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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q54PK9 | MINGRYQKEDVVNNNNNLNLNLIEKTLNDLTIKNNTNINNNNTNNKNTNYYNNNNFNNNNNNNNNNNNNNNNINNNNNNNKYLNNSHNNNNNNNNNNNNNNNNNNNNNNNEINNNNNNVLSHSSLSGKGGSTTYETTSYTTSITSSRDTGTISTSYESSSSSSSSSSSSLYDDDEYSDYSDSSDSIDSYVNHRQALSKSQQQQHLQQQQDQPQPLHSSMGAISNEKPPSPTNQQQQQQHHHPKHNIELPKTSSFGLQPNSSIPHKKSRSDFDFIRTIGKGAYGKVKLVIEKETQLIFASKILNKKLIIKEKKAKYVNTEKTILDSLDNPNIVKLFYTFQDENNLYFILEYCPNGDLLGALKKAGCFSIDVVRFYAAEILIALEYLHGKGIAHRDLKPENILLGKNQHLKLSDFGSAKQLSIGSHHKGSRSGSFCGTAEYVCPELLTEKSAGVEADIWSYGCLLYQLVSGKLPFKGFNEYQTFLLITKREFSYPDNFDKCCMNLIDQLLDLDPYKRPTISEIKNHEFFSSIQDWSSIPSQTPPPIEQMVPQSPFPSPNSSLRLKKRSLSVGSPINSSLTYLSQPPIKPLNLDNSNIDYNDFENNQIISNNNNNNNNTTTTTTTTTTSANTSGSTNNTLYFTSPNVTSPPTSMSSNNTPRYINPLPTQSTTTTTTKPAYSSTPSSTILKSTPPPPILSSCSSNNLLGKSSNQQYQPFQFHQQQQQQQQQQQRERSSTTTPSPTFLSNHHNQHQKNLQQSFSSIDKSSFSTSSPMSSPRILLKPTELVLMDKDRKRNIREQQQIDQYQWSRFLLPNDEIILACGITEKRSGLITKKRQLIITDTPRIFYVDPVKMTQKGEITVDGSLSAQQKSSKHFIINSKGRSRHFYDLDGQSKLWVDLINELNMLSFK | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 102361
Sequence Length: 908
Domain: The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.
EC: 2.7.11.1
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Q86YL7 | MWKVSALLFVLGSASLWVLAEGASTGQPEDDTETTGLEGGVAMPGAEDDVVTPGTSEDRYKSGLTTLVATSVNSVTGIRIEDLPTSESTVHAQEQSPSATASNVATSHSTEKVDGDTQTTVEKDGLSTVTLVGIIVGVLLAIGFIGAIIVVVMRKMSGRYSP | Function: Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation . Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN . Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness . Interaction with CD44 promotes directional cell migration in epithelial and tumor cells . In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation (By similarity). Through binding with LGALS8 may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix . In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion . Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 . Required for normal lung cell proliferation and alveolus formation at birth (By similarity). Does not function as a water channel or as a regulator of aquaporin-type water channels . Does not have any effect on folic acid or amino acid transport (By similarity).
PTM: Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Disialylated at Thr-52; sialic acid is critical for platelet-aggregating activity and for CLEC1B interaction .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 16698
Sequence Length: 162
Domain: The cytoplasmic domain controls FRC elongation but is dispensable for contraction (By similarity). The cytoplasmic domain is essential for recruitment to invadopodia and ECM degradation .
Subcellular Location: Membrane
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Q62011 | MWTVPVLFWVLGSVWFWDSAQGGTIGVNEDDIVTPGTGDGMVPPGIEDKITTTGATGGLNESTGKAPLVPTQRERGTKPPLEELSTSATSDHDHREHESTTTVKVVTSHSVDKKTSHPNRDNAGDETQTTDKKDGLPVVTLVGIIVGVLLAIGFVGGIFIVVMKKISGRFSP | Function: Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation . Interaction with CD9, on the contrary, attenuates platelet aggregation and pulmonary metastasis induced by PDPN. Mediates effects on cell migration and adhesion through its different partners. Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness. Interaction with CD44 promotes directional cell migration in epithelial and tumor cells (By similarity). In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation . Through binding with LGALS8 may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix (By similarity). In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion . Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 (By similarity). Required for normal lung cell proliferation and alveolus formation at birth . Does not function as a water channel or as a regulator of aquaporin-type water channels (By similarity). Does not have any effect on folic acid or amino acid transport .
PTM: Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Disialylated at Thr-52; sialic acid is critical for platelet-aggregating activity and for CLEC1B interaction (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 18233
Sequence Length: 172
Domain: The cytoplasmic domain controls FRC elongation but is dispensable for contraction . The cytoplasmic domain is essential for recruitment to invadopodia and ECM degradation (By similarity).
Subcellular Location: Membrane
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Q8E3P1 | MEDQLTIFIISDSLGETAKAIAKACLSQFPGHDDWHFQCFSYINSQERLEQVFEEASQKTVFMMFSLVDVALASYAQKRCESEHYAYVDLLTNVIQGISRISGIDPLGEPGILRRLDNDYFKRVESIEFAVKYDDGRDPRGILQADLVIIGISRTSKTPLSMFLADKNIKVINIPLVPEVPVPKELRMIDSRRIIGLTNSVDHLNQVRKVRLKSLGLSSTANYASLERILEETRYAEEVMKNLGCPIINVSDKAIEETATIILEILKTNGQVAKNL | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 31068
Sequence Length: 276
EC: 2.7.11.32
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A3CMR4 | MNMKKEIIVYSISDSLGGTSQKLLSAVTAQYPDIIFNNSYRFPFINKEEELLAILRDAIKDDALVISTLVDSKLAAVAREFSQANGLAYLDLMHPFFEIIREKTGTSPIEVPGTLHRLDTEYFNKISAIEFAVKYDDGKAPQGFLDSDLVLLGVSRTSKTPLSIYLANKGYKVSNLPLIPEVPLPQVLEKVDPERIIGLLCEPEKLSKIRSNRLNSLGLTQSTSYTDLEKIYEELDYSKEVFKKYRAHVINITDKSIEETAFLIEDHLKKLR | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 30736
Sequence Length: 272
EC: 2.7.11.32
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B9DVG9 | MDDRLTIFIISDSLGVTARTIAKACIQQFPNHDNWQFERYSNINNKELLDKVLEKAKDKNVCLMFSLVDDDLARYAQERSEEEHFVYVDLLSNVIKAMSKLSGVEPLGQPGLLRKLDKHYFKRVEAIEFAVKYDDGKDPRGILKADLILLGISRTSKTPLSMYLADKHLKVVNIPIVPEVPLPKELNEVSPKKIVGLTNSVERLSQVRKERLRSLGVSGTASYANKDRIYEEAAYAEEVMRKLKCPIINVSDKAIEETATIILEMIKENQL | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 30807
Sequence Length: 271
EC: 2.7.11.32
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Q8UGD4 | MTHASLPLALTQGDPAGIGPDIAINAWAKRRENGVPPFIFIGDPDVVASRAALIGVPVNIETCDPESAVSLFERAFPILPLPVGFDVQAGQPHVGAAHATIKAIEMAVSLTVEGRAAAVVTNPIAKSVLYEAGFGFPGHTEFLADLALRQTGKPVTPVMMIAGPKVRVVPVTIHIPIKDVPTALTEELIVTTCRIIDTDLREKFGIAAPRLAVAGLNPHAGEDGALGTEDRDVVHPATIRLRKDGIDAFGPLPADTMFHDAARKRYDVAVCMYHDQALIPAKALGFDDSVNVTLGLPFIRTSPDHGTAFGIAGQGIASETSLVAALKMAAEIYARSRVGA | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 35727
Sequence Length: 340
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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O67019 | MNKKIGITLGDPAGIGPELILKISKHFKEKFTYVIYGEEKTLLEASKLTGIKLNYKKIEKVEEAKERGVYLIDLNVLKVPVVEPSVSSGKAAVAYLARAVADAIRGNIHGILTMPINKFWAKKAGFQYEGQTEFLAKASGTKDYAMMMYSEKLKVVLLTTHIPLKDVPNYVKKEEILKKVRLIRKEFLEKFKFEPLIKVLGLNPHAGEMGELGREEIEEIIPAVEEAKKEGIKVVGPLVPDVAFINPSEEDVFLCMYHDQGLIPFKMLAFDEGVNFTLGLPFIRTSPDHGTAYDIAWKNKARESSSLHALRLIEDLLDKI | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 35914
Sequence Length: 320
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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Q89ZK3 | MEENKIRIGITQGDINGVGYEVILKTFSDPTMLELCTPIIYGSPKVAAYHRKALDVQANFSIVNTASEAGYNRLSVVNCTDDEVKVEFSKPDPEAGKAALGALERAIEEYREGLIDVIVTAPINKHTIQSEEFSFPGHTEYIEERLGNGNKSLMILMKNDFRVALVTTHIPVREIATTITKELIQEKLMIFHRCLKQDFGIGAPRIAVLSLNPHAGDGGLLGMEEQEIIIPAMKEMEEKGIICYGPYAADGFMGSGNYTHFDGILAMYHDQGLAPFKALAMEDGVNYTAGLPVVRTSPAHGTAYDIAGKGLASEDSFRQAIYVAIDVFRNRQREKAARVNPLRKQYYEKRDDSDKLKLDTVDED | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 40325
Sequence Length: 364
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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B2IDU5 | MVMLDHPLAVTMGDPSGIGPEIIAKMYLRRPDKRNWIVVGDPLVMEHAIANLGVAVQIRRIATVEEAGCEDGVLNVLASSSLATLPAVGRVSAVSGQAAYDAIVTAIGLARQGTIRGIVTAPIHKEALAAAGIHYPGHTEILAEQGGAQHVAMMLANDEIRTVLVTIHCSLADAIRKADFPAQMQAIRLAHEGARALGIVQPRIAVAGLNPHAGEGGLFGDEEIRIITPAIAAARAEGIDATGPWPGDTVFMQARLGKFDVVVAQYHDQGLIPVKFMGLEKGVNITLGLPFVRTSPDHGTAFDIAGRGIADSSSLETAFDYATRLKVPTPFFSGAMS | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 35408
Sequence Length: 337
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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Q89MT9 | MANHAAKPLALTLGEPAGIGPDITIAGWLRRRELNLPAFYLLGDEALIARRAKTLDKTLGKALGAEIRIASVSAHEAAAAFTEALPVVATGERATAEPGQPDASSAPAALASIRQAVADVRAGRAGAVVTNPIAKSVLYRAGFRHPGHTEFLAELAAKDGRVPQPVMMLWSPRLAVVPVTIHVSLRDALSQLTSELIVSTVRIVATELKSRFGIARPRIAVSGLNPHAGEDGSLGHEEQTIIAPALKTLRNDGIDARGPLPADTMFHEAARSSYDCAVCMYHDQALIPIKTVAFDDAVNVTLGLPFIRTSPDHGTAFDIAGTGKANPASLIAALELASRMAAAKT | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 36145
Sequence Length: 345
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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P65680 | MRAKPLPPLAVSIGDPSGIGADVALAAWLKRCELSLPPFFLIADPKQLAARARHLGLAVDFAILSDPREAEAAFGERLPLLALKHSHTESPGKPLTENAAGVIEAIERAVELTLKGEAAAVVTCPIAKKPLYEAGFQHPGHTEFLAELAGHHLGKPVTPVMMLAGPQLRAVPVTIHIPLSEVPARLTTTEIVAVSRITANELRERFGIASPRLAISGLNPHAGEGGALGKEDDAIILPAIEQLIREGIDARGPLPADTMFHAPARATYDAAICMYHDQALIPAKALAFDETVNVTLGLPFIRTSPDHGTAFDIAGKGIARPDSLVAAMRLAQQLAENAASRNA | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 36193
Sequence Length: 343
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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A0RNS3 | MSLPKIAISVGDINGVGIEIALKSHDEIKNICSPIYFINNELLNSAANILKFTVPNDFEIFECGSSFNIKPGRVSKKSGKFSFVSFENAILYTQNKRAQALVTMPINKESWKKAGVPYVGHTDALGKYFGKNAIMMLGCEELFVALYTDHLALKDVSAKIKAKNLALFLVDFYNSSKFENIGVLGFNPHASDNETIGGKEEKEIIKAIKSANNRLKKEVFTGPLVPDAAFTKSSLKRCNRLVSMYHDVGLAPLKALYFDKSINVSLNLPIVRTSVDHGTAFDIAYKGKAETKSYIEAIKFAIKLCDY | Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 33925
Sequence Length: 307
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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Q9PN58 | MKKLAISIGDINSIGLEILVRSHEELSKICTPFYFIHESLLNKALKLLNLKLFNAKIVAFKDDKDYEFNFIKKENSLEIYSFCLPLGFKVDENFEIQAGEIDAKSGLYGFLSFKAASYFVYEKHAHALLTLPIHKKAWEDAGLKYKGHTDALRDFFKKNAIMMLGCKELFVGLFSEHIPLAKVSKKITFKNLSIFLKDFYKETHFKKMGLLGFNPHAGDYGVIGGEEEKIMEKAIAFVNAFLHSKKDEKFFKKALKDENLQKELLLNFKGKGVYLPYPLVADTAFTKTGLKNCNRLVAMYHDLALAPLKALYFDKSINVSLNLPIIRVSVDHGTAFDKAYKNAKINTKSYFEAAKFAINLHSKA | Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 41387
Sequence Length: 364
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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Q9A7N4 | MTSRPLAISAGDPAGVGAEIIAKAWRALRQDGPTFVVIGDAQLLASAGGGVKVRAVTRPQEAAQVFPDALPVLDIPVLSPVVYGRPSPSHAPQIIRWIETGVGLALSGAVSGLVTAPIAKAPLYEAGFQFPGHTEFLAELTAAASMVGARGPVMMLAAGDLRATLVTIHTALAKAPSALTTEAIINSGLVTAQALRKDFGIAEPRLAVAALNPHAGEGGALGREEIDIIAPAVEALRALGVQASGPAPADTLFHPEARARYDGVLCMYHDQALIPVKMLDFWGGVNITLGLPIVRTSPDHGTGFDIAGRGIARPDSLIAAIQLAAKIAARRGV | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 34206
Sequence Length: 333
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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A8ALP8 | MATVQRVVITPGEPAGIGPDLVVQLAQREWPVELVVCADARLLTDRAALLGLPLSLLPYSPNHPAKPQSAGTLTLLPTALRAPVTPGQLSVENGQYVVDTLARACDGCLQGEFAALITGPVHKGVINDAGVPFTGHTEFFEARSQAKKVVMMLATEELRVALATTHLPLRAVADAITPALLHEVIGILHHDLRTKFGLADPHILVCGLNPHAGEGGHMGTEEIDTIVPVLDDLRAQGMRLSGPLPADTLFQPKYLDHADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTALELAGRGQADVGSFITALNLAIKMIVNTQ | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 34928
Sequence Length: 329
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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Q47VJ9 | MTQRIAITPGEPAGVGPDLIITIAQQDWPVEMVVIASKALLQERSKALSLPLTIIDYDQHAPAKSQKSGSLTVLDVELTEPCVPGTLNSANGSYVVETLRIASEKNISGEFDAIVTGPVHKGLINKAGIAFSGHTEYFATQANCSDVVMMLATKGLRVALVTTHIPLAYVSKAITYERLQKVTRILHKDLQEKFGIKSPKIYACGINPHAGEDGHLGREEIEIMEPAFAELRADGIDIIGPLPADTIFQEKYLAEADAILAMYHDQGLPVLKYKGFGSSVNITLGLPFIRTSVDHGTALELAGKGTADSGSFIEAMNNAINLASNK | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 34947
Sequence Length: 326
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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Q2SJQ9 | MKIVADENIPLLQPFFGSMGEIHTLPGREISNQHLRDADVLLVRSVTKVDERLLENTGVKFVGSATIGCNHVDLDYLTSRGIGFSNAPGCNASAVVEYVVSCLSVLSEQLGFELEDKTVGIIGRGEIGGRLERALTLLGLEVKSNDPPKEAAGEQNLFSLEEVLQCDIITLHTPLTDSGSYPTRELLNATIIENLRPDQILINTCRGEVIDEAALKGRLQKGDGLTVALDVWNNEPAIDVELAMLCHFATPHIAGYTLDGRTAGTEIIYQHLSRYLGLPVRHKLGQFLPEPPLRRMAFSSGVDPDWALHTAIRASYDVRHDDSQLKRTLRLDAPMRAQEFDRLRREYRVRRGFDRIKIELKGGKADLLATLSAVGFNLSSK | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 42089
Sequence Length: 381
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q31IH6 | MTPSRTLVIDDAVPYAKELFSHLGNVISLPGKEINTEHLQNADALIVRSRTQVNSALLEHTNVSFVGSTVVGLDHVDQPYLKENAIEFYSAQGCNANSVSEYVITNLVNLAIEKKFTLSEKSLAIIGVGHVGKLVEKKARALGMTVLLNDPPRARQEMSDEFIDLDNALKSDIITVHTPLTKTGQDATFHLLSTDKLKKIQPHQILINAARGGIIDEQAWINTPTESNIIDCWENEPNINPDLYNQADIATPHIAGHALDAKIAGSEMVYRALCQHWQISPDDSWRRFLPPPPPPISLSLTGNHQEDIHNVLQQCYRPEEDDAAIRANNIVVTHKKYEYYRRHYPIHREWPQHRVIKTPDPTFNNLLYSLGFQLI | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 42174
Sequence Length: 375
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q5QUE2 | MKIVADQNIPALSDLLSGAGTLSYFSERIPPQKLLAEADALLVRSVTQVDEVLLEQAPELKFVASATIGTEHINLQALEERGIGFAHAPGANAQSVGEYVLCAVLNWLSDQPRYVADEIDVAIVGAGHTGKAAGKRLEALGLNVHYYDPPLCKKGVKFVHDHWQRVLTADIISCHVPLTRDGDFPTQHLFENTALQSLHSQQLLINASRGAVIDNNALLERVEQGERPSLVLDVWENEPEVLSGLVPYVDIATPHIAGHSLEGKVGGAVMISNALLEHFGKPADKTLSDVLPGKAWNERDAGGLNSLESLNLWAKEHYDLFRDDELFRQQGLTTEGFDSLRRNYRKESPRREFINQVVTCHNSEQYIQFLQLGFSARLLSK | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 42036
Sequence Length: 381
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q5WXZ0 | MNILADALLPGLDSAFPPPFTVTLYHKADEIPELLHHKDVLLCRSTLKINGDLLKHHQIKVVATATSGTDHIDFPFLESQNISIIDAKGCNATSVADYVVACLAYLDKQQLIQGKTAGIIGLGQVGTKVYERLNAAEFQLCLYDPPKATRDTSFQSCSLEDLLECDFLCVHAELHSNAPYPSLNLINRDFLKELKPGCIIINASRGGIINEEALLHLGSAILYCTDVYNNEPHIDNRIVSRATLCTPHIAGHSLEAKFAAVAIVSRKLHQMLGLPYPQFATPEKPYRLNDDSNWRELALSIYNPIHETLELKHAGNLSSAFLTLRKNHHHRHDFTTYFDSDSIKKYPLLG | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 38943
Sequence Length: 350
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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A6VXM3 | MKIIADENMPNAKVLFSHLGDVELVNGRTLTHEQVREADVLLVRSVTKVTKELLEGSSVRFVGSATIGVDHIDLDYLSKANIGFSSAPGCNAEAVADYVFSALSHLYLTKKINWLSKKIGVIGYGNVGKTVYTRFANMGCQVHVYDPIREKEGGSANFVSLDEILSCDVISLHAPLTHTGSYPTKGMIGRKELAKLSAGVTIISAGRGGVIDESALFDRHKQLNGNLHLVLDVWDGEPAINQKLIAIVDIATPHIAGYSKQGREKGTWMVYQALCQYLALDANVISKHDAISAGWLSFVNVSAEEPQEEMLARSMHAIYDVSRDDIRLRFKYRENKEKNVFDWLRKHYVERDEFNTCIIGVSSSDASNLMSAAGFSVDNK | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 41881
Sequence Length: 380
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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A1U1I8 | MLIVADENIPLLDSFFGDIGEIRRVNGRTLTPDQVKDADILLVRSVTRVDRQLLEGTRVRFVGTATIGTDHIDQTWLQEQGIGFAAAPGCNAVSVAEYVLSVLSLYAEKRGIEDWSSLTVGIVGVGNVGGELARMLERLDFTVKLCDPPRQEAEEERAEEFVPLAEALECDVVTLHTPLTRTGDHPTNRMIAGSELAALGQDQLLINAGRGEVIDGEALLARLQQADAPTVVLDVWEHEPRINPDLLDRVWLATPHIAGYSLEGKMQGTEMIYQALCRYLGLPVRKKAGQFLPEPALSKVSFTSSADEDEAVQVALRACYDPRRDDARLRLTMRGNPEERAQAFDRLRRDYPVRRECSSLKVQLKGSSKSIQDSFRAIGFKLKI | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 42533
Sequence Length: 384
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q7MV70 | MKIVAEASVPYLRGIVDPVADITYLHSDCFSPDTIRHARVLIVRSITKCTPALLQGTDVRLITTATAGFDHIDREYCESHGILWRNSPGCNATAVAQYVMCCLCRLALREGFSLKEKVMGIVGVGHVGGELKRLASAYGMEFLLCDPPRSEAEQDNSFLPLSRLVEQCDIISFHVPLTHEDPHATYHLIGEAFLRSCADKRPILINACRGAVADTQALIRAVKSGWLQALVIDCWEGEPDIDLSLLDLADIATPHIAGFSADGKANGARMCLEAITEVFGLEFPLLHTLAPPPPTHPIIDLSLFPDHRIERALLHTFDPLVPDRSLRASPKTFEEQRKAYPHPREMKAFTVVGATTEEAKILRGMDFIS | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 40669
Sequence Length: 369
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q1QWA6 | MNYDIADLRRDYAGETLSVESAPASPLDLFQTWFAAAREHETQDANAMTLATVDSQGLPHARVVLLKQLDDKGLVFFTNYQSHKGSELTNVPYAALVFWWPTLQRQIRIEGRVEKASAEVSDAYFANRPRDSQLGAWISQQSVEIPDRDWLEERKQRFEQVYGEQTVERPPHWGGYRVLPFLLEFWQGQPNRLHDRIRYRYHEQDAAWSKTRLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 25050
Sequence Length: 215
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
Q83D18 | MFRLDLLSDPLEQFKLWYDEAIRHETLHPDAMVLATADSKGKPSARNVLYKGISKGGFLIFTNYHSRKAHELDENPQAAWVFYWPKTYKQVRGEGRVERLTQEESEAYFETRSYESQIAAWVSEQSQEIPDREYLITRYKKYREKFQDDVRCPEFWGGFRLIPDRMEFWVGQEHRLHDRFCYLKENQEWKIIRLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 23636
Sequence Length: 196
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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B1WR90 | MDLTALREEYTRHGLTRDDLEDNPFKQFEKWFQQATEAELSEPNAMSLATASAKGEPSIRTVLLKYFDEKGFVFFTNYESRKAQQIEENPHVALLFLWLPLERQVKIQGTATKVSTAESLNYFTSRPRGSQLGAWCSAQSSVISSRKLLEMKFEELKYKFQHGEIPLPSFWGGYRVKPTRFEFWQGRPNRLHDRFSYTLTETDDTTWGIHRLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24939
Sequence Length: 214
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q0K7Z0 | MTQLADLRRSYVLGSLSETDVAPDPMSQFKRWFDEAVTAKLPEPNAMTLATVDADGQPSARIVLLKGIDDRGFTFFTNYESRKGLDLAANPRAALLFHWVQLERQVRVEGRVEKVSDDESDAYFATRPLGSRVGAWASAQSREVPGRDVLEQREQEYRSKFGENPPRPPHWGGYRLVPTALEFWQGRPSRLHDRIAFRLQPGGDWQIVRLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24081
Sequence Length: 212
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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B8HMK7 | MTISISDLRKDYRQQSLSETEVDPNPLQQFQTWFKQAIEAEILEPNAMTLATLSREGKPAARIVLLKEVDDRGFTFFTNYKSRKGEELAHDPWAALVFWWAELERQVRIEGSVSQVSAADSDRYFSSRPWGSRLGAWASEQSKAITGREVLEQNLRALEQEYRDREVPRPPHWGGYRLSPTLIEFWQGRPNRLHDRLCYRLQGDQWQLERLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24909
Sequence Length: 213
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q11U72 | MKTNLADIRKEYSSRSLDTKDILPSPVEQFRLWLNQALEAGALEATAMNLATVNEAGKPASRIVLLKGIEHGSFVFYTNYKSHKGSDITHNSFGALNFFWPELERQVRIEGKITKVSPEDSDTYFNSRPYQSKIGAWVSDQSKEVASREELESKITYYENKYPEGSVVPRPAHWGGYTLKPAYFEFWQGRPSRLHDRIVYDLEGDIRWNVFRICP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24745
Sequence Length: 215
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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C1D0Z0 | MTDLSTLRLSYTHGELRRADLNADPAQQFQSWLDAALRSGLREPYAMSLATADREGRPSVRTVLLRGIQDGGLTFFTNYESHKGHDLTDNPQAEVLFFWAEHERQVRAYGPVERLSSEDSAAYFHSRPRESQLAAHASDPQSAPVSNRAELETRLTALHERFAADQEVPCPEFWGGYRIQVQEWEFWQGRPNRMHDRFRYRRNDAGWHIDRLMP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24799
Sequence Length: 214
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q2NT03 | MTEQLIDIAALRREYTRGGLRRADLTAEPMDLFEQWLKQACAAQLPDATAMSVGTVDENGQPYQRLVLLKHFDRQGMVFYTNLGSRKAAHLAHNPRISLHFPWHVLERQVLVLGRAERLSVIEVMKYFHSRPRDSQIGAWVSRQSSRISSRGVLESKFLELKQKFAQGDVPLPSFWGGYRVSIEAMEFWQGGEHRMHDRFLYRRENGGWHIDRLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 25030
Sequence Length: 216
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q1GVE7 | MRAAAVKFRTCRSTTRVPRIMTARMSDDPLALFDSWFAEARASEPNDSNAMALATATPDGRPSLRMVLLKGHGPDGFVFYTNLDSRKGGELAANPHVALLFHWKSLRRQIRIEGSVAPVDNATADAYFATRSRDSQIGAWASDQSRPLDSRATFEARFAEMQARFAGQDVPRPPRWSGWRVTPERIEFWQDRAHRLHERTLFERTAIGWTKGYLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24512
Sequence Length: 216
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q9K3V7 | MGGVTDRDADSAVPTADPVPFDLASMRKQYRAEGLSETELAATPVEQFARWFKQAATDGGLFEPNAMVVSTADPEGRPSSRTVLLKHFDEQGFVFYTNYDSRKARELDANPHVSLLFPWHPMARQVVVTGVARRTGRDETAAYFRTRPHGSQLGAWASVQSSVVADRRALDGAYAELAARYPEGEQVPVPPHWGGFRVVPDAVEFWQGRENRLHDRLRYVAEGGGGWRVERLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 26012
Sequence Length: 234
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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P74211 | MDGVSLADLRLNYTQGGLIEAEVADHPFAQFHIWLQQAIAAELPEPNAMTLSTLSEEGHPVGRMVLLKGLDERGFVFYTNYDSAKGQQLTAHPWAGLVFWWAALERQVRVDGQVEKIDPAESDAYFQSRPRGSQLGAWASPQSRIVGDRQELEDNLARWEKQYENQSIPRPPHWGGFRVIPHRIEFWQGRPSRLHDRLQFNLLDGQWHRQRLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24587
Sequence Length: 214
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q47TD1 | MDYSDPAELRESYDGAPLDPRGLAPQPMDQFHAWFTEACEAELSEPNAMVLSTVDPDGAPSARTVLLKGYDRRGLRFFTNYRSRKGVALAREPRACVVFPWHAIRRQVIVYGFAERLSDEENDAYFAQRPHGSQLGAWASEYQSAPVADRAELDRAYARCAEQWPPGTPVPRPEYWGGFLLVPQEVEFWQGRSDRMHDRFRYRLVSGTPSEGAWQIDRLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 25197
Sequence Length: 221
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q8DLZ5 | MTRIADLRRDYRRQRLLESDAAEDPIEQFRLWLTDAVNAELPEPNAMTLATVGLDGMPAARLVLLKEVDDRGFVFFTNYRSRKGRELAAHPKAALVFWWAELERQVRIEGNVEQISAAESDAYFQSRPLGSRWGAWASQQSEVLASYAELEARLAAVEAHYGENVPRPEHWGGYRVLPTLIEFWQGRPNRLHDRLCYRRQGDHWQRVRLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24534
Sequence Length: 211
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q9KKM4 | MDLSDIRREYIHGGLRRKDLQANPIDQFNLWLQQAIDANLSDPTAMTVATVDEHGQPFQRIVLLKNVDDAGFVFYTNLGSRKAQHIAHNNKISLHFPWHPLERQVHITGVAEKLTAMENMKYFMSRPKESQIAAIASHQSSRISARGVLEGKYLELKQKFANGEIPVPSFWGGYRIRPESLEFWQGGEHRLHDRFLYSRQDDNWTVDRLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24363
Sequence Length: 211
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q16AJ0 | MSDQKKLRLGVNIDHVATVRNARGGAYPDPLRAARIAEEAGADGITAHLREDRRHISDADIEGLMDVLSVPLNFEMAATDEMQQIALRHKPHAVCIVPEKREERTTEGGLEVAREENVLAHFIAPLREAGCRVSIFIAAEQRQIEAAHRIGAEVIELHTGAYCDAHAEGDFAQRDAELARLRDMATFAHGLGLEVHAGHGLTYDTVQPIAAFPEVIELNIGHFLIGESIFRGLEPAIAEMRRLMDAARA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 27341
Sequence Length: 249
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
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Q58090 | MKKGTDLLKKGFAKMVKHGVVMDVTNVEQAQIAEEAGAVAVMALERVPADIRAAGGVARMSDPALIEEIMDAVSIPVMAKCRIGHTTEALVLEAIGVDMIDESEVLTQADPFFHIYKKKFNVPFVCGARNLGEAVRRIWEGAAMIRTKGEAGTGNIVEAVRHMRLMNEAIAQLQRMTDEEVYGVAKFYANRYAELAKTVREGMGLPATVLENEPIYEGFTLAEIIDGLYEVLLEVKKLGRLPVVNFAAGGVATPADAALMMQLGSDGVFVGSGIFKSENPLERARAIVEATYNYDKPDIVAEVSKNLGEAMKGIDITQISEAEKMQYRGD | Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 35856
Sequence Length: 330
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q6M115 | MKKLGTDLLKRGFAKMVKHGVVMDVTNVEQALIAEEAGATAVMALERVPADIRVQGGVARMSDPEMILEIKDAVSIPVMAKARIGHYVEAQVLESIGVDMVDESEVLTPADEVNHIDKRAFTAPFVCGARNLGEALRRIDEGAAMIRTKGEAGTGNVVEAVKHMRAVNEGIARVIGYKEMGLEAELIQMARNELKVPMELISEVAELKRLPVVNFAAGGIATPADAALMMQMGCDGVFVGSGIFKSGNPAVRAKAIVEATYNFDKPEVIAEVSKNLGEAMVGINIDEIPEEMLLAKRGI | Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 32022
Sequence Length: 299
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q4JVD5 | MIIGVLSVQGGFVEHMRSIERLGHEARAVRRAEQLEGLDGLIMPGGESTTMSKLLELGGMLEPLRELIADGLPVFGTCAGLILLADRVLDTRSDAHSLHAMDITVRRNAFGRQVDSFETQLPFGDIDTPVEAVFIRAPKVEEVGDGVEVVSTLPDGTVVGVRQGNVLGCSFHPELSEDDRVHEYFLRMVKQRGVE | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21290
Sequence Length: 195
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q6A947 | MAPLVGVVALQGGFAEHIEVLESLGANTRRVRRSADLQGLDGIVLPGGESTVIDKLMRSFSLAEPLKDAVRRGLPVLATCAGLVVLATDLEDAAKGQHTLSLLDVTVRRNAFGSQLDSFEGTLDIDGVGDGVSATFIRAPVITRVGPGVEVIAQLPDEAGNVSGAIVGVRQRNVLALSFHPEETDDDRVHRTWLRQVSEEV | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21324
Sequence Length: 201
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q3Z8V9 | MKIGVLALQGAFREHINMLRTLGAEAVEVRKAEELAELSGLIIPGGESTTITKLLYTFGLAKPVKDLARNGMPVWGTCAGMICLAKELSGDISGVKTLELMDITVRRNAFGRQVDSFEAMLKVKALEGGDFPAVFIRAPLVEKTGQWVEVLAKLPDGTMVAVRENNLLATSFHPELSADNRFHRYFVQMAKDYKP | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21408
Sequence Length: 195
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q9RUL8 | MTVGVLALQGAFREHRQRLEQLGAGVREVRLPADLAGLSGLILPGGESTTMVRLLTEGGLWHPLRDFHAAGGALWGTCAGAIVLAREVMGGSPSLPPQPGLGLLDITVQRNAFGRQVDSFTAPLDIAGLDAPFPAVFIRAPVITRVGPAARALATLGDRTAHVQQGRVLASAFHPELTEDTRLHRVFLGLAGERAY | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 20691
Sequence Length: 196
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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B1I158 | MLKVGILALQGAFLEHARAVEACGALPVEIRKPGQLGDCRALIIPGGESTAIGKLMAAFDLLEPVRRFGAEGRPVFGTCAGMVLLAKDIEDSEQTRLGLMDITVRRNAFGRQVDSFEAKIHVPVLGDEPVRGVFIRAPHVTAVGPGVEILAAFEEKIILVRQDRLLAGAFHPELTADMRLHRYFLDFVD | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 20567
Sequence Length: 189
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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A4J0G0 | MVIGVLALQGAFIEHQKSLAACGVDSIQVRKPHQLEDIQGLIIPGGESTTMGKLMNQFELFEPIVEKAHNGLPLFGTCAGMIMLAKDIAGSTQPRLGLMDIEVERNAFGRQVESFETELTISELGEAPVRAVFIRAPYIKSVAANVKVLAKYNEKIVLAQQDHYLVAAFHPELTNDVRLHQHFLKMIK | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 20761
Sequence Length: 188
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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B8E120 | MRIGILAIQGSVVEHEKMLKRLEVETVLVKKPEHLDIINGIILPGGESTTFFTLLENRLLFDVLREKLANGLPAMGTCAGLILLANRIENHPDQKTLKVLDITVSRNAYGRQRESFSTYIKIPILGEKEFECVFIRAPQIVEIGKNVKVHATFENKPIFVEEGNILGLTFHPELTDDLRIHEYFLKRCSE | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21578
Sequence Length: 190
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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B1YGC2 | MVIGILGVQGAVREHQEMLHLLGVKTMIVKSSADLDGIDGLIFPGGESTTIRRLIDRYGLLDVLRRQADTLPMFGTCAGMILLASELTEGPSHLGAIPMTVRRNAFGRQIDSFETSLNVEGAGQDIEAVFIRAPFVEQVGEGVRVLAAIGIAAVVVETDLHLACSFHPELTSDRRLHDYFIQKIRRRTAVSV | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 20920
Sequence Length: 192
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q2JD98 | MSGPRIGILALQGDVREHARALTEAGARPVAVRHAVELAEVDGLVLPGGESTTIGRLLRVFELLEPLRAAVAAGLPVFGSCAGMILLARDVVGGRPDQPLIGGLDIVVRRNAFGRQVDSFEAHLEVVGVAGPPVHAVFIRAPWVEKAGDAVEVLARVAEAPVTVRQGPLLATAFHPELTGDARVHRLFVDSVRSSGSGR | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 20870
Sequence Length: 199
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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P06300 | MAWSRLMLAACLLVIPSEVAADCLSLCSLCAVRTQDGPHPINPLICSLECQDLVPPSEEWETCRGFWSFLTLTASGLHGKDDLENEVALEEGYTALTKLLEPLLKELEKGQLLTSVSEEKLRGLSSRFGNGRESELLGTDLMNDEAAQAGTLHFNEEDLRKQAKRYGGFLRKYPKRSSEMTGDEDRGQDGDQVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQENPNTYSEDLDV | Function: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity).
PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
Sequence Mass (Da): 28079
Sequence Length: 248
Subcellular Location: Secreted
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Q13113 | MSALSLLILGLLTAVPPASCQQGLGNLQPWMQGLIAVAVFLVLVAIAFAVNHFWCQEEPEPAHMILTVGNKADGVLVGTDGRYSSMAASFRSSEHENAYENVPEEEGKVRSTPM | Function: May play an important role in tumor biology.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12227
Sequence Length: 114
Subcellular Location: Membrane
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P48612 | MKLLGKYVDKGMQGNVTLVPEESEDMWHAYNLIAKGDSVRSTTIRKVQNETATGSSTSSRVRTTLTIAVESIDFDTQACVLRLKGRNIEENQYVKMGAYHTLDLELNRKFELRKPEWDTIALERIEMACDPTQSADVAAVVMQEGLAHVCLITASMTLVRSKIEVSIPRKRKGSVQQHEKGLAKFYEQVMQSILRHVNFDVVKCVLIASPGFVRDQFYDYMFQQAVKMDYKLLLDNKSKFMLVHASSGFKHSLREILQDPAVLAKMSDTKAAGEVKALEQFYMMLQCEPAKAFYGKKHVLQAAESQAIETLLISDNLFRCQDVSLRKEYVNLVESIRDAGGEVKIFSSMHISGEQLAQLTGIAALLRFPMPELEDSDDDDDEDGAAGGVADSDSD | Function: Component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway . In the Pelota-HBS1L complex, pelo recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel. Following ribosome-binding, the Pelota-HBS1L complex promotes recruitment of pix, which drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (By similarity). Required prior to the first meiotic division for spindle formation and nuclear envelope breakdown during spermatogenesis . Together with HBS1, promotes spermatid individualization during spermatogenesis . Required for ovarian germ line stem cell self-renewal and oocyte development during oogenesis . Together with HSB1, required for transposon silencing in the ovary and testis . As part of the Pink1-regulated signaling, is recruited to damaged mitochondrial and is required for recruitment of autophagy receptors and induction of mitophagy . Required for normal eye patterning and for mitotic divisions in the ovary .
Sequence Mass (Da): 44212
Sequence Length: 395
Domain: The PGF motif may be involved in the interaction with HBS1 and is required for silencing of germline transposons.
Subcellular Location: Nucleus
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A2BL82 | MKILAVDTKRGLVRVVPETTDDIWLLSTVIQPGDLVRAKTLREIHFGDRGSGRSSRIPMVLTVRVEAVEFQAFTTRLRIRGIVIEGPEKYGVVGKYHTLSIEPGRELDIVKPSGWPQVLIEKLKRGSYNVAAVVVAVDYDDYAVAVVRGQGVKILASGGLHLPGKDDPTREDKLREAVTVIAKTTADVARRENALLVVAAGPGTVKNLVAEKLRGLVQGVKILVDNVSMGGEAGVFEEVRRGIMRQALQDAAVVEAERILEEFERRLAKEPGRIAYTLEQVYRAAEMGAVEELLILDETLHHPDPEVRARVDELLRLADATRAKIHFVSVESPVGYKVKALGGVIALLRYAINFAGETGG | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Sequence Mass (Da): 39374
Sequence Length: 360
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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A8A935 | MRVLEVNESKGEVKVRVEDEEDVWILHSALRPGDLVRARTARSVAGSSGKEKIPMTLTIKVTGSEFQAFSNVLRVKGVVVEGPDKFGLIGSHHAIKVYPGKEITIIRERGLAQLLERLKKGEERKPQVPVLAVDYDEYSLAVVRGQGIEWVFEGSLRLPGKGDEGREAATERKINELAKRVSEELKLRNLDHVVVVGPGFLKDKVAQRLSEEGFKVKVDSASSGGRAGVLEAIRKGSLRGVAKELESIKALEALEEFVKHVARGDGYALYGVDDCMTAAQANAVKTLIISDDLLHSPDLGERAVELVELAEKKGAEVIIVPKGTEAWERLRPFGDVVCLLRFPISL | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Sequence Mass (Da): 37928
Sequence Length: 346
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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B1L659 | MRILEEDLKRGLVKLRVDNLNDIYWLASIIEEGDLITMKTLRRVKQEGIRADSGERIPMILTIEVDKVKLDPYSSRLRISGVVRVGPDKFGIQGQHHTFSVDEGSSLTIVKKEWRKTHLEILKRAESMSEKGEVLLVAMDDEGATIAKAGSMRVEEIAYIRSRLPSKMDTRGREGEERRYFSEILDTLRELYSKIKPRAIVVGGPGFFKDRFLSYARAKDPEMGEKMREGDASNATFSGVLEMIRRGEADKVLRELDLAKDMAAVEEIFELLSKNSDLVTYGVDEVLEAVNQGAAEIVLISASVFFDPDMRDKVFSLIEGCERTRAEFRIIDSTSEPGEKLDAIGGVAAKLRYRI | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Sequence Mass (Da): 40054
Sequence Length: 355
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q8TSZ1 | MRVTNRSLRGREGEIAITAETLDDLWHLKYIIEKGDLVFALTKRKADSASDKLRPEKVEKVKVRLGIRVEEMEFHKFANRLRIHGPIEHGMDVGSYHTLNVEIGTNISIIKERWKNDQLQRIQDAEEAGKRPKVVIVAVEEGDADIGFVRHYGIEVYSHIRQSSGKRENGLRSEFFREIVDQLRHAVPEDASIVIAGPGFTKEDFLKYFHETEPEMASKALTEDTSMIGMSGFQEVLRRGAVDRIMQESRIARESSLMEDLLREISMDGKAAYGFADVKNALKYGAVETLLIADETLREGREKGEDIDKVLMEVEQAQGKVVVFSTAFEPGEKLHKLGGVAALLRFKVTG | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Sequence Mass (Da): 39525
Sequence Length: 350
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q2FQH4 | MKAEIEELQRSFGEIRLFPENSDDLWHLHNLITPGSLVYATTLRSVEGSQDKIRPEKQEKRPVRLGIRVEDVEFHEYSIRLRVFGTIESGVDIGSHHTLNLEPGYEISVIKSWSGSDLERIDRAIKGSTSEAIHILTVEEGEAELYRVQSYGPKQVWSLAAGSGKTAEVSSREEFSEAVVSQVSQLTGPLVIAGPGFVKEEIIAKFKRKNPSRSAPLVIGDTRAGGRRAVQEVIGQGILEKLNGDLQLAREVTCLDELMRRIGKDEPVAYGIDAVRDATGCGAVQTLMVVDTLLRDPDAADLIRQAEAMRSEVVIFSSRFEPGERLAGLGGIAALLRYSIA | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Sequence Mass (Da): 37492
Sequence Length: 341
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q57638 | MKIIEEIPQKNIIKLMPENLDDLWVLYNIIEEGDKIFAVTERRVQDKGDVIRADRGAKRKMFLGIEVKNVEFDENTKRVRILGTIIHGPDDVPLGSHHTIEIKPFDELSIEKNWKKWQIERIKEAIESSKRPKVLVVVMDDEEADIFEVRDYSIKEICSIKSHTSKKLDYKINEELKKEYYHEIAKVLSEYDVDNILVAGPGFAKNSFYNFISSQYPELKNKIVVESISTTSRAGLNEVIKRGIINRIYAESRVAKETQLIEKLLEEIAKKGLAVYGIDEVKKALEYSAIDTLLVSDSLVRNHEIEKIIDTTEEMGGKVVIVSSEHDAGKQLKALGGIAGLLRFPIE | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Sequence Mass (Da): 39624
Sequence Length: 347
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q8TZ98 | MKVVEKDLDKGYIEVLPETLDDLWHLYHVVRKGDLVFALERRRVKDERAETIRRDKGERKPVYLGVRVEDVEFDKYANRLRIKGVIEHGPESGSHHTVNVTTGKRIKIVKDEWERKDLERIEEAEMSRPPVMLVAVDTGEGTIGIVRDYGLDVVARVRHNVPGKRGGDRRAEMRKFFHRLADEIERIAEEEGVEHIVVGGPGFVKSDFAEFLREERDIPAHVEDTGSAGEAGLIEMIRRGAVERAVEESRVAEEVKHLEEVFKRIGKGDDKVAYGVRECLKAAEFGAIDVLLVADEKFREAMVEGEEDVLNAVKYAERTGAEVLIVSTEHEWGERLRELGGIAALLRFSIPTG | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Sequence Mass (Da): 40007
Sequence Length: 353
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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I6Y4D2 | MIVGVLVAAATPIISSASATPANIAGMVVFIDPGHNGANDASIGRQVPTGRGGTKNCQASGTSTNSGYPEHTFTWETGLRLRAALNALGVRTALSRGNDNALGPCVDERANMANALRPNAIVSLHADGGPASGRGFHVNYSAPPLNAIQAGPSVQFARIMRDQLQASGIPKANYIGQDGLYGRSDLAGLNLAQYPSILVELGNMKNPADSALMESAEGRQKYANALVRGVAGFLATQGQAR | Function: Cell-wall hydrolase that hydrolyzes the amide bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides . Is able to hydrolyze the cell walls of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli DH5alpha, E.aerogenes, L.acidophilus, B.thuringiensis, B.pumilus, B.subtilis and E.coli W3110), thereby showing that it is a cell-wall hydrolase with broad-spectrum activity . May have a role in peptidoglycan fragment recycling .
