRLKSAGPVNSGATGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALLGTIAGSEAGLGKLIQAASTPDEIFQLIDSELGK

fadD22

p-hydroxybenzoic acid--AMP ligase FadD22

702 amino acids

Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. This intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B).

Belongs to the ATP-dependent AMP-binding enzyme family.

75.181 kDa

MRNENVAGLLAERASEAGWTDQPAYYAPDVVTHGQIHDGAARLGAVLANRGLCRGDRVLLCMPDSPELVQVLLACLARGILAFLANPELHRDDHAFQERDTQAALVITSGPLCDRFAPSTVVDAADLFSEAARVGPADYEILGGDAAAYATYTSGTTGPPKAAIHRHCDVFAFVEAMCRNALRLTPADIGLSSARMYFAYGLGNSVWFPLATGSSAVVNPLPVGAEVAATLSARFEPSVLYGVPNFFARVVDACSADSFRSVRCVVSAGEALEVGLAERLTEFFGGIPILDGVGSTEVGQTFVSNTVDEWRPGSLGKVLPPYQIRVVAPDGAAAGPGVEGDLWVRGPSIAESYWNWPEPLLTDEGWLDTRDRVCIDDDGWVTYACRADDTEIVGAVNINPREIERLIVEEDAVAEVAVVGVKEATGASTLQAFLVPASAEGIDGSVMRDIHRRLLTRLSAFKVPHRFAVVERLPRTANGKLLRSALRGQTPAKPIWELASAEHRSGAPGQLDDQSASALVSGSREVSLKERLAALQQERHRLVLDAVCGETAKMLGEPDPRSVNRDLAFSELGFDSQMTVELCHRLAAATGLRVPETVGWDYGSISGLAQYLEAELSGADRRVTPQSARSGARALPLIEAQLNKVEELTAAIADGEKPRVAERLRALLGTITEGQEHWGQRIAAASTPDEIFQLIDSEFGES