>GFF269 FitnessBrowser__Phaeo:GFF269
MAKFRHDGRANRRKLMQSQTTQVVIVGGGPSGLLLSQLLHRAGIDTIVLERQTRDYVLGRIRAGVLEHGFVDLLRRAGASARMDRDGMVHHGFHIAHQGRLDRIDLAGSAKGQTVMVYGQTEVTRDLYDARDAMGGQIIHEAANVALHDLTTARPNVTYEQQGETRRIDTKFIVGADGFHGVSRKSIPSDVLQEYEKVYPFGWLGVLSQTSPAADELIYARHDRGFALCSMRNAQLSRYYIQVPLTDRVEDWSDAAFWEELKRRLPEDVAKGLQTGVSIEKSIAPLRSFVAEPMRYGALFLAGDAAHIVPPTGAKGLNLAASDIHYLYEGLSDHFQRNDDTALDSYSERALARIWKAERFSWWMTNLLHRFPDMSPADLRLQQADLDYLFSSDAAQASLAENYVGLPY
>PDB_2phh_A The coenzyme analogue adenosine 5-diphosphoribose displaces fad in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
>PDB_1pdh_A Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified fad present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
>metacyc__MONOMER-11534 <i>p</i>-hydroxybenzoate hydroxylase (EC 1.14.13.2) (Pseudomonas fluorescens)
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>SwissProt__P20586 p-hydroxybenzoate hydroxylase; PHBH; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1))
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>PDB_1pbc_A Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate, 2,4-dihydroxybenzoate and 2-hydroxy- 4-aminobenzoate and of the try222ala mutant, complexed with 2- hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
>PDB_1ius_A P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFW
TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>PDB_1dod_A The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFW
TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>PDB_8y2s_A 4-hydroxybenzoate 3-monooxygenase
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGMLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVMVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHENIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
>PDB_1bf3_A P-hydroxybenzoate hydroxylase (phbh) mutant with cys 116 replaced by ser (c116s) and arg 42 replaced by lys (r42k), in complex with fad and 4-hydroxybenzoic acid
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGKIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
>PDB_1k0l_A Pseudomonas aeruginosa phbh r220q free of p-ohb
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSQYYVQVPLSEKVEDWSDERFW
TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>PDB_1k0j_A Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSQYYVQVPLSEKVEDWSDERFW
TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>PDB_1ykj_B A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRGGVLEQGMVDLLREAGVDRRMARLVHEGVEIAFAGQ
RRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFH
GISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTE
LKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRG
ELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>biolip__6dllB 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad.
SNAMKTQVAIIGAGPSGLLLGQLLHKAGIDNIIVERQTAEYVLGRIRAGVLEQGTVDLLREAGVAERMDREGLVHEGVELLVGGRRQRLDLKALTGGKTVMVYGQTEVTRDLMQAREASGAPIIYSAANVQPHELKGEKPYLTFEKDGRVQRIDCDYIAGCDGFHGISRQSIPEGVLKQYERVYPFGWLGLLSDTPPVNHELIYAHHERGFALCSQRSQTRSRYYLQVPLQDRVEEWSDERFWDELKARLPAEVAADLVTGPALEKSIAPLRSLVVEPMQYGHLFLVGDAAHIVPPTGAKGLNLAASDVNYLYRILVKVYHEGRVDLLAQYSPLALRRVWKGERFSWFMTQLLHDFGSHKDAWDQKMQEADREYFLTSPAGLVNIAENYVGLPFEEVA
>metacyc__MONOMER-11506 <i>p</i>-hydroxybenzoate hydroxylase (EC 1.14.13.2) (Pseudomonas putida)
MKTQVAIIGAGPSGLLLGQLLHNAGIETVIVERQTPEYVLGRIRAGVLEQGTVDLLREAGVSARMDREGLVHEGVELLVGGRRQRLDLKALTGGKTVMVYGQTEVTRDLMQAREASGAPIIYAANNVQPHELKGERPYLTFEKDGQAHRLECDYIAGCDGFHGVSRQSIPEGVLKQYERVYPFGWLGLLSDTPPVNHELIYAHHERGFALCSQRSQTRSRYYLQVPLDDKVEAWSDERFWDELKARLPAEVAADLVTGPALEKSIAPLRSLVVEPMQYGHLFLVGDAAHIVPPTGAKGLNLAASDVNYLYRILVKVYGEGRTDLLQQYSPLALRRVWKGERFSWFMTQLLHDFGSHKDAWDQKMQEADREYFLNSPAGLLNIAENYVGLPYEAVV
>metacyc__MONOMER-20325 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) (Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1))
MKTKVAIIGAGPSGLLLGQLLAKQGIDNVIIERVTGEYILGRIRAGVLEQGMVNLLREAGVSERMDKEGEVHDGFELAFNNKRVRIALDELTGGDTVMVYGQTEVTRDLMEARAKAGYTTVYEASDVKLHDVKSDTDTPYVTFEKNGEQVRLDCDYIAGCDGFHGVSRKTIPDDVKTEFERVYPFGWLGLLSDTKPAHDELIYCKTDRGFALASMRSQTRSRYYLQVPLTDKVENWSDEAFWEELKKRLPDDVASKMQTGPSIEKSIAPLRSFVCEPMQYGNLFLVGDAAHIVPPTGAKGLNLAASDVATLYKIMTRVYKENDKDCINQYSEICLRRVWNGERFSWWMTNMMHDFDDVSVSGADAITFDRFMSSELNFYTDNEEGRKVVAMQYVGLPYEDLK
>reanno__pseudo6_N2E2_Pf6N2E2_2914 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) (Pseudomonas fluorescens FW300-N2E2)
MKTLKTQVAIIGAGPSGLLLGQLLHNAGIDTVILERQTPEYVLSRIRAGVLEQGMVELLRQAGVGQRMDAEGLPHDGFELVLNDRRVHIDLKGLTGGKNVMVYGQTEVTRDLMAAREAAGARTLYLASNAQPHDMQTQTPFVTFEHEGETWRLDCDYIAGCDGFHGVARQSIPAEKLKVFERVYPFGWLGVLADTPPVHEELVYARHTRGFALCSMRSKTRTRYYLQVPAEEQVADWPDERFWGELKNRLPADLAAALVTGPSIEKSIAPLRSFVVEPMQYGRMFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYRDGRVELLEKYSAICLRRVWKAERFSWWMTSMLHRFDDDAFNQRISEAELEYFVDSEAGRKTIAENYVGLPYEAIE
>ENA__AAA73519.1 4-hydroxybenzoate hydroxylase (Rhizobium leguminosarum)
MRTQVAIIGSGPSGLLLGQLLTEAGIDNVILDRVNKDYILGRVRAGVLEEGTVGLLDQARSGARLHAEGLPHDGFSLAFDGRDHRIDLHELTGGRRVTVYGQTEVTRDLMERREESGSLSIYDAVDVAPHDFDGPSPFVTYVKDGVAKRIDCDFIAGCDGFHGASRKAVPERAIRSFEKIYPFGWLGILADVAPVSHELIYANHPRGFALCSMRSATRSRYYIQCTLDEKIDDWSDDRFWDELRRRLPTHHAEALATAPSFEKSIAPLRSFVAEPMRFGRLFLVGDAAHIVPPTGAKGLNLAASDVHYLFSGLIEHYREGSNSGIDAYSHKALARVWKAVRFSWWMTTMMHLFPDTGDFDQKIQEAELDYLTHSRAASMALAENYVGLPF