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 24836
Sequence Length: 241
Pathway: Cell wall degradation; peptidoglycan degradation.
Subcellular Location: Periplasm
EC: 3.5.1.28
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A0A146F0J0 | MVNTSLLAALTAYAVAVAAAPTAPQVKGFSVNQVAVPKGVYRHPAAQLAKAYGKYHATVPTQVAAAAAATGSVTTNPTSNDEEYITQVTVGDDTLGLDFDTGSADLWVFSSQTPSSERSGHDYYTPGSSAQKIDGATWSISYGDGSSASGDVYKDKVTVGGVSYDSQAVESAEKVSSEFTQDTENDGLLGLAFSSINTVQPTPQKTFFDNVKSSLSEPIFAVALKHNAPGVYDFGYTDSSKYTGSITYTDVDNSQGFWSFTADGYSIGSDSSSDSITGIADTGTTLLLLDDSIVDAYYEQVNGASYDSSQGGYVFPSSASLPDFSVTIGDYTATVPGEYISFADVGNGQTFGGIQSNSGIGFSIFGDVFLKSQYVVFDASGPRLGFAAQA | Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A (By similarity). Hydrolyzes myoglobin, hemoglobin and other natural proteins. Hydrolyzes equine myoglobin between positions 'Met-1' and 'Gly-2', 'Lys-43' and 'Phe-44', and 'Leu-70' and 'Thr-71' .
Catalytic Activity: Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.
Sequence Mass (Da): 40623
Sequence Length: 390
Subcellular Location: Secreted
EC: 3.4.23.18
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Q12567 | MVVFSKTAALVLGLSTAVSAAPAPTRKGFTINQIARPANKTRTVNLPGLYARSLAKFGGTVPQSVKEAASKGSAVTTPQNNDEEYLTPVTVGKSTLHLDFDTGSADLWVFSDELPSSEQTGHDLYTPSSSATKLSGYSWDISYGDGSSASGDVYRDTVTVGGVTTNKQAVEAASKISSEFVQDTANDGLLGLAFSSINTVQPKAQTTFFDTVKSQLDSPLFAVQLKHDAPGVYDFGYIDDSKYTGSITYTDADSSQGYWGFSTDGYSIGDGSSSSSGFSAIADTGTTLILLDDEIVSAYYEQVSGAQESYEAGGYVFSCSTDLPDFTVVIGDYKAVVPGKYINYAPVSTGSSTCYGGIQSNSGLGLSILGDVFLKSQYVVFNSEGPKLGFAAQA | Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A.
Catalytic Activity: Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.
Sequence Mass (Da): 41298
Sequence Length: 394
Subcellular Location: Secreted
EC: 3.4.23.18
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Q9GMY6 | MKWLLLISLVALSECAIVKVPLVRKKSLRQNLIEHGLLNDFLKNQSPNPASKYFPQEPTVLATQSLKNYMDMEYFGTIGIGTPPQEFTVIFDTGSSNLWVPSVYCSSPACSNHNRFNPQESSTYQGTNRPVSIAYGTGSMTGILGYDTVQVGGIADTNQIFGLSETEPGSFLYYAPFDGILGLAYPQISASGATPVFDNMWNEGLVSQDLFSVYLSSDDQSGSVVMFGGIDSSYYSGNLNWVPVSVEGYWQITVDSVTMNGQAIACSDGCQAIVDTGTSLLAGPTNAIANIQSYIGASQNSYGQMVISCSAINSLPDIVFTINGIQYPLPPSAYILQSQQGCVSGFQGMNLPTASGELWILGDVFIRQYFAVFDRANNQVGLAPVA | Function: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
Catalytic Activity: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
Sequence Mass (Da): 41551
Sequence Length: 386
Subcellular Location: Secreted
EC: 3.4.23.1
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P00793 | SIHRVPLKKGKSLRKQLKDHGLLEDFLKKHPYNPASKYHPVLTATESYEPMTNYMDASYYGTISIGTPQQDFSVIFDTGSSNLWVPSIYCKSSACSNHKRFDPSKSSTYVSTNETVYIAYGTGSMSGILGYDTVAVSSIDVQNQIFGLSETEPGSFFYYCNFDGILGLAFPSISSSGATPVFDNMMSQHLVAQDLFSVYLSKDGETGSFVLFGGIDPNYTTKGIYWVPLSAETYWQITMDRVTVGNKYVACFFTCQAIVDTGTSLLVMPQGAYNRIIKDLGVSSDGEISCDDISKLPDVTFHINGHAFTLPASAYVLNEDGSCMLGFENMGTPTELGEQWILGDVFIREYYVIFDRANNKVGLSPLS | Function: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
Catalytic Activity: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
Sequence Mass (Da): 40432
Sequence Length: 367
EC: 3.4.23.1
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C5PEI9 | MQNRPRVFDSAMNLSPNMHFLSLMPGLLLLSLQVHTSPTPLKKTIRSVRIERIRQPNYVPDGPGALKKAYAKFGIIPSGISFDSFEDFTPFSSDNVRNTVSKAMQANETGIVTNTPTNNDVEYLSPVTIGGQKFVMNLDTGSSDTWVFNTQLSEDAKRGHSIFDPAKSKAFSDLEDATFNITYGDASFAFGRVGIDTVDIGGATVQKQAVGLPTDVSGSFILDQASDGLIGLGFDELNTVEPQQQKSFFTNLAANLDEPVLAAQLKKGAPGSYEFGSIDETKFKGDLVTIPVNNSRGFWEVKSTMFKVGKDEQLHRITKGVGSAIADTGTTLMLVNEEIVNSYYDQVDNARSVYAAGGFIFPCNATLPDLYVSLGDTHLARIPGDLMNFSKVGLSTETGEELCFGGVQSNSGSGLQVFGDVLFKAIFVVFDLRGPSLHVAGHA | Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions.
Sequence Mass (Da): 47804
Sequence Length: 443
Subcellular Location: Secreted
EC: 3.4.23.-
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P94870 | MAHELTVQELEKFSADFNKNPKNKVVARAAQRSGVLEASYNDRVQSELTRVFSTELDTDNVTNQKHSGRCWLFATLNVLRHEFGKKYKAKDFTFSQAYNFFWDKIERANMFYNRILDSADMPLDSRQVKTDLDFAGTDGGQFQMAAALVEKYGVVPSYAMPETFNTNDTTGFATALGDKLKKDALVLRKLKQEGKDDEIKKTREKFLSEVYQMTAIAVGEPPKKFDLEYRDDDKKYHLEKDLTPLEFLHKYLGGVDFDDYVVLTNAPDHEYDKLYGLPAEDNVSGSIRIKLLNVPMEYLTAASIAQLKDGEAVWFGNDVLRQMDRKTGYLDTNLYKLDDLFGVDLKMSKADRLKTGVGEVSHAMTLVGVDEDNGEVRQWKVENSWGDKSGAKGYYVMNNEWFNDYVYEVVVHKKYLTDKQKELAEGPITDLPAWDSLA | Function: Can hydrolyze internal peptide bonds in Met-enkephalin and bradykinin; however, hydrolysis of alpha-, beta-, and kappa-caseins is not detected.
Sequence Mass (Da): 50022
Sequence Length: 438
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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P65811 | MGSRRFDAEVYARRLALAAAATADAGLAGLVITPGYDLCYLIGSRAETFERLTALVLPAAGAPAVVLPRLELAALKQSAAAELGLRVCDWVDGDDPYGLVSAVLGGAPVATAVTDSMPALHMLPLADALGVLPVLATDVLRRLRMVKEETEIDALRKAGAAIDRVHARVPEFLVPGRTEADVAADIAEAIVAEGHSEVAFVIVGSGPHGADPHHGYSDRELREGDIVVVDIGGTYGPGYHSDSTRTYSIGEPDSDVAQSYSMLQRAQRAAFEAIRPGVTAEQVDAAARDVLAEAGLAEYFVHRTGHGIGLCVHEEPYIVAGNDLVLVPGMAFSIEPGIYFPGRWGARIEDIVIVTEDGAVSVNNCPHELIVVPVS | Cofactor: Binds 2 manganese ions per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39440
Sequence Length: 375
Subcellular Location: Cell membrane
EC: 3.4.13.-
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P58493 | MSKRLLLLSNSTNIGEEYLFYARQEIKNFLGSSVKKIAFIPFAAVTSTYQHYSEKVRKVFQDIGYEFDAIHLVESSHELIKNAEAVVVGGGNTFHLIHCLHETKLLDDIRNKVSNGTPYIGWSAGSNVACPTIKTSNDMPIIEPISFQGLNLVPFQINPHYTNAVIPNHNGETREQRLEDFLVLNPDIYVVGLPEGTMLKIEDSSIRLIGNKTIYLFKFGEEKQEYYPHDNLDFLLERASFT | Function: Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.
Catalytic Activity: Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Sequence Mass (Da): 27458
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 3.4.13.21
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Q9CNH7 | MKNMLLMSGSKYQNTDYLVHTLPWLQDFLADYQGKTVAFVPYAGVRQSYDEYELKVQKALAELNVAILSVHRAEKHAEIIEKADVIAIGGGNTFCLLKGMYEHHLLPLIREKVQSGTPYFGWSAGANVAGRSIMTTNDMPITYPPSFDALNLFPHQLNPHFISGKPAGHNGESREERLAEFLIVNPTANVYALPEGTALHIQGQQARVLGQHDVLLFSENMQLATLPVNSVFDY | Function: Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.
Catalytic Activity: Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Sequence Mass (Da): 26058
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 3.4.13.21
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P36936 | MELLLLSNSTLPGKAWLEHALPLIANQLNGRRSAVFIPFAGVTQTWDEYTDKTAEVLAPLGVNVTGIHRVADPLAAIEKAEIIIVGGGNTFQLLKESRERGLLAPMADRVKRGALYIGWSAGANLACPTIRTTNDMPIVDPNGFDALDLFPLQINPHFTNALPEGHKGETREQRIRELLVVAPELTVIGLPEGNWIQVSNGQAVLGGPNTTWVFKAGEEAVALEAGHRF | Function: Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.
Catalytic Activity: Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Sequence Mass (Da): 24769
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 3.4.13.21
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A1S5J3 | MNIRALLLSASRVGDTPYLEHTLPFIAPLTEHARNWVFIPYAGISLGYDVYLEKVREGLRNLNINISGIHEHADPRQAIRDADGIFVGGGNTFHLLHELYRYDLLFVIREQVEAGKPYVGWSAGSNIAGLSIRTTNDMPIIEPPSFTALGLLPFQLNPHYTDYQAPGHNGETRAQRLLEFTMVDPLTPVVGIQEGSALYRQGDKLTLLGDKEAYFFKGSVQKSPIAAGADLSELL | Function: Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.
Catalytic Activity: Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Sequence Mass (Da): 26018
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 3.4.13.21
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P55179 | MKEEIIERFTTYVKVDTQSDESVDTCPSTPGQLTLGNMLVDELKSIGMQDAAIDENGYVMATLPSNTEKDVPTIGFLAHVDTATDFTGKNVNPQIIESYDGKDIVLNEQLQVTLSPDQFPELSGYKGHTLITTDGTTLLGADNKAGIAEIMTAMDYLIKHPEIKHGTIRVAFTPDEEIGRGPHKFDVKRFNASFAYTVDGGPLGELEYESFNAAAAKITIKGNNVHPGTAKGKMINSAKIAMKLNSLLPADEAPEYTEGYEGFYHLLSIQGDVEETKLHYIIRDFDKENFQNRKETMKRAVEELQNEYGQDRILLDMNDQYYNMREKIEPVIEIVNIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYISVDNMVKAVNVIVEIAKQFEAQA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45509
Sequence Length: 410
Subcellular Location: Cytoplasm
EC: 3.4.11.4
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Q89YZ7 | MTLVDRFLKYVSFDTQSDESTGLTPSTPKQMVFAEYLKTELESLGLEDITLDEHGYLFATLPANIDKKVPTIGFIAHMDTSPDMTGKDVTPRIVKGYDGTDIVLCAEENIILSPAQFPELLDHKGEDLIVTNGKTLLGADDKAGIAEIVSAIVYLKEHPEIKHGKIRIGFNPDEEIGEGAHKFDVGKFGCEWAYTMDGGEVGELEFENFNAAAAKITFKGRNVHPGYAKNKMINSIRVANQFIAMLPSTETPEQTEGYEGFYHLISIQGDVEQSTVSYIIRDHDRAKFEKRKEEIKRLVAQVNTEYGEGTATLELRDQYYNMREKIEPVMHIIDTAFAAMEAVGVKPNVKPIRGGTDGAQLSFKGLPCPNIFAGGLNFHGRYEFVPIQNMEKAMNVIVKIAELVASK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45178
Sequence Length: 407
Subcellular Location: Cytoplasm
EC: 3.4.11.4
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Q038E8 | MKLNQFARLTPDFKVQVAELKQIGLQADPDDTFSQSTTDLFNAFFPEAYTLAAKKDKLAQVAVNMDQTLAAWLAKKPSKMTRRDFYNVALQLLGFEAFTDFDLNDPFKMMTATKLPSLDHDLTSTADLLKAVYLLLNTRTKHLVSYLDDLANRGFLKDFQKKQKKPTHLLFNGKVQQVFDARQAVREVVWIESDMDTDHDGQRDLLEATIYRPKATDQGLKVPVLFTANPYFHGTNDVTAVTHVPETTLAVKTHGASKAEVTANPEEPANLPHHPVNGEATQAEAYAEENGMYAFNDYFLARGFAVVYSAGVGTRYSDGFRTTGGPEETDGAVAVIEWLTGKRRAFTNRTDGITIKAWWSTGLVAMTGKSYLATLAMAAATTGVDGLKTIVADAGISSWYDYYRENGLVVAPGGFQGEDADVLAVDTFSRQKSGGDLINIKQAWEKHLATITHDQDRTTGAYNTWWDARNYRKNANKVKADVVLIHGLNDWNVKPTNAIKFWEAIADLPIQKKLVLHQGQHVYVHNVRSLDFLDMMNLWLTHELLGEANGAEDVLPNVVVQDNVAVQTWSAYQNFASPAAEHVTNTRNLKTDFEAATDQFTDHATATFDAQHDTSASFETAIITPNSAYANSRLWLTQPPLERDQTLEGIPHLELTLAIDAPTGILSVRLIDLGMAKRFGETAATVALNGLQLGFDYKTTDILEFKPTAKPTPSKLISLGHINLQNPKNAYEVQRITPGQPFHISLDLQPTHYHLPAGRQLALVIHGADMAQTIRPIKTTHYQIDLANSSITLPYRI | Function: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Catalytic Activity: Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
Sequence Mass (Da): 88464
Sequence Length: 797
Subcellular Location: Cytoplasm
EC: 3.4.14.11
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Q88YC0 | MKNNQFAIVPTDSETAIAELTKIHFITPDMDALTTVPAVYQALLAKSLPEVHTASGLTHKFNNIMATSQHTLSEWLADATIVNNQVFYNVGLQLLGFLPGQDFELADPLLAMRDIHLPMVGDSAFDREALYYAWYLLLNTRGNNGQTLIESLTTRGYFVPFYQLPNDQKPLFFNGKAQAVFDTNALIRDVVYVEAPLDTDHDGQRDLLKVEILRPAETETGLKVPVLYTASPYNQGINDQAGDAQMHNVDVPLTAKEPDENTYADVEFQPTTAQLPAARTATTTTDTAEETFSREKSYTLNDYFLARGFAVVYAAGIGSIDSDGLAPTGDVDETTSTVAIIEWLTGKRQAFTNRDGNIAIKAWWCNGAVAMTGRSYLGTLATAAATTGVAGLKTIISEAAISSWYDYYRDNGLVVAPDTFQGEDTDVLAAEVFSRSLKAGDAHQIQPAFDQKLAELTADQDRASGNYNRFWDERNYLKNVDKIKADIIMVHGLNDWNVKPRNVANLWDKLQAVPVTKKLILHQGQHIYINNLQSLDFTDMMNLWLSHKLYGLDNHAETLLPNVLVQDNTQAQTWHGYDNWWQDTTDALDFKVQYKELVPADHTVDQRAAHFTDKLPDKLFDHYKHHLDSWQRDLLQEDKLNPLYDHRLLFKSWQAPEDQLLVGIPHVAGSVAVNKNFGMLSFMLIDFGAARRLTVSPQILAAKALDLGYHWREDDLKDFKLAGETPFKMITKGHLNLQNRHHPWHAEAIQPNVFYDFSVDLQPLFHHLLKGHQLGLVIYATDMKMTIRGNQDLQYSLNLNDIRLHVPMKKITD | Function: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Catalytic Activity: Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
Sequence Mass (Da): 91548
Sequence Length: 813
Subcellular Location: Cytoplasm
EC: 3.4.14.11
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Q03PM5 | MRNQQFAIRPTTLDQARVELQQIHFLDDTNLSFTTPSDLLRDFYDRSWPEYTTSSVVAQQLSNLMATPETDGLTYLTTHEQVPVDVFYNLALQRLGFAVDLDFQLTDPLAAMTKIQLPVADHEGTTFTLNELMNAWYVLLTTHNKTGQTFLDQLTTHGYFAPLIHDNSVPKPLIFNGKAQAVFDTTQLIHEVVYVESPQDTDHDGHRDLLKAEIIRPAETANGLKVPVLYTASPYNQGTNDEAGEALTHNVNVPLTAKQPAATTLADVTAESVTTPLPDARPVTATTHTAAETFAREQSYTLNDYFLARGFAVVYAAGIGTKDSDGLRTTGDPEETTSTIAIIEWLAGNRTAFTTRNATQAIPAWWSNHQVAMTGRSYLGTLATAAATTGVAGLKTVISEAAISNWYDYYRDGGLVVAPGGFPGEDADVLAEETFSRQLLAGDYHRIQEKWQHQLAAITQNQDRVTGNYNRFWDARNYLKNAKNIKADLLLVHGLNDWNVKPRNVNNLWRAVRDLPVTKKLILHQGQHIYINAFRSIDYTDIVNLWLTHELLGVDNHAETLLPNVIIQDNVTPETWQAYPDWDAPSNPVQHFNLQADELVAPSDHIPAAATSFNDQLPVDQFNHYTHHIDEWQADLLGDKHNAMFKHRLLFKSAVLTDDLVLDGRPTIDLQVAVNQPLGLLSFQLVDYGDAKRLGVSPTPLRIRLDEGYRWREDNLREFTVAATTPWKMITKGHRNLQNRTNAYQVDELKPNTFYDLSVTLQPTHYRLLAGHQLGLVIYATDFGMTVRGNQDLQYSIQLGQSALHVPFITD | Function: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Catalytic Activity: Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
Sequence Mass (Da): 90917
Sequence Length: 811
Subcellular Location: Cytoplasm
EC: 3.4.14.11
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Q03H46 | MKNNQFGRIRLDRTTELEELKNIHFIDADLLADPKAQLKDFLKRSCLVSNSEATFQQKLSNLLATPDQTMAAFFESDQPLTLEIFILLELQLLQFEADTDYQIEDPLSAISKIQLPELDLKNFETSADVAHAWYNLLTTHTKNGEVYLDRLTQQGYFVSFYPTTTKPLFFNGKAQAVFDPHQLIREVVYVEAPLDTDHDGQRDLLKAEILRPAQTAHGYQAPVLYTASPYNQGTNDSYGEAITHNVDVPLTEKAVQKISKSDVTAEPFSQTLPAERKVAGMATKASETFAREQPYTLNNYFLSRGFAVVYAAGIGTRDSDGLRDTGSVEETISTTAIIEWLAGNRRAFTNKTDNLEIKASWSNHKIAMTGRSYLGTLATAAATTGVEGLETIISEAAISSWYDYYRDGGLVAAPDTFQGEDMDVLAAEVLSRKHDAGDYLGIKAHFDQILKRIEKDQDRDSGNYSKYWDSKNYLNNVKNIKADIIMVHGLNDWNVKPRNVGKLWNAVRDLPINKKIILHQGQHIYINAFRSIDFTDMMNLWLSYKLFDVQNGANEVLPNVIIQDNVEPETWNTYQDWQAADDEIREFTLQAKTLVDRASETKNEAASFRDSLDPEFFEMYKNDLKHWHTDLLNTEHATNGKNQMRNNRLIFKTAQTKEDWLIDGTPEVSVNVAVNQPFGMLSFQLVDFGDAKRLNPSPSILQPRSLSGSFDWRTDDLREFTLQNAVTPWKMISKGHINLQNRTNNYCVDEVKPHQFYDVKLELQPTFYRLLAGHQLGLVIYATDFETTIRGNQELLYSLQLNQSHLKIKLAH | Function: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Catalytic Activity: Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
Sequence Mass (Da): 92354
Sequence Length: 812
Subcellular Location: Cytoplasm
EC: 3.4.14.11
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Q93M42 | MRYNQYSYTKASEEVMLDELARLGFTIQTTNSPKENLHHFLQKILFRYQDVNYVLSSWVADQKTDLLTFFQSDKQLTEEVFYTVALQVLGFAPFVDFDDVTAFCKEIHFPITYGNILENLYQLLNTRTKLGNTLIDQLVSEGFIPESNDYHFFNGKSLATFSSHEAIREVVYVESRVDTDGDGKPDLVKVSIIRPSYEGQVPAVMTASPYHQGTNDKASDKALHNMNVDLSCKNPRTITVQESSIQTIEPQGQASLVEKAEEKLGHIGSYTLNDYLLPRGFANLYVSGVGTKDSEGMMTSGDYQQIEAYKNVIDWLNGRCRAFTDHTRQREIKATWSNGKVATTGISYLGTMSNGLATTGVDGLEVIIAEAGISSWYNYYRENGLVTSPGGYPGEDFESLTELTYSRNLLAGEYLRHNQAYQAYLDQQRKDLERETGDYNQFWHDRNYLIHADKVKAEVVFTHGSQDWNVKPLHVYNMFHALPAHIKKHLFFHNGAHVYINNWQSIDFRESMNALLSKKLLGHSSDFDLPPVIWQDNSQAQNWMSLDDFGNQEDYSHFHLGKGSQEIRNRYSDEDYNRFAKSYQVFKNELFEGKTQQITLDWTLEQDLFINGPAKLKLRLKSSTNKGLISAQLLDYGPAKRLTPIPSLLEPRVMDNGRYYMLDNLMELPFADTPHRVITKGFLNLQNRTDLLTVEEVVPNQWMELSFELQPTIYKLKKGDQLRLVLYTTDFEHTVRDKTDYHLSVDMEHSSLSLPHKKS | Function: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Catalytic Activity: Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
Sequence Mass (Da): 87115
Sequence Length: 759
Subcellular Location: Secreted
EC: 3.4.14.11
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P82600 | MAKKVLLLSLYSAVLSTWFGFGYVQCKLPTSRSEIPNFDYTVAQQPDQSDACEQNEVCMVSVECILDAKKKAILKPCSTVPSVDGVCCPSSEYNGTSSRVQQNSEEHAADHLVLQAIHEGRREYDEKLRFEDEHRAVMTAKEKPEAMFHRMFLPGGLKTHGKEVVDAEEQANVYGHVFASRKYAELTNMTLKQRQGDRFARIPRAIRKRCLPPVPCNPHSRYRTIDGSCNNPLPDRTSWGMEGYPFDRVLEPAYEDGVWAPRIHSVTGNLLPSARVISVALFPDEYRPDPRLNILFMQMGQFISHDFTLSRGFTTKHGQAIECCTPNCTAPLFGPHRHFACFPIEVPPNDPFYSRFGVRCLNLVRIRLAQGPECQLGYAKQADLVTHFLDASTVYGSTNDVAAELRAFQQGRLKDSFPNGIELLPFARNRTACVPWARVCYEGGDIRTNQLLGLTMVHTLFMREHNRLAVGLSKINPHWDDERLYQEARRILIAEYQNVVYNEFLPILLGHERVQQLGLADPFDTYTNYYDPNLRPMTLAEVGAAAHRYGHSLVEGFFRFLTRESPPEDVFIKDIFNDPSKTLEPNSFDVMMFSFNQQPMEQMDRFLTYGLTRFLFKERKPFGSDLASLNIQRGRDFAVRPYNDYREWAGLGRITDFNQLGEVGALLAQVYESPDDVDLWPGGVLEPPAEGAVVGSTFVALLSAGYTRYKRADRYYFTNGPEVNPGAFTLQQLGEIRRTTLAGIICANADHKEDFYQAQEALRQSSADNVPVPCTRYDTVNLGLWREEGF | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per heterodimer.
Function: Involved in the formation of a rigid and insoluble egg chorion by catalyzing chorion protein cross-linking through dityrosine formation and phenol oxidase-catalyzed chorion melanization.
PTM: N-glycosylated on Trp by mannose and on Asn by N-acetylglucosamine.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 89605
Sequence Length: 790
Subcellular Location: Secreted
EC: 1.11.1.7
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Q7QH73 | MLPKGVLLFLVLIVLVQHFATVQTTNAIERPSAPSSQCTSSHESCVLRVMCEVEPRARTTLVPCLTADGLEGVCCSVAKEGKQRKKRSLPFELSQELFQNAVGEGHRVYTRKLANIDHHREVMRGGSVDTLVRQFHAPPGEPLGAEDPTAYEDMFVARSFANALNLSVAERLDLPELTLDPALRRKRCLPPRSCDPHARYRSLDGSCNNPVPARSSWGAAGYPFERLLPPAYEDGVWAPRVHSSVSGRLLASARDISVAVFPDVDRRDRKFNLLLMQFGQFMSHDFTRSASVRIGQEEVQCCNAEHSGALRGEQAHFACMPIAVSPADPFYSRFGIRCLNFVRLALARDGKCRLGYGKQLNRVTHFIDGSAVYGSNEALAASLRTFEGGRLRSSFPTGEELLPFARTRAACEPWAKACFRAGDDRVNQIVSLTEMHTLFLREHNRVATALAALNRHWDDERLYQETRRIVGAVMQKIFYNEYLPSIVGHSKARQYGLLDSHGEQTDFYSPDVKPAVFNELSGAAFRFGHSTVDGAFLIQHRHRRTELVPIQEVFLNPSRLLQRSFFDDFLFSLMDQPQQQLDDSITFGLTRLLFAGRNPFGSDLASLNIQRGRDHALRPYNDYRSWAGLERLTSFEQFGPVGARLASVYEFPDDVDLWVGGLLEPPTQDGALFGETFAAIISEQFARLKFGDRYYYTNGPRTNPGFFTGEQLRELSKVSLASVICANLDQADGFSAPRDAFRQPSEHNPPVPCQTLVGMDLSAWRGH | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per heterodimer.
Function: Involved in the formation of a rigid and insoluble egg chorion by catalyzing chorion protein cross-linking through dityrosine formation and phenol oxidase-catalyzed chorion melanization.
PTM: N-glycosylated on Trp by mannose.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 85796
Sequence Length: 767
Subcellular Location: Secreted
EC: 1.11.1.7
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Q9VEG6 | MSRILFILLLLIVTQLSELQAAAFSVRQNRFDEVPDLQTPAPLATSTESSKKPEKATSGLLKKCLPCSDGIRCVPQIQCPAHVRMESHEKPQICDLPAGKFGYCCETGQNHTAPKPETSPKERRSGFPTILSPAVLDEARRNFEHLMHGVAQIPVRRGFPDFAHGLVFHSTAKDDLHNFAISNSAIEQVMTTQLFGKKEQVPVEDFITNNVPIKFTETPLAHHCQPPPVCGNIRSVYRSMDGTCNNPEPQRSLWGAAGQPMERMLPPAYEDGIWTPRAHSSDGTPLLGARKISRTLLSDVDRPHPKYNLMVMQFGQVLAHDISQTSSIRLEDGSLVQCCSPEGKVALSPQQSHFACMPIHVEPDDEFFSAFGVRCLNFVRLSLVPSPDCQLSYGKQLTKVTHFVDASPVYGSSDEASRSLRAFRGGRLRMMNDFGRDLLPLTNDKKACPSEEAGKSCFHSGDGRTNQIISLITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGPQQMKRFRLVPLHQGYSHDYNVNVNPAITNEFSGAAYRMGHSSVDGKFQIRQEHGRIDEVVNIPDVMFNPSRMRKREFYDDMLRTLYSQPMQQVDSSISQGLSRFLFRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQFPIEIAQKLSRVYRTPDDIDLWVGGLLEKAVEGGVVGVTFAEIIADQFARFKQGDRYYYEYDNGINPGAFNPLQLQEIRKVTLARLLCDNSDRLTLQAVPLAAFVRADHPGNQMIGCDDPNLPSVNLEAWRA | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per heterodimer.
Function: Required for ovarian follicle maturation. Involved in the formation of a rigid and insoluble egg chorion by catalyzing chorion protein cross-linking through dityrosine formation and phenol oxidase-catalyzed chorion melanization.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 90539
Sequence Length: 809
Subcellular Location: Secreted
EC: 1.11.1.7
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P11678 | MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARKIMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPFMFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDELRDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLARKFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTKRQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT | Cofactor: Binds 1 Ca(2+) ion per heterodimer.
Function: Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 81040
Sequence Length: 715
Subcellular Location: Cytoplasmic granule
EC: 1.11.1.7
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P80550 | GDKYRXIXGRXNNVDXEKTXAQLPPXFPIKIPPNDXRI | Cofactor: Binds 1 Ca(2+) ion per heterodimer.
Function: Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 4342
Sequence Length: 38
Subcellular Location: Cytoplasmic granule
EC: 1.11.1.7
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P10820 | MATCLFLLGLFLLLPRPVPAPCYTATRSECKQKHKFVPGVWMAGEGMDVTTLRRSGSFPVNTQRFLRPDRTCTLCKNSLMRDATQRLPVAITHWRPHSSHCQRNVAAAKVHSTEGVAREAAANINNDWRVGLDVNPRPEANMRASVAGSHSKVANFAAEKTYQDQYNFNSDTVECRMYSFRLVQKPPLHLDFKKALRALPRNFNSSTEHAYHRLISSYGTHFITAVDLGGRISVLTALRTCQLTLNGLTADEVGDCLNVEAQVSIGAQASVSSEYKACEEKKKQHKMATSFHQTYRERHVEVLGGPLDSTHDLLFGNQATPEQFSTWTASLPSNPGLVDYSLEPLHTLLEEQNPKREALRQAISHYIMSRARWQNCSRPCRSGQHKSSHDSCQCECQDSKVTNQDCCPRQRGLAHLVVSNFRAEHLWGDYTTATDAYLKVFFGGQEFRTGVVWNNNNPRWTDKMDFENVLLSTGGPLRVQVWDADYGWDDDLLGSCDRSPHSGFHEVTCELNHGRVKFSYHAKCLPHLTGGTCLEYAPQGLLGDPPGNRSGAVW | Function: Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells . Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores . Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes . Perforin pores allow the release of mature caspase-7 (CASP7) into the extracellular milieu .
PTM: N-glycosylated. The glycosylation sites are facing the interior of the pore.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62081
Sequence Length: 554
Domain: Perforin consists of three domains: (1) the MACPF domain, which includes the central machinery of pore formation, (2) the EGF-like domain, which forms a 'shelf-like' assembly connecting the MACPF and C2 domains, and (3) the C2 domain, which mediates calcium-dependent binding to lipid membranes . The C2 domain is critical for initial calcium-dependent interaction with lipid membranes of the target cell: calcium-binding causes a significant structural rearrangement, leading to oligomerization and deployment of the two transmembrane beta-strands (named CH1/TMH1 and CH2/TMH2) that enter the membrane as amphipathic beta-hairpins . The third calcium-binding site (Ca(2+) 3), which constitutes the weakest affinity site, triggers structural rearrangements in the C2 domain that facilitate its interaction with lipid membranes .
Subcellular Location: Cytolytic granule
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P41219 | MSHHPSGLRAGFSSTSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSASPSSSVRLGSFRSPRAGAGALLRLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYESIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRISVPVHSFASLNIKTTVPEVEPPQDSHSRKTVLIKTIETRNGEVVTESQKEQRSELDKSSAHSY | Function: Class-III neuronal intermediate filament protein (By similarity). May form an independent structural network without the involvement of other neurofilaments or may cooperate with the neuronal intermediate filament proteins NEFL, NEFH, NEFM and INA to form a filamentous network . Assembly of the neuronal intermediate filaments may be regulated by RAB7A (By similarity). Plays a role in the development of unmyelinated sensory neurons (By similarity). May be involved in axon elongation and axon regeneration after injury (By similarity). Inhibits neurite extension in type II spiral ganglion neurons in the cochlea (By similarity).
PTM: Phosphorylated; phosphorylation increases after nerve injury in regenerating neurons.
Sequence Mass (Da): 53651
Sequence Length: 470
Subcellular Location: Cytoplasm
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P85317 | LSPTFYATSXPNVXXTRDSVVEIGQLADTVAPVRGFDVIDNIKDMVALSGSHTIGQARQATRSPAQVDLSNTRGLLGQAGNDFALVDDK | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. Active against p-coumaryl alcohol, coniferyl alcohol and coniferyl aldehyde.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 9406
Sequence Length: 89
Subcellular Location: Secreted
EC: 1.11.1.7
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Q25020 | GVVMYTTSSITATLGFPKDMWIGRSFIDFLHPKDANTFASQITNGLAIPKIVNDTQEKAQIFGTQGSTMVCRIRRYRGLSSGFGVKDTSVSYMPFLLKFRFRNISDDKGLVVYLVIQTVPFFSAYKTPNEILTQEVSFIMRHSANGNLEYIDPDCVPYLGYIPQDITNRNALVLYHPGDLPFLQEVYQAIVKEGSVTRSKSYRMVTQNGHFIKVETEWSAFINPWSRKLEFVNGKYYIIEGPANPDVFESPDPEKTPKLTEERKNQAQICRDDIIRIMNEVLTNPAEIAKQQMSKRCQELALFMEILQEEQPKAEEEFHLQTQDVDHTYYERDSVMLGGISPHHEYNDIKSSAETSLS | Function: Involved in the generation of biological rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the tim-per complex. Light induces the degradation of tim, which promotes elimination of per. Nuclear activity of the heterodimer coordinatively regulates per and tim transcription negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity).
