pobA

Phenoxybenzoate dioxygenase subunit alpha

409 amino acids

Degrades exclusively diarylether compounds having carboxyl groups in the 3- or 4-position. Yields a hemiacetal that spontaneously hydrolyzes to phenol and protocatechuate.

Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.

46.259 kDa

MSKTIPIVDAQHAGSAYQHVPGHPDPQLSAVAKGTPTGEYLRRYWQPVALSADVTDRPQMVRILGEDLVLFRDKAGRPGLLYPRCMHRGTSLYYGHVEEAGIRCCYHGWLFAVDGTCLNQPCEPEGGLRREAARQPWYPVEERYGLVFAYMGPPEKKPVLPRYDILEDLEEGEFIEVISGGFVSYADHVEDPNVPYHWLQNWENIMDPYHVYILHSTFSGIQFAENFKILPRVDFEAVDGGVIYHAWRDLEDGRQLERINSALFPNISAIPMIDLSPGQGRWIGWHVAVDDQHYRGFFAARTRQPGNFAPIKMHNGKSWTELSEQEKQDFPGDFEAQFGQGRVTLHGEEHLATSDHGIALLRRQMKQQIAIVQQGGDPAGVHFNEADALVRIRSGNFYTTSDKTETAAD

pobA

p-hydroxybenzoate hydroxylase

404 amino acids

Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.

Belongs to the aromatic-ring hydroxylase family.

45.271 kDa

MQTMKTKVAIIGSGPAGLLLGQLLYKAGIEHVIVEQRSADYVASRIRAGILEQVSVDLLEQAGVDQNLKEKGLPHSGIEILTNGQKFRVDLSALTQGKQVTVYGQTEVTKDLMQAREQAGLCSFYESNDVQIHDFYNAPKVTFESNGTHYQIECDFIAGCDGYHGVCRASVPQDKIKTFEKVYPFGWLGVLADVPPVADELIYVQSERGFALCSMRSETRSRYYIQVPLTDHVENWSDDQFWEELKNRLDPESCEKLVTGPSIEKSIAPLRSFVTEPMRFGKLFLAGDAAHIVPPTGAKGLNLAASDIAYLSSALIEFYTQGSEQGIDQYSEKCLQRVWKAERFSWWMTHLLHRFETESEFDHKIKQAELSYILGSTAGQTTLAENYVGLPYEIKSLDYLKHAS

pobA

p-hydroxybenzoate hydroxylase

394 amino acids

Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.

Belongs to the aromatic-ring hydroxylase family.

44.324 kDa

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

pobA

p-hydroxybenzoate hydroxylase

394 amino acids

Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.

Belongs to the aromatic-ring hydroxylase family.

44.322 kDa

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE