>RR42_RS20365 FitnessBrowser__Cup4G11:RR42_RS20365
MATATHAGDAQASFSGTLTDKLKEQFDAGLLSGQELRPDFTIAQPLERYTDTDHAVWAKLYDRQASMLRGRVCDEFLQGLSTLGMERDRVPSFDQLNETLMRATGWQVVAVPGLVPDAVFFEHLANRRFPASWWMRKPEQLDYLQEPDCFHDVFGHVPLLINPVFANYMEAYGKGGLKAASLGALDMLARLYWYTVEFGLIRTPEGLRIYGAGILSSQGESIYSLDSASPNRIGFDVRRIMRTRYRIDTFQKTYFVIDSFDQLFDATRPDFAPLYEELRAQPTLGAGDVGQSDLVLQRGSREGWADSDDV
>metacyc__MONOMER-12067 phenylalanine hydroxylase (EC 1.14.16.1) (Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757))
MNDRADFVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFMEGLERLEVDADRVPDFNKLNQKLMAATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKAKALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDSFKQLFDATAPDFAPLYLQLADAQPWGAGDVAPDDLVLNAGDRQGWADTEDV
>PDB_3tcy_A Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site
FVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFLEGLERLEVDADRVPDFNKLNEK
LMAATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKA
KALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDS
FKQLFDATAPDFAPLYLQLADAQPWGAGDIAPDDLVL
>PDB_1ltv_A Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized fe(iii)
VPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFLEGLERLEVDADRVPDFNKLNEKLM
AATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKAKA
LGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDSFK
QLFDATAPDFAPLYLQLADAQPWGAGDIAPDDLVL
>biolip__4etlA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum f258a mutation
FVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFLEGLERLEVDADRVPDFNKLNEKLMAATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKAKALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDSFKQLFDATAPDAAPLYLQLADAQPWGAGDIAPDDLVL
>PDB_1ltz_A Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin
FVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFLEGLERLEVDADRVPDFNKLNEK
LMAATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKA
KALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDS
FKQLFDADFAPLYLQLADAQPWGAGDIAPDDLVL
>reanno__acidovorax_3H11_Ac3H11_1847 Phenylalanine 4-monooxygenase (EC 1.14.16.1) (Acidovorax sp. GW101-3H11)
VRKVMAAKEKKMGQAPVVYGQSTRPPRGDYSRANADYTCPQDYAAYTDADHDTYRRLYERQRALLPGLASQAFIDALPSLGASDQIPRFEEVNERLYKATGWELVGVPGLIPEVPFFTLLANRQFPVTDWIRKPEEFEYIVEPDIFHDLFGHVPLLFNPVFADYVQRYGQGGLKAQGLGSCEMLSRLYWYTIEFGLIREAGELRAYGAGILSSSGELAYSVQSPEPQRIPLALERTMRTRYKIDTYQQTYFVIDSFEQLFEMTAADFAPIYERLRGLPEFAADEREAVAA
>reanno__pseudo3_N2E3_AO353_18585 Phenylalanine 4-monooxygenase (EC 1.14.16.1) (Pseudomonas fluorescens FW300-N2E3)
MKQTQYVAREPDAQGFIHYTAEEHAVWNTLITRQLKVLEGRACQEYMDGIEKLGLPHDRIPQLDEINKVLGETTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLQASKEERVYLARLYWMTIEFGLVDTPQGKRIYGGGILSSPKETVYSLSGEPEHQAFDPLEAMRTPYRIDILQPLYFVLPNLKRLFDLAHEDIMGMVHQGMQLGLHAPKFPPKPKAA
>reanno__pseudo5_N2C3_1_AO356_03975 Phenylalanine 4-monooxygenase (EC 1.14.16.1) (Pseudomonas fluorescens FW300-N2C3)
MKQTQYVAREPDAQGFIHYTAEEHAVWNTLITRQLKVIEGRACQEYLDGIDKLGLPHDRIPQLDEINKVLGQTTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLQASKEERVYLARLYWMTIEFGLVQTPQGRRIYGGGILSSPKETVYCLSDEPEHQAFDPLEAMRTPYRIDILQPVYFVLPELKRLFDLAHEDIMGMVKRGRELGLHAPKFPPKAA
>reanno__pseudo6_N2E2_Pf6N2E2_2630 Phenylalanine 4-monooxygenase (EC 1.14.16.1) (Pseudomonas fluorescens FW300-N2E2)
MKQTQYVAREPDAQGFIHYTAEEHAVWNTLITRQLKVIEGRACQEYLDGIDKLGLPHDRIPQLDEINKVLGETTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLQASKEERVYLARLYWMTIEFGLVQTPQGRRIYGGGILSSPKETVYCLSDEPEHQAFDPLEAMRTPYRIDILQPVYFVLPELKRLFDLAHEDIMGMVKRGRELGLHAPKFPPKAA
>reanno__pseudo13_GW456_L13_PfGW456L13_4394 Phenylalanine 4-monooxygenase (EC 1.14.16.1) (Pseudomonas fluorescens GW456-L13)
MKQTQYVAREPDAQGFIDYPAEEHAVWNTLITRQLKVIEGRACQEYLDGIEKLGLPHDRIPQLGEINKVLAETTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLKASKEERVYLARLYWMTIEFGLLDTPQGQRIYGGGILSSPKETVYSLSNEPEHQAFDPLECMRTPYRIDILQPLYFVLPNLKRLFDLAHEDIMGMVKQAMQMGLHTPKFPPKAA
>reanno__MR1_200831 Phenylalanine 4-monooxygenase (EC 1.14.16.1) (Shewanella oneidensis MR-1)
MTIDTVHTAPYVARSADDSGYIHYPQEEHDIWRQLYARQAVNLPGRACKEYLQGLDALAMPKDRIPQLAEIDKVLMATTGWKTADVPALISFGRFFELLANKEFPVATFIRRKEEFDYLQEPDIFHEIFGHCPLLTNPSFAHFSHMYGQLGLNASKEDRVFLARLYWFTVEFGLLKPQEGELCIYGGGILSSPGETLYAMESQVPERKPFDLLDVLRTPYRIDIMQPIYYVIEHIDVLDEIAKMDIMAYVAKARQLGLFAPKYPPKAKKAS
>biolip__7vgmA Crystal structure of phenylalanine hydroxylase from bacillus cereus atcc 14579
KKTEIPSHLKPFVSTQHYDQYTPVNHAVWRYIMRQNHSFLKDVAHPAYVNGLQSSGINIDAIPKVEEMNECLAPSGWGAVTIDGLIPGVAFFDFQGHGLLPIATDIRKVENIEYTPAPDIVHEAAGHAPILLDPTYAKYVKRFGQIGAKAFSTKEEHDAFEAVRTLTIVKESPTSTPDEVKAAENAVIEKQNLVSGLSEAEQISRLFWWTVEYGLIGNIDDPKIYGAGLLSSVGESKHCLTDAVEKVPFSIEACIGTTYDVTKMQPQLFVCESFEELTDALETFSKTMAFKTGGKEGLEKAIRSENYATAELNSGLQITGTFSETIENDAGELIYMRTNSPTALALHNKQLANHSTSVHSDGFGTPIGLLTENIALENCTDEQLQSLGITIGTIAEFTFASGIHVKGTVTDIVKNDKKIALISFIDCTVTYNARVLFDASWGAFDMAVGSQITSVFPGAADAAAFFPMDEEVHEIPAPLVLNELERMYQTVRDIRSEGILHDAHIDQLIAIQEVLNKFYAKEWLLRLEVLELLLEHNKGHETSAALLHQLSTFTTDEAVTRLINNGLALLP
>metacyc__MONOMER-17816 phenylalanine hydroxylase (EC 1.14.16.1) (Chlamydomonas reinhardtii)
MLALRQGALLLSARGGQTTHDNLQLCAGPSRRPRARWISSAPRPSTLVERHIRPQASTASDATTSTSQRILSIHDVDNGQILGFGADLAEDHPGFHDPAYKQRRAWLAEMAKTHRIGTPIPDVEYSPAEVATWDAVLEELSGLLPQHACREYLRCLTLFDFRKGRVPQLEEMNTVLRSTTGWTVRPVAGLMHPRHFLAGLAFKHFHSTQYMRHPSKPSYTPEPDVVHELIGHVPLLADPAYARLIQTIGLASLAADDKQIWHLTKVYWHTVEFGVVREGDQVKAFGAGILSSYGELAHMASGAAALERLDPFRPQPRMAYKDGFQKRYFVLDSFAEGSELLSSYAASLGLPESLRGDASVA
>SwissProt__Q54XS1 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; Tryptophan 5-hydroxylase; TRH; Tryptophan 5-monooxygenase; EC 1.14.16.1; EC 1.14.16.4 (Dictyostelium discoideum (Social amoeba))
MESNTNSQGQGIIPQSYHSSIFFSISKGSDKIGGLLEYLEIIKKHNINITRIESRPSKTEKKDYDFFLDLEYPTENNKEVEKVIKDLEEKGVKATTLQESSNQTYAPWFPRKISDLDLFANKVLEMGSDLTSDHPGASDPVYRERRREIAKIASTYKHGDEIPRIDYTEEEIKTWGVVYNRLKELFPTNACHQHAYIFPLLEQNCGYSPDNIPQLQDISNFLQECTGWRIRPVQGLLSARDFLNGLAFRVFHATQYIRHPSVPLYTPEPDCCHELLGHVPLLADPDFADFSQEIGLASIGASDEDIQLLSTCYWFTVEFGLCKEGDTIRAYGAGILSSTGEMEHFLTDKAKKLPFNPFDACNTEYPITTFQPLYYVAESFQKAKEQMRQFADSFKKPFSIRYNPYTQSIEILDNKDKLLNICNDIRNQSEILADAISKLKA
>biolip__5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
QSYHSSIFFSISKGSDKIGGLLEYLEIIKKHNINITRIESRPSKTEKKDYDFFLDLEYPTENNKEVEKVIKDLEEKGVKATTLQESSNQTYAPWFPRKISDLDLFANKVLEMGSDLTSDHPGASDPVYRERRREIAKIASTYKHGDEIPRIDYTEEEIKTWGVVYNRLKELFPTNACHQHAYIFPLLEQNCGYSPDNIPQLQDISNFLQECTGWRIRPVQGLLSARDFLNGLAFRVFHATQYIRHPSVPLYTPEPDCCHELLGHVPLLADPDFADFSQEIGLASIGASDEDIQLLSTCYWFTVEFGLCKEGDTIRAYGAGILSSTGEMEHFLTDKAKKLPFNPFDACNTEYPITTFQPLYYVAESFQKAKEQMRQFADSFKKPFSIRYNPYTQSIEILDN
>PDB_5jk8_A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
QSYHSSIFFSISKGSDKIGGLLEYLEIIKKHNINITRIESRPSKTEKKDYDFFLDLEYPTENNKEVEKVIKDLEEKGVKA
TTLQESSNQTYAPWFPRKISDLDLFANKVLEPGASDPVYRERRREIAKIASTYKHGDEIPRIDYTEEEIKTWGVVYNRLK
ELFPTNACHQHAYIFPLLEQNCGYSPDNIPQLQDISNFLQECTGWRIRPVQGLLSARDFLNGLAFRVFHATQYIRHPSVP
LYTPEPDCCHELLGHVPLLADPDFADFSQEIGLASIGASDEDIQLLSTCYWFTVEFGLCKEGDTIRAYGAGILSSTGEME
HFLTDKAKKLPFNPFDACNTEYPITTFQPLYYVAESFQKAKEQMRQFADSFKKPFSIRYNPYTQSIEILD
>SwissProt__E5KBU3 Phenylalanine 4-monooxygenase, chloroplastic; Aromatic amino acid hydroxylase; Phenylalanine 4-hydroxylase; EC 1.14.16.1 (Pinus taeda (Loblolly pine))
MAFPLQKTFLCSNGQSFPCSNGRSTSTLLASDLKFQRLNKPFILRVGSMQIRNSPKEHPRVSSAAVLPPVPRSIHDIPNGDHILGFGANLAEDHPGYHDEEYKRRRSCIADLAKKHKIGEPIPEINYTTEEAHVWAEVLTKLSELYPSHACKEYLESFPLFNFSPNKIPQLEELSQILQHYTGWKIRPVAGLLHPRQFLNGLAFKTFHSTQYIRHTSNPMYTPEPDICHEILGHMPMLVHPEFADLAQVIGLASLGASDKEIWHLTKLYWYTVEFGTIEENKEVKAFGAGILSSFGELQHMKSSKPTFQKLDPFAQLPKMSYKDGFQNMYFLCQSFSDTTEKLRSYARTIHSGN
>BRENDA__A7VKD9 tryptophan 5-monooxygenase (EC 1.14.16.4) (Dugesia japonica)
MCERDKVFAENKKNSIISLTKAKSVSENLIQINSAKHRRGRFSSVSSMIDEEDFEIIKGELLDLNIVMEENKSISTRRSTSFIFGVNDNVKGLVRVLEIFEKFEVSVIHIETRKSLKNKSKFEIFIDVDCKKDEIKSLIKCLEQNVDNDFHVQEVDMISSNPNGIKCDSADRPNNESLDQNQIQIKAKKRAMTVDNLPWFPKYIKDLDKISNRVIMYGSELDADHPGFKDELYRKRRNQFSEIAYSYKHGNPIPKIEYTKDEITTWGNVYRELTKLYPTHACREFLENLPLLQKYCGYREDNIPQLEEVSQFLKNRSGFTLRPVAGYLSSRDFLAGLAFRVFHCTQYIRHPSDPFYTPEPDCCHELMGHVPLLADSSFAQFSQEIGLASLGASEEEVQKLATCYFFTIEFGLCHQDGELRAYGAGLLSSIGELKHALSTESNIQKFDPKLVMEQECLVTTFQNAYFYTPSFEDAKDKMRDFAKTIKKPFDVHYNPYTQMIEILDSTDSVTSVIENIKGELATITNALKKLNIYWYGSHRSEADQSI
>SwissProt__P04177 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 (Rattus norvegicus (Rat))
MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS
>BRENDA__A5YVV2 tyrosine 3-monooxygenase (EC 1.14.16.2) (Tribolium castaneum)
MAAVAAAQKNREMFAIKKSYSIENGYPARRRSLVDDARFETLVVKQTKQSVLDEARLRANDSSVDPEIDIEDKPAQKIDGEDDSGLTEEEVVLSNAIAEGPDAEKALQRAALILRLREGMNSLSRVLKSIEKHQGAVCHLETRPNQSDNNQLDALVKVEMTRVSLLQLIKSLRQSSSLEHCTLIGEDNISAKNPWFPRHASDLDNCNHLMTKYEPDLDMNHPGFADKEYRARRKEIAEIAFAYKYGDPIPYIQYTETETKTWGSVFNTVLELMPKHACSEYCRVFKMLQEEDIFTPDRIPQLEEMSNFLKRHTGFSLRPAAGLLTARDFLASLAFRIFQSTQYVRHKNTPYHTPEPDCIHELLGHMPLLADPSFAQFSQEIGLASLGASDAEIEKLSTVYWFTVEFGLCKESGVVKAYGAGLLSAYGELLHALSDKPELRPFEPAVTAVQPYQDQEYQPIYFVAESFDDMKDKFRRWVSAMSRPFEVRFNPHTGRVEVLDSVEKLETLVHQLNTEVLHLSNAINKMKAPSYQ