>reanno__Cup4G11_RR42_RS21940 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) (Cupriavidus basilensis FW507-4G11)
MRTQVAIIGAGPAGLLLGQLLAKAGIDAVIVEQRSPDYILGRIRAGILESVTADALERAGVAQRLQHDGLVHHGIELSYGGERHRIDFHALIGRSVTVYGQTEVTRDLMAARQAGNAVTIYDAQDVSVHDFDTATPMVRYRKGGQQYELRCDFIAGCDGFHGVTRRSVPEPSRRIFERVYPFGWLGVLADTPPVANELIYASHERGFALCSMRSLTRSRYYVQVSADERVEDWSDQRFWDELRSRLDTSAAEALVTGASIEKSIAPLRSFVCEPMRFGNLFLAGDAAHIVPPTGAKGLNLAASDVLYLADGLIARYLRDDASELDAYSQKCLRRVWKAERFSWWMTSLLHRFPDADDFALRIQQAELDYLAGSRAAQMSLAENYVGLPY
>biolip__7on9A Crystal structure of para-hydroxybenzoate-3-hydroxylase prai
MRTQVGIIGAGPAGLLLSHLLYLQGIESIIIENRTREEIEGTIRAGVLEQGTVDLMNQMGVGARMMKEGHFHEGFELRFNGRGHRINVHELTGGKYVTVYAQHEVIKDLVAARLQTGGQIHFNVGDVSLHDVDTSSPKIRFRPNKDGELQEIECDFIAGCDGFRGPSRPAIPQSVRKEYQKVYPFSWLGILVEAPPSAHELIYANHERGFALVSTRSPQIQRLYLQVDAQDHIDNWSDDRIWSELHARLETRDGFKLLEGPIFQKGIVSMRSFVCDPMQHGRLFLAGDAAHIVPPTGAKGLNLAAADVQVLARGLEAYYKAGKMEILNRCTEICLRRIWKAERFSWFMTTMLHRDQGHTPFERGIQLAELDYVTSSRAASTSLAENYIGLPME
>SwissProt__C4TP09 4-hydroxybenzoate 3-monooxygenase (NAD(P)H); 4-hydroxybenzoate 3-hydroxylase; 4HB 3-hydroxylase; EC 1.14.13.33 (Paenibacillus sp.)
MRTQVGIIGAGPAGLLLSHLLYLQGIESIIIENRTREEIEGTIRAGVLEQGTVDLMNQMGVGARMMKEGHFHEGFELRFNGRGHRINVHELTGGKYVTVYAQHEVIKDLVAARLQTGGQIHFNVGDVSLHDVDTSSPKIRFRPNKDGELQEIECDFIAGCDGFRGPSRPAIPQSVRKEYQKVYPFSWLGILVEAPPSAHELIYANHERGFALVSTRSPQIQRLYLQVDAQDHIDNWSDDRIWSELHARLETRDGFKLLEGPIFQKGIVSMRSFVCDPMQHGRLFLAGDAAHIVPPTGAKGLNLAAADVQVLARGLEAYYKAGKMEILNRCTEICLRRIWKAERFSWFMTTMLHRDQGHTPFERGIQLAELDYVTSSRAASTSLAENYIGLPMEF
>biolip__8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole
MRTQVGIVGAGPAGLMLAHLLRREGIDAVVIERAAREHVRTRLRAGVLEQGTVEMLREAGVGGRIDAVGMEMHAIDFRFGGRSHRLDFHEASGGRRAWVYPQHEVVTDLMSACDAGDVPILYEAPVERIEGLEDDRARIVFGQDGAAGEITCDFVAGCDGFRGVSRGSMPAGIARGYDRIYPFGWLGILADAPPASPDVTWGCSDRGFAMMSMRSPTVTRLYLQCEPDEDPDAWSDDRIWSELHRRLDVEGMPSLREGPIRDKGVTAMRSFLSEPMQHGRLFLAGDAAHIVPPTGAKGLNSAMADIKVLAAALVDHYRHGRSDRLATYSERCLRRMWLVQRFSAALCTMVHQFPGQNEFVRRLQRADLDYMTGTHAGRLQFAENFTGLPIE
>biolip__8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole
TQVGIVGAGPAGLMLAHGVLEQGTVEMLREEMHAIDFRFGGRSHRLDFHEASGGRRAWVEGLEDDRARIVCDFVAGCDGFRGVSRGSMPGIARGYDRIYPFGWLGILADAPPASPDVTWGCSDRGFAMMSMRSPTVTRLYLQCEPDEDPDAWSDDRIWSELHRRLDVEGMPSLREGPIRDKGVTAMRSFLSEPMQHGRLFLAGDAAHIVPPTGAKGLNSAMADIKVLAAALVDHYRHGRSDRLATYSERCLRRMWLVQRFSAALCTMVHQFPGQNEFVRRLQRADLDYMTGTHAGRLQFAENFTGLPIE