PTM: Phosphorylated with a circadian rhythmicity.
Sequence Mass (Da): 40930
Sequence Length: 358
Subcellular Location: Nucleus
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Q25478 | GIVMYTTSSLTTTLGFPKDMWIGRSFIDFVHPRDRNTFASQITSGLAVPKIVNGQSPGNPASTMVCRIRRYRGLTTGFGVKDRVVTFMPFLLKFTFKNVSDEEGKVIYLVIQATQFFSAFRIPSEVVSKAVPFVMRHAANGNLEYIDPESVPYLGYLPQDVTDKDALQLYHPEDLDYLQQVYETIVKEGGVPRTKAYRMMAQNGDYLKLETEWSSFINPWSKRLDFVIGKHHIIEGPSNPDVFQSPDPEKAVAMSEEEKAKEQKYRRDIIRTMNEVLTKPAEVAKQQMTKRCQDLASFMESLMEEQQPKVDEDLRLDIQDPDHSYYQRDSVMLGGISPHHDYNDSKSSTGTPLS | Function: Involved in the generation of biological rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the tim-per complex. Light induces the degradation of tim, which promotes elimination of per. Nuclear activity of the heterodimer coordinatively regulates per and tim transcription negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity).
PTM: Phosphorylated with a circadian rhythmicity.
Sequence Mass (Da): 40303
Sequence Length: 354
Subcellular Location: Nucleus
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Q25637 | MEETATHNTKISDSAYSNSSNSQSQRSSGSSKSRHSNSSGSSGYCGHGSSIQGSSNEPFPQPSVTKRNKDKEHKKKKLKSSVTTAATATVTSVVTTVSEYTEHENGTSHMSLGVSGTVVPLSGTVAEETEITEAGSEGSVISSHAGVALGAAGVVPATTPGPENEAHQMASLTQTLNSIKKMKKMKDLSTDIPEETEGHSFSLPMVAEEKEEHIRNSFDAEPPAHNEGEFCVVVSMQDGVVVFTTPSITDVVGFPKDMWLGRSFIDFVHPRDRTAFANHITSGVITPLSNSNPKGGSHPGKNSFYCCLRRYRGLKSTGYGVTEKEVSYLPFQLNMTFRELLPHSNPLEVEGNTSPESVPGGCNSMFLVITAKLICSAYKHAGETCASPKFVTRHLATCKLNYVDPECMPYLGYLPHEMLGNSVLDFYHPEDLPFLKEVYQIVMQENGAPFRSKPYRFRSHNGGYILLETEWSSFVNPWSKKLEFVVGQHRVLKGPENADVFMAPVEDDTLQISEEVLKESKIIQEEIRSLLSEMVKNNGHLEKQQMSKRCRDLATFMESLMDDITKPDLKLELPQEEHSFSEHDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNDNIQRFFESKPKTTLSDESGESKIEANRSLMSTDEEGKSGPAADSSLGSSNRKCCSPVNGSGSGSGSGHSSGSAGIGGSAESRRDTSATNTSHGSYKPPLLTEALLCRHNEDMEKKMVQKHREQRNKGSERESKLKKCVHDKLLQEQCHGVKRSGSHSWEGEVYKASKHPHVEGGKELNPGSGGSGGGGVTSGLSQCLGVAATGKQYSGVGSVPPIFQGGTNVNLWPPFSVTVTPLQPTPPCSTHGFATNNIPTPPHMASMIPVYYIEKRAPNFKNN | Function: Involved in the generation of biological rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the tim-per complex. Light induces the degradation of tim, which promotes elimination of per. Nuclear activity of the heterodimer coordinatively regulates per and tim transcription negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity).
PTM: Phosphorylated with a circadian rhythmicity.
Sequence Mass (Da): 97174
Sequence Length: 893
Subcellular Location: Nucleus
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Q26612 | SKSSTETPPSYNQLNYNENLQRFFNSKPATAPVEFDPIKMDQSYNEPAEAECTVSPVQCFEGSGGSGSSGNFTSGSNLNMRSVTNTSNTGTGTSSESVPLVTLTEALIS | Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity).
PTM: Phosphorylated with a circadian rhythmicity, probably by the double-time protein (dbt). Phosphorylation could be implicated in the stability of per monomer and in the formation of heterodimer per-tim (By similarity).
Sequence Mass (Da): 11525
Sequence Length: 109
Subcellular Location: Nucleus
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Q9ZVN2 | MATCSSSLLVLPNLRLSSNQRRNFKVRAQISGENKKATSLEPVNNNGSVSLSTTVQNQKGANEVNGKGKSKRKIVSDEIELLWDDGYGSKSVKDYFAAAKEILKADGGPPRWFSPVDCGRPVEDAPTLLFLPGMDGTGMGLVPHHKALGKAFHVSCLHIPVLDRTPFEGLLKVVEDVLRQEQATRPNKPIYLVGDSFGGCLALAVAARNRSLDLVLILVNPATSFDRSPLQPLLPILEMVPEELHFTVPYALSFIMGDPIKMATLGIDNQLPTGVKIEKLRQRLTKTMLPLLSELGGIIPRETLLWKLKLLRSGCAYANSRIHAVQAEVLVLASGKDMMLPSQEEAKRLHGLLKNCSVRCFKDNGHTLLLEDSISLLTVIKGTGKYRRSWRYDLVSDFLPPSKGELAYALDEVLGFLRNAVGSVFFSTMEDGKIVKGLAGVPDKGPVLLVGYHMLMGLELGPMSEAFIKEKNILFRGMAHPVLYSDNDPAKAFDYGDWIKVFGAYPVTATNLFKLLDSKSHVLLFPGGAREALHNRGEQYKLIWPEQQEFVRMAARFGATIVPFGTVGEDDIAELVLDYNDLMKIPILNDYITEVTRDTKQFKLREESEGEVANQPLYLPGLIPKVPGRFYYLFGKPIETKGRPELVKDKEEANQVYLEVKAEVENSIAYLLKKREEDPYRSVLDRLNYSLTHTTATHVPSFEP | Function: Acyltransferase involved in fatty acid phytyl ester synthesis in chloroplasts, a process required for the maintenance of the photosynthetic membrane integrity during abiotic stress and senescence . Exhibits phytyl ester synthesis and diacylglycerol acyltransferase activities with broad substrate specificities, and can employ acyl-CoAs, acyl carrier proteins, and galactolipids as acyl donors .
Catalytic Activity: a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + a 1,2-diacylglycerol = a triacylglycerol + an acyl-3-O-(beta-D-galactosyl)-sn-glycerol
Sequence Mass (Da): 78204
Sequence Length: 704
Subcellular Location: Plastid
EC: 2.3.1.-
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Q9LW26 | MAVTVLPSVSGLSAVASSSNLRRLTSASNHRLTAIKSVTSTSSPPTPSSGVQRRRKNNDENRATVAKVVENPYSKVEAARPDLQKRLSDFLEEAREFVGDGGGPPRWFSPLECGAQATNSPLLLYLPGIDGTGLGLIRHHKKLGEIFDIWCLHIPVSDRTPVKDLVKLIEETVKSENFRLPNRPIYLVGESIGACLALDVAARNPNIDLSLILVNPATHVNNFMVQPLSGMLNVLPDGLPTLLEDIFDFGFKQGDPLTGMLDALSNEFSVQRMGGVGGGMLRDVLAVSANLPTLSRMFPKDTLLWKLEMLKYAIASVNSHIYSVRAETLILLSGRDHWLLKEEDIDRYSRTLPKCIVRKLDDNGQFPLLEDGVDLATIIKCTCFYRRGKSHDHITDYIMPTTFELKQQVDDHRLLMDGTSPVMLSTLEDGTVVRSLEGLPSEGPVLYVGYHMILGFELAPMVIQLMTERNIHLRGLAHPMLFKNLQDSLVDTKMFDKYKIMGGVPVSHFNIYKLLREKAHVLLYPGGVREALHRKGEEYKLFWPERSEFVRVASKFGAKIVPFGVVGEDDICEIVLDSNDQRNIPILKDLMEKATKDAGNIREGDESELGNQECYFPGLVPKIPGRFYYYFGKPIETAGKEKELKDKEKAQELYLQVKSEVEQCIDYLKVKRESDPYRHLLPRMLYQASHGWSSEIPTFDL | Function: Acyltransferase involved in fatty acid phytyl ester synthesis in chloroplasts, a process required for the maintenance of the photosynthetic membrane integrity during abiotic stress and senescence . Exhibits phytyl ester synthesis and diacylglycerol acyltransferase activities with broad substrate specificities, and can employ acyl-CoAs, acyl carrier proteins, and galactolipids as acyl donors .
Catalytic Activity: a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + a 1,2-diacylglycerol = a triacylglycerol + an acyl-3-O-(beta-D-galactosyl)-sn-glycerol
Sequence Mass (Da): 78609
Sequence Length: 701
Subcellular Location: Plastid
EC: 2.3.1.-
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Q2MI70 | MGITKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPAGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVALWLGIGATLPIDKSLTLGLF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17473
Sequence Length: 160
Subcellular Location: Plastid
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Q47RJ6 | MAVMTPRRERSSLLSRALQVTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF | Function: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle . Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) . Also hydrolyzes the triglyceride triolein (Probable). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world .
Catalytic Activity: a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+)
Sequence Mass (Da): 32218
Sequence Length: 301
Subcellular Location: Secreted
EC: 3.1.1.74
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A0A0K8P6T7 | MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS | Function: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET . Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl) terephthalate (MHET) as the major product . Also depolymerizes another semiaromatic polyester, poly(ethylene-2,5-furandicarboxylate) (PEF), which is an emerging, bioderived PET replacement with improved gas barrier properties . In contrast, PETase does not degrade aliphatic polyesters such as polylactic acid (PLA) and polybutylene succinate (PBS) . Is also able to hydrolyze bis(hydroxyethyl) terephthalate (BHET) to yield MHET with no further decomposition, but terephthalate (TPA) can also be observed . Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) in vitro .
Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
Sequence Mass (Da): 30247
Sequence Length: 290
Domain: PETase retains the ancestral alpha/beta-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases.
Pathway: Xenobiotic degradation.
Subcellular Location: Secreted
EC: 3.1.1.101
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Q85FK4 | MFTLLSYFAFLMLALTFTLALFVGLNKIQIL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3554
Sequence Length: 31
Subcellular Location: Plastid
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Q85AP7 | MLTLFSYFGFLFAALTLALVLFIGLNKIQLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3492
Sequence Length: 31
Subcellular Location: Plastid
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A4QK36 | MPTITSYFGFLLAALTITSVLFIGLSKIRLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3401
Sequence Length: 31
Subcellular Location: Plastid
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P56776 | MLTITSYFGFLLAALTITSVLFIGLSKIRLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3417
Sequence Length: 31
Subcellular Location: Plastid
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