ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q54PK9 | MINGRYQKEDVVNNNNNLNLNLIEKTLNDLTIKNNTNINNNNTNNKNTNYYNNNNFNNNNNNNNNNNNNNNNINNNNNNNKYLNNSHNNNNNNNNNNNNNNNNNNNNNNNEINNNNNNVLSHSSLSGKGGSTTYETTSYTTSITSSRDTGTISTSYESSSSSSSSSSSSLYDDDEYSDYSDSSDSIDSYVNHRQALSKSQQQQHLQQQQDQPQPLHSSMGAISNEKPPSPTNQQQQQQHHHPKHNIELPKTSSFGLQPNSSIPHKKSRSDFDFIRTIGKGAYGKVKLVIEKETQLIFASKILNKKLIIKEKKAKYVNTEK... | 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 tha... |
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, ... |
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, ... |
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-hist... |
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-hist... |
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-hist... |
Q8UGD4 | MTHASLPLALTQGDPAGIGPDIAINAWAKRRENGVPPFIFIGDPDVVASRAALIGVPVNIETCDPESAVSLFERAFPILPLPVGFDVQAGQPHVGAAHATIKAIEMAVSLTVEGRAAAVVTNPIAKSVLYEAGFGFPGHTEFLADLALRQTGKPVTPVMMIAGPKVRVVPVTIHIPIKDVPTALTEELIVTTCRIIDTDLREKFGIAAPRLAVAGLNPHAGEDGALGTEDRDVVHPATIRLRKDGIDAFGPLPADTMFHDAARKRYDVAVCMYHDQALIPAKALGFDDSVNVTLGLPFIRTSPDHGTAFGIAGQGIASET... | 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).
Cataly... |
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(... |
Q89ZK3 | MEENKIRIGITQGDINGVGYEVILKTFSDPTMLELCTPIIYGSPKVAAYHRKALDVQANFSIVNTASEAGYNRLSVVNCTDDEVKVEFSKPDPEAGKAALGALERAIEEYREGLIDVIVTAPINKHTIQSEEFSFPGHTEYIEERLGNGNKSLMILMKNDFRVALVTTHIPVREIATTITKELIQEKLMIFHRCLKQDFGIGAPRIAVLSLNPHAGDGGLLGMEEQEIIIPAMKEMEEKGIICYGPYAADGFMGSGNYTHFDGILAMYHDQGLAPFKALAMEDGVNYTAGLPVVRTSPAHGTAYDIAGKGLASEDSFRQA... | 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(... |
B2IDU5 | MVMLDHPLAVTMGDPSGIGPEIIAKMYLRRPDKRNWIVVGDPLVMEHAIANLGVAVQIRRIATVEEAGCEDGVLNVLASSSLATLPAVGRVSAVSGQAAYDAIVTAIGLARQGTIRGIVTAPIHKEALAAAGIHYPGHTEILAEQGGAQHVAMMLANDEIRTVLVTIHCSLADAIRKADFPAQMQAIRLAHEGARALGIVQPRIAVAGLNPHAGEGGLFGDEEIRIITPAIAAARAEGIDATGPWPGDTVFMQARLGKFDVVVAQYHDQGLIPVKFMGLEKGVNITLGLPFVRTSPDHGTAFDIAGRGIADSSSLETAFD... | 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).
Cataly... |
Q89MT9 | MANHAAKPLALTLGEPAGIGPDITIAGWLRRRELNLPAFYLLGDEALIARRAKTLDKTLGKALGAEIRIASVSAHEAAAAFTEALPVVATGERATAEPGQPDASSAPAALASIRQAVADVRAGRAGAVVTNPIAKSVLYRAGFRHPGHTEFLAELAAKDGRVPQPVMMLWSPRLAVVPVTIHVSLRDALSQLTSELIVSTVRIVATELKSRFGIARPRIAVSGLNPHAGEDGSLGHEEQTIIAPALKTLRNDGIDARGPLPADTMFHEAARSSYDCAVCMYHDQALIPIKTVAFDDAVNVTLGLPFIRTSPDHGTAFDIA... | 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).
Cataly... |
P65680 | MRAKPLPPLAVSIGDPSGIGADVALAAWLKRCELSLPPFFLIADPKQLAARARHLGLAVDFAILSDPREAEAAFGERLPLLALKHSHTESPGKPLTENAAGVIEAIERAVELTLKGEAAAVVTCPIAKKPLYEAGFQHPGHTEFLAELAGHHLGKPVTPVMMLAGPQLRAVPVTIHIPLSEVPARLTTTEIVAVSRITANELRERFGIASPRLAISGLNPHAGEGGALGKEDDAIILPAIEQLIREGIDARGPLPADTMFHAPARATYDAAICMYHDQALIPAKALAFDETVNVTLGLPFIRTSPDHGTAFDIAGKGIAR... | 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).
Cataly... |
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
Seque... |
Q9PN58 | MKKLAISIGDINSIGLEILVRSHEELSKICTPFYFIHESLLNKALKLLNLKLFNAKIVAFKDDKDYEFNFIKKENSLEIYSFCLPLGFKVDENFEIQAGEIDAKSGLYGFLSFKAASYFVYEKHAHALLTLPIHKKAWEDAGLKYKGHTDALRDFFKKNAIMMLGCKELFVGLFSEHIPLAKVSKKITFKNLSIFLKDFYKETHFKKMGLLGFNPHAGDYGVIGGEEEKIMEKAIAFVNAFLHSKKDEKFFKKALKDENLQKELLLNFKGKGVYLPYPLVADTAFTKTGLKNCNRLVAMYHDLALAPLKALYFDKSINVS... | 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
Seque... |
Q9A7N4 | MTSRPLAISAGDPAGVGAEIIAKAWRALRQDGPTFVVIGDAQLLASAGGGVKVRAVTRPQEAAQVFPDALPVLDIPVLSPVVYGRPSPSHAPQIIRWIETGVGLALSGAVSGLVTAPIAKAPLYEAGFQFPGHTEFLAELTAAASMVGARGPVMMLAAGDLRATLVTIHTALAKAPSALTTEAIINSGLVTAQALRKDFGIAEPRLAVAALNPHAGEGGALGREEIDIIAPAVEALRALGVQASGPAPADTLFHPEARARYDGVLCMYHDQALIPVKMLDFWGGVNITLGLPIVRTSPDHGTGFDIAGRGIARPDSLIAA... | 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).
Cataly... |
A8ALP8 | MATVQRVVITPGEPAGIGPDLVVQLAQREWPVELVVCADARLLTDRAALLGLPLSLLPYSPNHPAKPQSAGTLTLLPTALRAPVTPGQLSVENGQYVVDTLARACDGCLQGEFAALITGPVHKGVINDAGVPFTGHTEFFEARSQAKKVVMMLATEELRVALATTHLPLRAVADAITPALLHEVIGILHHDLRTKFGLADPHILVCGLNPHAGEGGHMGTEEIDTIVPVLDDLRAQGMRLSGPLPADTLFQPKYLDHADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTALELAGRGQADVGSFITALNL... | 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).
Cataly... |
Q47VJ9 | MTQRIAITPGEPAGVGPDLIITIAQQDWPVEMVVIASKALLQERSKALSLPLTIIDYDQHAPAKSQKSGSLTVLDVELTEPCVPGTLNSANGSYVVETLRIASEKNISGEFDAIVTGPVHKGLINKAGIAFSGHTEYFATQANCSDVVMMLATKGLRVALVTTHIPLAYVSKAITYERLQKVTRILHKDLQEKFGIKSPKIYACGINPHAGEDGHLGREEIEIMEPAFAELRADGIDIIGPLPADTIFQEKYLAEADAILAMYHDQGLPVLKYKGFGSSVNITLGLPFIRTSVDHGTALELAGKGTADSGSFIEAMNNAI... | 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).
Cataly... |
Q2SJQ9 | MKIVADENIPLLQPFFGSMGEIHTLPGREISNQHLRDADVLLVRSVTKVDERLLENTGVKFVGSATIGCNHVDLDYLTSRGIGFSNAPGCNASAVVEYVVSCLSVLSEQLGFELEDKTVGIIGRGEIGGRLERALTLLGLEVKSNDPPKEAAGEQNLFSLEEVLQCDIITLHTPLTDSGSYPTRELLNATIIENLRPDQILINTCRGEVIDEAALKGRLQKGDGLTVALDVWNNEPAIDVELAMLCHFATPHIAGYTLDGRTAGTEIIYQHLSRYLGLPVRHKLGQFLPEPPLRRMAFSSGVDPDWALHTAIRASYDVRH... | 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 b... |
Q31IH6 | MTPSRTLVIDDAVPYAKELFSHLGNVISLPGKEINTEHLQNADALIVRSRTQVNSALLEHTNVSFVGSTVVGLDHVDQPYLKENAIEFYSAQGCNANSVSEYVITNLVNLAIEKKFTLSEKSLAIIGVGHVGKLVEKKARALGMTVLLNDPPRARQEMSDEFIDLDNALKSDIITVHTPLTKTGQDATFHLLSTDKLKKIQPHQILINAARGGIIDEQAWINTPTESNIIDCWENEPNINPDLYNQADIATPHIAGHALDAKIAGSEMVYRALCQHWQISPDDSWRRFLPPPPPPISLSLTGNHQEDIHNVLQQCYRPEE... | 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 b... |
Q5QUE2 | MKIVADQNIPALSDLLSGAGTLSYFSERIPPQKLLAEADALLVRSVTQVDEVLLEQAPELKFVASATIGTEHINLQALEERGIGFAHAPGANAQSVGEYVLCAVLNWLSDQPRYVADEIDVAIVGAGHTGKAAGKRLEALGLNVHYYDPPLCKKGVKFVHDHWQRVLTADIISCHVPLTRDGDFPTQHLFENTALQSLHSQQLLINASRGAVIDNNALLERVEQGERPSLVLDVWENEPEVLSGLVPYVDIATPHIAGHSLEGKVGGAVMISNALLEHFGKPADKTLSDVLPGKAWNERDAGGLNSLESLNLWAKEHYDL... | 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 b... |
Q5WXZ0 | MNILADALLPGLDSAFPPPFTVTLYHKADEIPELLHHKDVLLCRSTLKINGDLLKHHQIKVVATATSGTDHIDFPFLESQNISIIDAKGCNATSVADYVVACLAYLDKQQLIQGKTAGIIGLGQVGTKVYERLNAAEFQLCLYDPPKATRDTSFQSCSLEDLLECDFLCVHAELHSNAPYPSLNLINRDFLKELKPGCIIINASRGGIINEEALLHLGSAILYCTDVYNNEPHIDNRIVSRATLCTPHIAGHSLEAKFAAVAIVSRKLHQMLGLPYPQFATPEKPYRLNDDSNWRELALSIYNPIHETLELKHAGNLSSA... | 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 b... |
A6VXM3 | MKIIADENMPNAKVLFSHLGDVELVNGRTLTHEQVREADVLLVRSVTKVTKELLEGSSVRFVGSATIGVDHIDLDYLSKANIGFSSAPGCNAEAVADYVFSALSHLYLTKKINWLSKKIGVIGYGNVGKTVYTRFANMGCQVHVYDPIREKEGGSANFVSLDEILSCDVISLHAPLTHTGSYPTKGMIGRKELAKLSAGVTIISAGRGGVIDESALFDRHKQLNGNLHLVLDVWDGEPAINQKLIAIVDIATPHIAGYSKQGREKGTWMVYQALCQYLALDANVISKHDAISAGWLSFVNVSAEEPQEEMLARSMHAIYD... | 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 b... |
A1U1I8 | MLIVADENIPLLDSFFGDIGEIRRVNGRTLTPDQVKDADILLVRSVTRVDRQLLEGTRVRFVGTATIGTDHIDQTWLQEQGIGFAAAPGCNAVSVAEYVLSVLSLYAEKRGIEDWSSLTVGIVGVGNVGGELARMLERLDFTVKLCDPPRQEAEEERAEEFVPLAEALECDVVTLHTPLTRTGDHPTNRMIAGSELAALGQDQLLINAGRGEVIDGEALLARLQQADAPTVVLDVWEHEPRINPDLLDRVWLATPHIAGYSLEGKMQGTEMIYQALCRYLGLPVRKKAGQFLPEPALSKVSFTSSADEDEAVQVALRACY... | 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 b... |
Q7MV70 | MKIVAEASVPYLRGIVDPVADITYLHSDCFSPDTIRHARVLIVRSITKCTPALLQGTDVRLITTATAGFDHIDREYCESHGILWRNSPGCNATAVAQYVMCCLCRLALREGFSLKEKVMGIVGVGHVGGELKRLASAYGMEFLLCDPPRSEAEQDNSFLPLSRLVEQCDIISFHVPLTHEDPHATYHLIGEAFLRSCADKRPILINACRGAVADTQALIRAVKSGWLQALVIDCWEGEPDIDLSLLDLADIATPHIAGFSADGKANGARMCLEAITEVFGLEFPLLHTLAPPPPTHPIIDLSLFPDHRIERALLHTFDPL... | 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 b... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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: ... |
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-am... |
Q58090 | MKKGTDLLKKGFAKMVKHGVVMDVTNVEQAQIAEEAGAVAVMALERVPADIRAAGGVARMSDPALIEEIMDAVSIPVMAKCRIGHTTEALVLEAIGVDMIDESEVLTQADPFFHIYKKKFNVPFVCGARNLGEAVRRIWEGAAMIRTKGEAGTGNIVEAVRHMRLMNEAIAQLQRMTDEEVYGVAKFYANRYAELAKTVREGMGLPATVLENEPIYEGFTLAEIIDGLYEVLLEVKKLGRLPVVNFAAGGVATPADAALMMQLGSDGVFVGSGIFKSENPLERARAIVEATYNYDKPDIVAEVSKNLGEAMKGIDITQIS... | 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 G... |
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 G... |
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-glutam... |
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-glutam... |
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-glutam... |
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-glutam... |
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-glutam... |
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-glutam... |
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-glutam... |
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-glutam... |
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-glutam... |
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.... |
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
|
P48612 | MKLLGKYVDKGMQGNVTLVPEESEDMWHAYNLIAKGDSVRSTTIRKVQNETATGSSTSSRVRTTLTIAVESIDFDTQACVLRLKGRNIEENQYVKMGAYHTLDLELNRKFELRKPEWDTIALERIEMACDPTQSADVAAVVMQEGLAHVCLITASMTLVRSKIEVSIPRKRKGSVQQHEKGLAKFYEQVMQSILRHVNFDVVKCVLIASPGFVRDQFYDYMFQQAVKMDYKLLLDNKSKFMLVHASSGFKHSLREILQDPAVLAKMSDTKAAGEVKALEQFYMMLQCEPAKAFYGKKHVLQAAESQAIETLLISDNLFRC... | 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-bi... |
A2BL82 | MKILAVDTKRGLVRVVPETTDDIWLLSTVIQPGDLVRAKTLREIHFGDRGSGRSSRIPMVLTVRVEAVEFQAFTTRLRIRGIVIEGPEKYGVVGKYHTLSIEPGRELDIVKPSGWPQVLIEKLKRGSYNVAAVVVAVDYDDYAVAVVRGQGVKILASGGLHLPGKDDPTREDKLREAVTVIAKTTADVARRENALLVVAAGPGTVKNLVAEKLRGLVQGVKILVDNVSMGGEAGVFEEVRRGIMRQALQDAAVVEAERILEEFERRLAKEPGRIAYTLEQVYRAAEMGAVEELLILDETLHHPDPEVRARVDELLRLADA... | 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
Seque... |
A8A935 | MRVLEVNESKGEVKVRVEDEEDVWILHSALRPGDLVRARTARSVAGSSGKEKIPMTLTIKVTGSEFQAFSNVLRVKGVVVEGPDKFGLIGSHHAIKVYPGKEITIIRERGLAQLLERLKKGEERKPQVPVLAVDYDEYSLAVVRGQGIEWVFEGSLRLPGKGDEGREAATERKINELAKRVSEELKLRNLDHVVVVGPGFLKDKVAQRLSEEGFKVKVDSASSGGRAGVLEAIRKGSLRGVAKELESIKALEALEEFVKHVARGDGYALYGVDDCMTAAQANAVKTLIISDDLLHSPDLGERAVELVELAEKKGAEVIIV... | 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
Seque... |
B1L659 | MRILEEDLKRGLVKLRVDNLNDIYWLASIIEEGDLITMKTLRRVKQEGIRADSGERIPMILTIEVDKVKLDPYSSRLRISGVVRVGPDKFGIQGQHHTFSVDEGSSLTIVKKEWRKTHLEILKRAESMSEKGEVLLVAMDDEGATIAKAGSMRVEEIAYIRSRLPSKMDTRGREGEERRYFSEILDTLRELYSKIKPRAIVVGGPGFFKDRFLSYARAKDPEMGEKMREGDASNATFSGVLEMIRRGEADKVLRELDLAKDMAAVEEIFELLSKNSDLVTYGVDEVLEAVNQGAAEIVLISASVFFDPDMRDKVFSLIEG... | 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
Seque... |
Q8TSZ1 | MRVTNRSLRGREGEIAITAETLDDLWHLKYIIEKGDLVFALTKRKADSASDKLRPEKVEKVKVRLGIRVEEMEFHKFANRLRIHGPIEHGMDVGSYHTLNVEIGTNISIIKERWKNDQLQRIQDAEEAGKRPKVVIVAVEEGDADIGFVRHYGIEVYSHIRQSSGKRENGLRSEFFREIVDQLRHAVPEDASIVIAGPGFTKEDFLKYFHETEPEMASKALTEDTSMIGMSGFQEVLRRGAVDRIMQESRIARESSLMEDLLREISMDGKAAYGFADVKNALKYGAVETLLIADETLREGREKGEDIDKVLMEVEQAQGK... | 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
Seque... |
Q2FQH4 | MKAEIEELQRSFGEIRLFPENSDDLWHLHNLITPGSLVYATTLRSVEGSQDKIRPEKQEKRPVRLGIRVEDVEFHEYSIRLRVFGTIESGVDIGSHHTLNLEPGYEISVIKSWSGSDLERIDRAIKGSTSEAIHILTVEEGEAELYRVQSYGPKQVWSLAAGSGKTAEVSSREEFSEAVVSQVSQLTGPLVIAGPGFVKEEIIAKFKRKNPSRSAPLVIGDTRAGGRRAVQEVIGQGILEKLNGDLQLAREVTCLDELMRRIGKDEPVAYGIDAVRDATGCGAVQTLMVVDTLLRDPDAADLIRQAEAMRSEVVIFSSRF... | 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
Seque... |
Q57638 | MKIIEEIPQKNIIKLMPENLDDLWVLYNIIEEGDKIFAVTERRVQDKGDVIRADRGAKRKMFLGIEVKNVEFDENTKRVRILGTIIHGPDDVPLGSHHTIEIKPFDELSIEKNWKKWQIERIKEAIESSKRPKVLVVVMDDEEADIFEVRDYSIKEICSIKSHTSKKLDYKINEELKKEYYHEIAKVLSEYDVDNILVAGPGFAKNSFYNFISSQYPELKNKIVVESISTTSRAGLNEVIKRGIINRIYAESRVAKETQLIEKLLEEIAKKGLAVYGIDEVKKALEYSAIDTLLVSDSLVRNHEIEKIIDTTEEMGGKVV... | 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
Seque... |
Q8TZ98 | MKVVEKDLDKGYIEVLPETLDDLWHLYHVVRKGDLVFALERRRVKDERAETIRRDKGERKPVYLGVRVEDVEFDKYANRLRIKGVIEHGPESGSHHTVNVTTGKRIKIVKDEWERKDLERIEEAEMSRPPVMLVAVDTGEGTIGIVRDYGLDVVARVRHNVPGKRGGDRRAEMRKFFHRLADEIERIAEEEGVEHIVVGGPGFVKSDFAEFLREERDIPAHVEDTGSAGEAGLIEMIRRGAVERAVEESRVAEEVKHLEEVFKRIGKGDDKVAYGVRECLKAAEFGAIDVLLVADEKFREAMVEGEEDVLNAVKYAERTG... | 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
Seque... |
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 ... |
A0A146F0J0 | MVNTSLLAALTAYAVAVAAAPTAPQVKGFSVNQVAVPKGVYRHPAAQLAKAYGKYHATVPTQVAAAAAATGSVTTNPTSNDEEYITQVTVGDDTLGLDFDTGSADLWVFSSQTPSSERSGHDYYTPGSSAQKIDGATWSISYGDGSSASGDVYKDKVTVGGVSYDSQAVESAEKVSSEFTQDTENDGLLGLAFSSINTVQPTPQKTFFDNVKSSLSEPIFAVALKHNAPGVYDFGYTDSSKYTGSITYTDVDNSQGFWSFTADGYSIGSDSSSDSITGIADTGTTLLLLDDSIVDAYYEQVNGASYDSSQGGYVFPSSAS... | 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' positio... |
Q12567 | MVVFSKTAALVLGLSTAVSAAPAPTRKGFTINQIARPANKTRTVNLPGLYARSLAKFGGTVPQSVKEAASKGSAVTTPQNNDEEYLTPVTVGKSTLHLDFDTGSADLWVFSDELPSSEQTGHDLYTPSSSATKLSGYSWDISYGDGSSASGDVYRDTVTVGGVTTNKQAVEAASKISSEFVQDTANDGLLGLAFSSINTVQPKAQTTFFDTVKSQLDSPLFAVQLKHDAPGVYDFGYIDDSKYTGSITYTDADSSQGYWGFSTDGYSIGDGSSSSSGFSAIADTGTTLILLDDEIVSAYYEQVSGAQESYEAGGYVFSCS... | 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' positio... |
Q9GMY6 | MKWLLLISLVALSECAIVKVPLVRKKSLRQNLIEHGLLNDFLKNQSPNPASKYFPQEPTVLATQSLKNYMDMEYFGTIGIGTPPQEFTVIFDTGSSNLWVPSVYCSSPACSNHNRFNPQESSTYQGTNRPVSIAYGTGSMTGILGYDTVQVGGIADTNQIFGLSETEPGSFLYYAPFDGILGLAYPQISASGATPVFDNMWNEGLVSQDLFSVYLSSDDQSGSVVMFGGIDSSYYSGNLNWVPVSVEGYWQITVDSVTMNGQAIACSDGCQAIVDTGTSLLAGPTNAIANIQSYIGASQNSYGQMVISCSAINSLPDIVF... | 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... |
P00793 | SIHRVPLKKGKSLRKQLKDHGLLEDFLKKHPYNPASKYHPVLTATESYEPMTNYMDASYYGTISIGTPQQDFSVIFDTGSSNLWVPSIYCKSSACSNHKRFDPSKSSTYVSTNETVYIAYGTGSMSGILGYDTVAVSSIDVQNQIFGLSETEPGSFFYYCNFDGILGLAFPSISSSGATPVFDNMMSQHLVAQDLFSVYLSKDGETGSFVLFGGIDPNYTTKGIYWVPLSAETYWQITMDRVTVGNKYVACFFTCQAIVDTGTSLLVMPQGAYNRIIKDLGVSSDGEISCDDISKLPDVTFHINGHAFTLPASAYVLNED... | 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... |
C5PEI9 | MQNRPRVFDSAMNLSPNMHFLSLMPGLLLLSLQVHTSPTPLKKTIRSVRIERIRQPNYVPDGPGALKKAYAKFGIIPSGISFDSFEDFTPFSSDNVRNTVSKAMQANETGIVTNTPTNNDVEYLSPVTIGGQKFVMNLDTGSSDTWVFNTQLSEDAKRGHSIFDPAKSKAFSDLEDATFNITYGDASFAFGRVGIDTVDIGGATVQKQAVGLPTDVSGSFILDQASDGLIGLGFDELNTVEPQQQKSFFTNLAANLDEPVLAAQLKKGAPGSYEFGSIDETKFKGDLVTIPVNNSRGFWEVKSTMFKVGKDEQLHRITKG... | 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' positio... |
P94870 | MAHELTVQELEKFSADFNKNPKNKVVARAAQRSGVLEASYNDRVQSELTRVFSTELDTDNVTNQKHSGRCWLFATLNVLRHEFGKKYKAKDFTFSQAYNFFWDKIERANMFYNRILDSADMPLDSRQVKTDLDFAGTDGGQFQMAAALVEKYGVVPSYAMPETFNTNDTTGFATALGDKLKKDALVLRKLKQEGKDDEIKKTREKFLSEVYQMTAIAVGEPPKKFDLEYRDDDKKYHLEKDLTPLEFLHKYLGGVDFDDYVVLTNAPDHEYDKLYGLPAEDNVSGSIRIKLLNVPMEYLTAASIAQLKDGEAVWFGNDVL... | 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 | MGSRRFDAEVYARRLALAAAATADAGLAGLVITPGYDLCYLIGSRAETFERLTALVLPAAGAPAVVLPRLELAALKQSAAAELGLRVCDWVDGDDPYGLVSAVLGGAPVATAVTDSMPALHMLPLADALGVLPVLATDVLRRLRMVKEETEIDALRKAGAAIDRVHARVPEFLVPGRTEADVAADIAEAIVAEGHSEVAFVIVGSGPHGADPHHGYSDRELREGDIVVVDIGGTYGPGYHSDSTRTYSIGEPDSDVAQSYSMLQRAQRAAFEAIRPGVTAEQVDAAARDVLAEAGLAEYFVHRTGHGIGLCVHEEPYIVA... | 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... |
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... |
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... |
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... |
P55179 | MKEEIIERFTTYVKVDTQSDESVDTCPSTPGQLTLGNMLVDELKSIGMQDAAIDENGYVMATLPSNTEKDVPTIGFLAHVDTATDFTGKNVNPQIIESYDGKDIVLNEQLQVTLSPDQFPELSGYKGHTLITTDGTTLLGADNKAGIAEIMTAMDYLIKHPEIKHGTIRVAFTPDEEIGRGPHKFDVKRFNASFAYTVDGGPLGELEYESFNAAAAKITIKGNNVHPGTAKGKMINSAKIAMKLNSLLPADEAPEYTEGYEGFYHLLSIQGDVEETKLHYIIRDFDKENFQNRKETMKRAVEELQNEYGQDRILLDMNDQ... | 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 | MTLVDRFLKYVSFDTQSDESTGLTPSTPKQMVFAEYLKTELESLGLEDITLDEHGYLFATLPANIDKKVPTIGFIAHMDTSPDMTGKDVTPRIVKGYDGTDIVLCAEENIILSPAQFPELLDHKGEDLIVTNGKTLLGADDKAGIAEIVSAIVYLKEHPEIKHGKIRIGFNPDEEIGEGAHKFDVGKFGCEWAYTMDGGEVGELEFENFNAAAAKITFKGRNVHPGYAKNKMINSIRVANQFIAMLPSTETPEQTEGYEGFYHLISIQGDVEQSTVSYIIRDHDRAKFEKRKEEIKRLVAQVNTEYGEGTATLELRDQYY... | 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 | MKLNQFARLTPDFKVQVAELKQIGLQADPDDTFSQSTTDLFNAFFPEAYTLAAKKDKLAQVAVNMDQTLAAWLAKKPSKMTRRDFYNVALQLLGFEAFTDFDLNDPFKMMTATKLPSLDHDLTSTADLLKAVYLLLNTRTKHLVSYLDDLANRGFLKDFQKKQKKPTHLLFNGKVQQVFDARQAVREVVWIESDMDTDHDGQRDLLEATIYRPKATDQGLKVPVLFTANPYFHGTNDVTAVTHVPETTLAVKTHGASKAEVTANPEEPANLPHHPVNGEATQAEAYAEENGMYAFNDYFLARGFAVVYSAGVGTRYSDGF... | 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-Pr... |
Q88YC0 | MKNNQFAIVPTDSETAIAELTKIHFITPDMDALTTVPAVYQALLAKSLPEVHTASGLTHKFNNIMATSQHTLSEWLADATIVNNQVFYNVGLQLLGFLPGQDFELADPLLAMRDIHLPMVGDSAFDREALYYAWYLLLNTRGNNGQTLIESLTTRGYFVPFYQLPNDQKPLFFNGKAQAVFDTNALIRDVVYVEAPLDTDHDGQRDLLKVEILRPAETETGLKVPVLYTASPYNQGINDQAGDAQMHNVDVPLTAKEPDENTYADVEFQPTTAQLPAARTATTTTDTAEETFSREKSYTLNDYFLARGFAVVYAAGIGSI... | 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-Pr... |
Q03PM5 | MRNQQFAIRPTTLDQARVELQQIHFLDDTNLSFTTPSDLLRDFYDRSWPEYTTSSVVAQQLSNLMATPETDGLTYLTTHEQVPVDVFYNLALQRLGFAVDLDFQLTDPLAAMTKIQLPVADHEGTTFTLNELMNAWYVLLTTHNKTGQTFLDQLTTHGYFAPLIHDNSVPKPLIFNGKAQAVFDTTQLIHEVVYVESPQDTDHDGHRDLLKAEIIRPAETANGLKVPVLYTASPYNQGTNDEAGEALTHNVNVPLTAKQPAATTLADVTAESVTTPLPDARPVTATTHTAAETFAREQSYTLNDYFLARGFAVVYAAGIG... | 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-Pr... |
Q03H46 | MKNNQFGRIRLDRTTELEELKNIHFIDADLLADPKAQLKDFLKRSCLVSNSEATFQQKLSNLLATPDQTMAAFFESDQPLTLEIFILLELQLLQFEADTDYQIEDPLSAISKIQLPELDLKNFETSADVAHAWYNLLTTHTKNGEVYLDRLTQQGYFVSFYPTTTKPLFFNGKAQAVFDPHQLIREVVYVEAPLDTDHDGQRDLLKAEILRPAQTAHGYQAPVLYTASPYNQGTNDSYGEAITHNVDVPLTEKAVQKISKSDVTAEPFSQTLPAERKVAGMATKASETFAREQPYTLNNYFLSRGFAVVYAAGIGTRDSD... | 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-Pr... |
Q93M42 | MRYNQYSYTKASEEVMLDELARLGFTIQTTNSPKENLHHFLQKILFRYQDVNYVLSSWVADQKTDLLTFFQSDKQLTEEVFYTVALQVLGFAPFVDFDDVTAFCKEIHFPITYGNILENLYQLLNTRTKLGNTLIDQLVSEGFIPESNDYHFFNGKSLATFSSHEAIREVVYVESRVDTDGDGKPDLVKVSIIRPSYEGQVPAVMTASPYHQGTNDKASDKALHNMNVDLSCKNPRTITVQESSIQTIEPQGQASLVEKAEEKLGHIGSYTLNDYLLPRGFANLYVSGVGTKDSEGMMTSGDYQQIEAYKNVIDWLNGRC... | 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-Pr... |
P82600 | MAKKVLLLSLYSAVLSTWFGFGYVQCKLPTSRSEIPNFDYTVAQQPDQSDACEQNEVCMVSVECILDAKKKAILKPCSTVPSVDGVCCPSSEYNGTSSRVQQNSEEHAADHLVLQAIHEGRREYDEKLRFEDEHRAVMTAKEKPEAMFHRMFLPGGLKTHGKEVVDAEEQANVYGHVFASRKYAELTNMTLKQRQGDRFARIPRAIRKRCLPPVPCNPHSRYRTIDGSCNNPLPDRTSWGMEGYPFDRVLEPAYEDGVWAPRIHSVTGNLLPSARVISVALFPDEYRPDPRLNILFMQMGQFISHDFTLSRGFTTKHGQA... | 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 A... |
Q7QH73 | MLPKGVLLFLVLIVLVQHFATVQTTNAIERPSAPSSQCTSSHESCVLRVMCEVEPRARTTLVPCLTADGLEGVCCSVAKEGKQRKKRSLPFELSQELFQNAVGEGHRVYTRKLANIDHHREVMRGGSVDTLVRQFHAPPGEPLGAEDPTAYEDMFVARSFANALNLSVAERLDLPELTLDPALRRKRCLPPRSCDPHARYRSLDGSCNNPVPARSSWGAAGYPFERLLPPAYEDGVWAPRVHSSVSGRLLASARDISVAVFPDVDRRDRKFNLLLMQFGQFMSHDFTRSASVRIGQEEVQCCNAEHSGALRGEQAHFACM... | 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.
Catalyt... |
Q9VEG6 | MSRILFILLLLIVTQLSELQAAAFSVRQNRFDEVPDLQTPAPLATSTESSKKPEKATSGLLKKCLPCSDGIRCVPQIQCPAHVRMESHEKPQICDLPAGKFGYCCETGQNHTAPKPETSPKERRSGFPTILSPAVLDEARRNFEHLMHGVAQIPVRRGFPDFAHGLVFHSTAKDDLHNFAISNSAIEQVMTTQLFGKKEQVPVEDFITNNVPIKFTETPLAHHCQPPPVCGNIRSVYRSMDGTCNNPEPQRSLWGAAGQPMERMLPPAYEDGIWTPRAHSSDGTPLLGARKISRTLLSDVDRPHPKYNLMVMQFGQVLAH... | 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.
Cata... |
P11678 | MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVS... | 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... |
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... |
P10820 | MATCLFLLGLFLLLPRPVPAPCYTATRSECKQKHKFVPGVWMAGEGMDVTTLRRSGSFPVNTQRFLRPDRTCTLCKNSLMRDATQRLPVAITHWRPHSSHCQRNVAAAKVHSTEGVAREAAANINNDWRVGLDVNPRPEANMRASVAGSHSKVANFAAEKTYQDQYNFNSDTVECRMYSFRLVQKPPLHLDFKKALRALPRNFNSSTEHAYHRLISSYGTHFITAVDLGGRISVLTALRTCQLTLNGLTADEVGDCLNVEAQVSIGAQASVSSEYKACEEKKKQHKMATSFHQTYRERHVEVLGGPLDSTHDLLFGNQAT... | 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 faci... |
P41219 | MSHHPSGLRAGFSSTSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSASPSSSVRLGSFRSPRAGAGALLRLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYESIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQ... | 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 inter... |
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 ... |
Q25020 | GVVMYTTSSITATLGFPKDMWIGRSFIDFLHPKDANTFASQITNGLAIPKIVNDTQEKAQIFGTQGSTMVCRIRRYRGLSSGFGVKDTSVSYMPFLLKFRFRNISDDKGLVVYLVIQTVPFFSAYKTPNEILTQEVSFIMRHSANGNLEYIDPDCVPYLGYIPQDITNRNALVLYHPGDLPFLQEVYQAIVKEGSVTRSKSYRMVTQNGHFIKVETEWSAFINPWSRKLEFVNGKYYIIEGPANPDVFESPDPEKTPKLTEERKNQAQICRDDIIRIMNEVLTNPAEIAKQQMSKRCQELALFMEILQEEQPKAEEEFHL... | 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 transcript... |
Q25478 | GIVMYTTSSLTTTLGFPKDMWIGRSFIDFVHPRDRNTFASQITSGLAVPKIVNGQSPGNPASTMVCRIRRYRGLTTGFGVKDRVVTFMPFLLKFTFKNVSDEEGKVIYLVIQATQFFSAFRIPSEVVSKAVPFVMRHAANGNLEYIDPESVPYLGYLPQDVTDKDALQLYHPEDLDYLQQVYETIVKEGGVPRTKAYRMMAQNGDYLKLETEWSSFINPWSKRLDFVIGKHHIIEGPSNPDVFQSPDPEKAVAMSEEEKAKEQKYRRDIIRTMNEVLTKPAEVAKQQMTKRCQDLASFMESLMEEQQPKVDEDLRLDIQD... | 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 transcript... |
Q25637 | MEETATHNTKISDSAYSNSSNSQSQRSSGSSKSRHSNSSGSSGYCGHGSSIQGSSNEPFPQPSVTKRNKDKEHKKKKLKSSVTTAATATVTSVVTTVSEYTEHENGTSHMSLGVSGTVVPLSGTVAEETEITEAGSEGSVISSHAGVALGAAGVVPATTPGPENEAHQMASLTQTLNSIKKMKKMKDLSTDIPEETEGHSFSLPMVAEEKEEHIRNSFDAEPPAHNEGEFCVVVSMQDGVVVFTTPSITDVVGFPKDMWLGRSFIDFVHPRDRTAFANHITSGVITPLSNSNPKGGSHPGKNSFYCCLRRYRGLKSTGYG... | 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 transcript... |
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 ... |
Q9ZVN2 | MATCSSSLLVLPNLRLSSNQRRNFKVRAQISGENKKATSLEPVNNNGSVSLSTTVQNQKGANEVNGKGKSKRKIVSDEIELLWDDGYGSKSVKDYFAAAKEILKADGGPPRWFSPVDCGRPVEDAPTLLFLPGMDGTGMGLVPHHKALGKAFHVSCLHIPVLDRTPFEGLLKVVEDVLRQEQATRPNKPIYLVGDSFGGCLALAVAARNRSLDLVLILVNPATSFDRSPLQPLLPILEMVPEELHFTVPYALSFIMGDPIKMATLGIDNQLPTGVKIEKLRQRLTKTMLPLLSELGGIIPRETLLWKLKLLRSGCAYANS... | 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... |
Q9LW26 | MAVTVLPSVSGLSAVASSSNLRRLTSASNHRLTAIKSVTSTSSPPTPSSGVQRRRKNNDENRATVAKVVENPYSKVEAARPDLQKRLSDFLEEAREFVGDGGGPPRWFSPLECGAQATNSPLLLYLPGIDGTGLGLIRHHKKLGEIFDIWCLHIPVSDRTPVKDLVKLIEETVKSENFRLPNRPIYLVGESIGACLALDVAARNPNIDLSLILVNPATHVNNFMVQPLSGMLNVLPDGLPTLLEDIFDFGFKQGDPLTGMLDALSNEFSVQRMGGVGGGMLRDVLAVSANLPTLSRMFPKDTLLWKLEMLKYAIASVNSH... | 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... |
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), ... |
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) ... |
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... |
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... |
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... |
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... |
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