>BRENDA__A0A084W0Q1 tyrosine 3-monooxygenase (EC 1.14.16.2) (Anopheles sinensis)
MMAVAAAQKNREMFAIKKSYSIENGYPSRRRSLVDDARFETIVVKQTKQTVLDEARAKANEDKLPQEVQQTVEDQDNDEEEIRMVAVDDLPQKPEEHVPSANDEDKETDAGLTEEEVVLQNAASESPEAEKEVVRAAVVVRLRDGMGSLGRILKAVEGYHGTVVHLESRQSRSEGVAFDVLIKVDMARSNLLQLIRSLRQTQSFGSVSLLSENNVNVKAPWFPKHASELDNCNHLMTKYEPDLDMNHPGFADQVYRARRKEIAEIAFAYRYGDPIPHINYTETENKTWSAVFTRVKELMVKHACSEYIAVFKKLEEEKIFVNERLPQLQEMSDFLRRNTGFTLRPAAGLLTARDFLASLAFRIFQSTQYVRHINSPYHTPEPDCIHELLGHMPLLADPSFAQFSQEIGLASLGASDEEIEKLSTVYWFTVEFGLCKEKNEVKAYGAGLLSAYGELLHAISDKPEHRPFDPASTAVQPYQDQEYQPIYYVAESFEDAKEKFRRWVSTMSRPFEVRFNPHTERVEVLDSVDKLDTLVSQLNTELLHLTNAIEKLRQPFC
>PDB_2toh_A Tyrosine hydroxylase catalytic and tetramerization domains from rat
REDKVPWFPRKVSELDKCHHLVTPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKG
LYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDYLASLAFRVFQCTQYIRHASSPM
HSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLH
SLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSLEG
VQDELHTLAHALSAIS
>SwissProt__P24529 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 (Mus musculus (Mouse))
MPTPSASSPQPKGFRRAVSEQDTKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASAEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRALKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGEPIPHVEYTKEEIATWKEVYATLKGLYATHACREHLEAFQLLERYCGYREDSIPQLEDVSHFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFSDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIRRSLEGVQDELHTLTQALSAIS
>biolip__6zvpD Atomic model of the em-based structure of the full-length tyrosine hydroxylase in complex with dopamine (residues 40-497) in which the regulatory domain (residues 40-165) has been included only with the backbone atoms
SLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAMLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
>SwissProt__P07101 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 (Homo sapiens (Human))
MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
>PDB_6zn2_A Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic domain and an alpha-helix from the regulatory domain involved in dopamine binding.
VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGL
YATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMH
SPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHC
LSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGV
QDELDTLAHALSAIG
>PDB_2xsn_A Crystal structure of human tyrosine hydroxylase catalytic domain
MVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKG
LYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPM
HSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLH
CLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEG
VQDELDTLAHALSAI
>SwissProt__P70080 Tryptophan 5-hydroxylase 1; Tryptophan 5-monooxygenase 1; EC 1.14.16.4 (Gallus gallus (Chicken))
MIEDNKENKDHAPERGRTAIIFSLKNEVGGLVKALKLFQEKHVNLVHIESRKSKRRNSEFEIFVDCDSNREQLNEIFQLLKSHVSIVSMNPTEHFNVQEDGDMENIPWYPKKISDLDKCANRVLMYGSDLDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPEIEFTEEEIKTWGTVYRELNKLYPTHACREYLKNLPLLTKYCGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCTQYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASDEAVQKLATCYFFTVEFGLCKQEGQLRVYGAGLLSSISELKHSLSGSAKVKPFDPKVTCKQECLITTFQEVYFVSESFEEAKEKMREFAKTIKRPFGVKYNPYTQSVQILKDTKSIASVVNELRHELDIVSDALSKMGKQLEV
>SwissProt__A0A060X6Z0 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; Tyrosine hydroxylase; EC 1.14.16.2 (Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri))
MPISSSSSSSTKSMRRAASELERSDSVTSPRFIGRRQSLIEDARKEREAAAAAAEAAEATEQIVFEEEDGKALLNLFFTLRSSKTPALSRSLKVFETFEAKIHHLETRPCRKPRDSLEGLEYFVRCEVHLSDVSTLISSIKRIAEDVKTTKEVKFHWFPKKISELDRCHHLITKFDPDLDQEHPGFTDPVYRQRRKMIGDIAFRYKQGEPIPRVEYTEEEIGTWREVYSTLRDLYTTHACSEHLEAFNLLERHCGYSPENIPQLEDVSRFLRERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCVHELLGHVPILADRVFAQFSQNIGLASLGASEEDIEKLSTLYWFTVEFGLCKQGGIVKAYGAGLLSSYGELVHALSDEPERREFDPEAAAIQPYQDQNYQSVYFVSESFTDAKEKLRSYVAGIKRPFSVRFDPYTYSIEVLDNPLKIRGGLESVKDELKMLTDALNVLA
>biolip__3e2tA The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan
NIPWYPKKISDLDKCANRVLMYGSDLDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPEIEFTEEEIKTWGTVYRELNKLYPTHACREYLKNLPLLTKYCGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCTQYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASDEAVQKLATCYFFTVEFGLCKQEGQLRVYGAGLLSSISELKHSLSGSAKVKPFDPKVTCKQECLITTFQEVYFVSESFEEAKEKMREFAKTIKRPFGVKYNPYTQSVQI
>SwissProt__Q8CGV2 Tryptophan 5-hydroxylase 2; Neuronal tryptophan hydroxylase; Tryptophan 5-monooxygenase 2; EC 1.14.16.4 (Mus musculus (Mouse))
MQPAMMMFSSKYWARRGLSLDSAVPEDHQLLGSLTQNKAIKSEDKKSGKEPGKGDTTESSKTAVVFSLKNEVGGLVKALRLFQEKHVNMLHIESRRSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPESIWTEEEDLEDVPWFPRKISELDRCSHRVLMYGTELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNLPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKSFDPKTTCLQECLITTFQDAYFVSDSFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI
>SwissProt_P17289 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Bos taurus (Bovine)
MPTPNAASPQAKGFRRAVSELDAKQAEAIMSPRFVGRRQSLIQDARKEREKAEAAASSSESAEAAAWLERDGEAVLTLLF
ALPPTRPPALTRAIKVFETFEAHLHHLETRPAQPLRAGSPPLECFVRCEVPGPVVPALLSALRRVAEDVRAAGESKVLWF
PRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYPTH
ACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPAAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEP
ECCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLSEE
PEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPHAIRHALDGVQDEM
QALAHALNAIS
>metacyc__HS10374-MONOMER phenylalanine hydroxylase subunit (EC 1.14.16.1) (Homo sapiens)
MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK
>metacyc__HS06603-MONOMER Tryptophan 5-hydroxylase 2 (EC 1.14.16.4) (Homo sapiens)
MQPAMMMFSSKYWARRGFSLDSAVPEEHQLLGSSTLNKPNSGKNDDKGNKGSSKREAATESGKTAVVFSLKNEVGGLVKALRLFQEKRVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPENIWTEEEELEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI
>BRENDA__Q2HZ26 tryptophan 5-monooxygenase (EC 1.14.16.4) (Macaca mulatta)
MQPAMMMFSSKYWARRGFSLDSAVPEEHQLLGNLTLNKANSGKNDDKGNKGSSKNETATESGKTAVVFSLKNEVGGLVKALRLFQEKRVHMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPENIWTEEEELEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI
>biolip__4v06A Crystal structure of human tryptophan hydroxylase 2 (tph2), catalytic domain
LYFQSMLEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI
>PDB_4anp_A Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKS
LYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPM
YTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQY
CLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLD
>PDB_6pah_A Human phenylalanine hydroxylase catalytic domain dimer with bound l- dopa (3,4-dihydroxyphenylalanine) inhibitor
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKS
LYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPM
YTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQY
CLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_5pah_A Human phenylalanine hydroxylase catalytic domain dimer with bound dopamine inhibitor
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKS
LYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPM
YTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQY
CLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_4pah_A Human phenylalanine hydroxylase catalytic domain dimer with bound nor- adrenaline inhibitor
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKS
LYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPM
YTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQY
CLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_3pah_A Human phenylalanine hydroxylase catalytic domain dimer with bound adrenaline inhibitor
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKS
LYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPM
YTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQY
CLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_1mmt_A Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (fe(ii)) complexed with tetrahydrobiopterin and norleucine
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKS
LYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPM
YTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQY
CLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_1kw0_A Catalytic domain of human phenylalanine hydroxylase (fe(ii)) in complex with tetrahydrobiopterin and thienylalanine
VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSL
YKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY
TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYC
LSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_1j8u_A Catalytic domain of human phenylalanine hydroxylase fe(ii) in complex with tetrahydrobiopterin
VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSL
YKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY
TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYC
LSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_1j8t_A Catalytic domain of human phenylalanine hydroxylase fe(ii)
VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSL
YKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY
TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYC
LSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>PDB_1dmw_A Crystal structure of double truncated human phenylalanine hydroxylase with bound 7,8-dihydro-l-biopterin
VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSL
YKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY
TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYC
LSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVL
>BRENDA__Q8TEY0 phenylalanine 4-monooxygenase (EC 1.14.16.1) (Homo sapiens)
MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPQPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK
>BRENDA__Q8CGU9 tryptophan 5-monooxygenase (EC 1.14.16.4) (Rattus norvegicus)
MQPAMMMFSSKYWARRGLSLDSAVPEEHQILGGLTQNKATASKSEDKRSGKDTSESSKTAVVFSLKNEVGGLVRALRLFQEKHVNMLHIESRRSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPDNIWTEEEELEDVPWFPRKISELDRCSHRVLMYGTELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQDAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI
>BRENDA__B3VBV0 tryptophan 5-monooxygenase (EC 1.14.16.4) (Micropogonias undulatus)
MQPAMMMFSSKYWARRGLSLDSAMFDHQQQRHTGGQMSRRPSFCPINETPDKESAEDSGKTAVVFSLKNEVGCLVKALRLFQEKRVNLNHIESRVSRRITNEVEIFADCSCSKKEFNELLQHLKDHVNIISFNTPAHVWSAEADGDDVPWFPMKISELDQCSHRVLMYGSELDADHPGFKDEVYRQRRKYFVEVAMNYKFGQPIPRIEYTLEEVQTWGVVFRELTKLYPTHACREYLKNLPLLSKHCGYREDNIPQLEDVSLFLRERSGFTVRPVAGYLSPRDFLAGLAYRVFNCTQYVRHSTDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDDDVQKLATCYFFTIEFGLCKQDGQLRAYGAGLLSSIGELRHALSDQARVKMFDPKTTCNQECLITTFQEVYFVSESFEEAKEKMRDFAKTIKRPFSVYYNPYTQSIDLLKDTRSIENVAQDLRSDLTTVCDALGKMNTYMGI
>SwissProt_P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse)
MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAVSLIFSLKEEVGALAKVLRLFEENEINLTHIESRPSRLNKDEYEFF
TYLDKRSKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQ
FADIAYNYRHGQPIPRVEYTEEERKTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGF
RLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEK
LATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKTACQEYTVTEFQPLYYVAESFNDAKEKVR
TFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSINSEVGILCHALQKIKS
>SwissProt__P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 (Rattus norvegicus (Rat))
MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRPSRLNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKTACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSINSEVGILCNALQKIKS
>biolip__5fgjA Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453
QETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRPSRLNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKTACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSINSEVGILCNALQK