ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q06J45 | MEVNILGVIAVALFILIPTSFLLILYVKTSAENKDN | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3964
Sequence Length: 36
Subcellular Location: Plastid
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Q09MI4 | MEVNILAFIATTLFVLVPTAFLLIIYVKTVSQSD | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3772
Sequence Length: 34
Subcellular Location: Plastid
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A7M8Z5 | MEVNILAFSATALLILFPTALLLILYVKTVSQNN | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3736
Sequence Length: 34
Subcellular Location: Plastid membrane
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C0HJG3 | MDSTAFVGAAAPLRVAAAARSTICMAAADDKPVVSRRAALTGAAAAALAAVAGSLPALAETEYANVPFLGGSVIIDINNANVRAYAKYPGMYPTVAGLIATNGPFETVSDLYKIPGLTDLQIATLKKYEDKLVALTPTPEYELDKVNNGLYR | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation (By similarity).
PTM: Predicted to be translocated into the thylakoid lumen by the Tat system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15777
Sequence Length: 152
Subcellular Location: Plastid
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Q7U480 | MKRLLSWLTGALLMAGLLAGLILPGSVHADEDLVGKYSGNEIRNIADDKIAAREGKVDLNNSSVRRFQQFPGMYPTMAGKIVLGGPYNDVDEVLNLDLSERQIELFNKYKENFTVTPPEIALNEGDDRINDGQYR | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15012
Sequence Length: 135
Subcellular Location: Cellular thylakoid membrane
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Q84XB6 | MKLAVFAVLISTVAAFVAPNGVQRAATTELNAERREFLSAAAVAAGLAFPLTANAIRDYENVGYLGGSEIVDVNNANVRVYLKMPGLYPTLAGKIASNGPYNAVGDLYNIPGLSGKEKELLKKYESRFTAQKPQADYVIDRFNNGLYR | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
PTM: Might be translocated into the thylakoid lumen by the Tat system. The position of the transit peptide cleavages have not been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15991
Sequence Length: 148
Subcellular Location: Plastid
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P20094 | MKRLVGVLMILGLMLTSWGLLGSPQTAIAASLSPLSFNPSPVLAEQQFRNAMDDKLATDFGKKIDLNNTNVRAFMQYPGMYPTLARMILKNAPFESVEDVLKMPGLTDTQKEILKNNFSNFVVSPPLDALVEGGDRFNNGIYR | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15810
Sequence Length: 143
Subcellular Location: Cellular thylakoid membrane
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Q31M07 | MKQLAQRLFSLALVLALVLGISVQSAQALSLQSPLLAVAEAEIRNEADAQRIEAGGKLDLNNIGVRAFQQFPGMYPYLASKIVLGGPYDSVDDVLKLDLSDRQREVFEQYKENFTVTPPRDALNEGDDRINNGIYR | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15066
Sequence Length: 136
Subcellular Location: Cellular thylakoid membrane
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Q2JSX7 | MRRLLSALVSILLLLCLCLVPLGIPAVAAELPPVKHLDTPIDVNNTILRNYRQLPGFYPTLARILVKNAPYNSLEDMLQIPELTEQQKALIKANAENFVFGEYQEGANQLENRINQGYYG | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13479
Sequence Length: 120
Subcellular Location: Cellular thylakoid membrane
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Q2JPY4 | MRWLLSILVRVVLVLCLCFAPLGIPVVARAAELPPVKHLDTPIDVNNTILRNYRQLPGFYPTLARILVKNAPYKSLEDMLQISGLTEQQKALIKANAENFVFGEYQEGANQLENRINQGYYG | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13771
Sequence Length: 122
Subcellular Location: Cellular thylakoid membrane
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Q55332 | MKFISRLLVACSLLIGLMGFLGADLAQALTPNPILAELNAVDAKLTTDFGQKIDLNNSDIRDFRGLRGFYPNLASEIIKNAPYDTVEEVLDIPGLSETQKSRLEANLGSFTVTEPSIELTSGDDRINPGVY | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation. May modulate the Cl(-) requirement for oxygen evolution.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14245
Sequence Length: 131
Subcellular Location: Cellular thylakoid membrane
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P80460 | MLNAVDAKLTTDFGQR | Function: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 1780
Sequence Length: 16
Subcellular Location: Cellular thylakoid membrane
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C6WID8 | MDNSSTGRYPAASLPPAYLRPGSSSFTDFLRAQAPELLPTARSFPEGSVVQAAHGTTIVALTFKGGVVIAGDRRATMGNVIAQRDMKKVFVTDDYSAVGIAGTAGIAIEIVRLFAVELRHYEKIEGVSLSLDGKANRLSGMVKGNLDAALAGLAVVPLFVGYDTDAADPDRAGRIVSYDVTGARFEETLGYQSVGSGSLFAKSALKKLYDPDADAEGAVRAAVEALYDAADDDSATGGPDLVRRIFPVVVTVTAEGAVHLPEERTSAIAETVVEGRRARPAG | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 29490
Sequence Length: 282
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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Q9P996 | MSMIEEKIYKGTTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIATLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRAIYSAMKRDSASGDGIDVVKITEDEFYQYSPEEVEQILAKFRK | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 23418
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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B9LTS6 | MRTPTGDLSDGPAEELGRDQPVFGPEIGEFEHSERRAAQADGEGEMKTGTTTVGIKTADGVVMATDMRASLGGMVSSKDVQKVEEVHPRGALTIAGSVSAAQNLISTLKAETSLYETRRGKDMSMEALSTLTGNLLRSGAFYIVQPILGGVDDEGSHIYSIDALGGTTEEEYTVTGSGSQYALGVLEQEYDDDVTVDEAKTMAAKAIQSAVERDLASGNGINVAVVTDDGVDITRYKDFDDLL | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 25677
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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D4GYZ1 | MRTPTHDEFSGRLDSLNGDRSNVFGPELGEFSNADRRADELGDKETKTGTTTVGIKTEEGVVLATDMRASMGYMVSSKDVQKVEEIHPTGALTIAGSVSAAQSLISSLRAEVRLYEARRGEDMSMQALSTLVGNFLRSGGFYVVQPILGGVDETGPHIYSIDPAGSILEEEYTVTGSGSQYALGVLEQEFEDGLSIEEAKGVATKAIRSAVERDLASGNGINIAVVTEDGVDIQRHQNFEGLE | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 25994
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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G0Y286 | MTMHQDHGVMKDLVKHPNEFPYLLQLAATTYGSPAAPIPKEPDRAFCYNTLHTVSKGFPRFVMRLPQELQDPICIFYLLLRALDTVEDDMNLKSETKISLLRVFHEHCSDRNWSMKSDYGIYADLMERFPLVVSVLEKLPPATQQTFRENVKYMGNGMADFIDKQILTVDEYDLYCHYVAGSCGIAVTKVIVQFNLATPEADSYDFSNSLGLLLQKANIITDYNEDINEEPRPRMFWPQEIWGKYAEKLADFNEPENIDTAVKCLNHMVTDAMRHIEPSLKGMVYFTDKTVFRALALLLVTAFGHLSTLYNNPNVFKEKVRQRKGRIARLVMSSRNVPGLFRTCLKLANNFESRCKQETANDPTVAMTIKRLQSIQATCRDGLAKYDTPSGLKSFCAAPTPTK | Function: Catalyzes the biosynthesis of presqualene diphosphate (PSPP). Works in combination with SSL-2 or SSL-3 to produce respectively squalene or botryococcene. In most other species, farnesyl diphosphate (FPP) is converted into squalene in a two-step reaction by a single enzyme.
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate
Sequence Mass (Da): 45953
Sequence Length: 403
EC: 2.5.1.103
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Q6F6W3 | MSFTSRLKKDLFIKAQSLVPQHQLSRVVGKVAESENILIKAAVIQAFKTKYGIDLSIAEQADALKYKSFNEFFTRALKEGVRVVDSATGSIVSPADGAISQLGTIHDGEVFQAKGQSFSVEKLIGDPQLAQPFKQGQFATVYLSPRDYHRVHMPFTGTLTETLYIPGELFSVNQVTAENIPGLFARNERMVCLFDTELGRMAVVLVGAMIVAGIETVVTGKVKPTGRLELNHHDVTLQKGDELGRFYLGSTAIILFEKDKMVWDQQFKANSIVVMGEKLGQSTNP | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31370
Sequence Length: 285
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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C1F3M6 | MVRDGYFYGLALLVVAVIVHLLTGGWSWAVLPLLLAAFFLWFFRDPKRAIPGGEGLVVSPADGKVTEVARIRTPQGELQRISIFLSVFDVHVNRSPVAGTIASVAYQKGLYLNAMDPASAKKNEQNTVVVRADAGYEITFKQIAGLLARRIVFTKRVGDRVERGQRVGLIKFGSRTDILMPPGFEILVRQGQRVSGGSTILARAAEGAGVLAAAPTAPGTLASTERPI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24527
Sequence Length: 228
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q8UGH4 | MNLFDTIRNTIVPIHKEGYVFVAAFFVASLVLGWIAEPLFWVGLVLTAWCAYFFRDPERVTPQDDDLIISPADGKVSAVQSVVPPLELELGKEPMVRISVFMNVFNCHVNRAPVRGRIVNVAYRPGLFLNAEVDKASEDNERNGLVIETSHGKVGVVQIAGMVARRIVCWVKPNEPVDAGERFGLIRFGSRLDIFLPAGFEPRVSVGQTAIAGETVLAEFGSAKGPVLSRRG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25478
Sequence Length: 232
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q221E5 | MFDRLAVLPQYLLPKQAITLLAGRVAGARGGKWTTRLIEWFVKRYKVNMREAANPEVASYATFNDFFTRALQAGARPLARADLICPVDGAISQFGAMAGQQIFQAKGHHYSSTALVGGDAALAAQFDDGHFATLYLSPRDYHRIHMPCDGVLRRMIYVPGALFSVNPTTALGVPGLFARNERVVCVFESARGPFVLVLVGATIVGSMATVWHGVVNPPRSTAVREWRYDEQPVRLKQGEEMGRFLLGSTVVMLFPKGPLQFNPAWSPGAAIRLGEAMARQPPLA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31070
Sequence Length: 284
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q0VMD7 | MSLRDKLFVTLQYLIPQHALSRLVGILARSEVPWIKTTFINMFMKRFGIDLSEAQIEDADQFPTFNAFFTRALKADARPLEASESNDIASPADGAVSQLGAIRANQVFQAKGHDYSLYDLLGGDSALASEFTNGQFATVYLSPRDYHRVHMPFTGTLRETRYVPGDLFSVNEATANGVPNLFARNERLVCIFDTEQGPMAVILVGAMIVAGIETVFSGQVTPLPKQVVTTDYLRSKPIALEKGEELGRFLLGSTVVMLFPEGKAKFAPNLKPGSQVRVRGKLGAYTNENKH | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32065
Sequence Length: 291
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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B3QU02 | MITPYGKKTLGQALVISMIFFALSYVLPPISSLIVSSLAIFILVFTLQFFRDPERKTPQKPNIIISPADGKVVLIKDLDFHDYFQGPVKQISIFMSPINVHVNRIPISGRVTHYKYIPGQYLMAFDHASGENNERTEIGIEGKNMKVFFKQISGFVARRIICEVRPGDEVEIGKRFGMIRFGSRVDIFFPPTVSLKVSEGQKTTAGETIIGEY | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23978
Sequence Length: 213
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q93SU4 | MRIAPYGTGSVVKTAIFCFVIFITALFLPQPGGVILATAALGFLLFTLYFYRDPERKIPDGKGLVIAPADGKIVLKQTLDHPVTGPGSTLVSIFMSPFNVHVNRIPVDGLVRDLRYHEGKFLMAFDHRSMTDNERMEITLDTAAGPLWFCQVSGFVARRIVCDLEAGQEVASGKRFGMIKLGSRVDIVLPSSIQIKVKEGMKTTAGETILGQTGGF | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23537
Sequence Length: 216
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q1QUI2 | MDTPVDRDELFARMQYPLPHHLISRGVGKLAESRTPWLKDWAIRRFIRTFDVDMSQALESDPEAYACFNDFFTRALRADARPIGEGVVSPADGTLSQFGAIRQDTLVQAKGHTYSLNALLGGDAARAAPFREGSFATVYLSPRDYHRVHMPVTGTLREMVYVPGRLFSVNQATANHVPGLFARNERLVCLFDTEHGPLAMVLVGAMIVAAIETVWAGQVTPLSGRVQTTRFDEPIVIEKGQEMGRFKLGSTVVMCFGHDVAFRDVCTDGLVVNMGQSLAS | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30890
Sequence Length: 280
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q3IFN3 | MSLDKFKIAMQYAMPKHFISRVVGKLAAAKAGVLTTTLIKLFIKQYKVDMSEAKHPDPAHYESFNEFFTRPLKDGARPIVADSDIIIHPVDGAISQLGDIVDGQLIQAKGHDYSLQALLGGNKDDTTPFLGGKFATIYLAPKDYHRIHMPIDGTLSKMIYVPGDLFSVNPLTAQNVPNLFARNERVVAIFETEIGPLAMVLVGATIVASIETIWAGTVTPPAGSDVFSWNYPTKGENAISLKKGEEMGRFKLGSTVVLAWGDDKADILDDQLPETVTRLGTPFAKIDD | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31432
Sequence Length: 288
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q4FQD5 | MNVFTTLQQFVPQQKISKVAGRLAASRHPWVKRTFIRSFAKAYDVSLDEYERQSLNAYESFNDFFTRELQDNARIIDASINGIVSPADGMISQLGQIHDHKLLQAKGRDYDIGQLLADSADGDYFADGSFATVYLAPSNYHRVHMPFDGTLIKTRYVPGTLFSVNNTTAANVPDLFARNERLVCLFDTAYGKAAVVMVGAMIVAGIETVATGKISRTDDIQEADHDMSFKKGDELGRFYLGSTAIVVLPKAAKTEWQATMQHGSTVQMGQLLANAKI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30614
Sequence Length: 277
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q9FDI9 | MSLIDTVRNTLVPVHREGYRFIAIFFVVSLALGFLWEPLMWIGFVLTAWCAYFFRDPERMTPIDDDLVISPADGTVSSVATVMPPEELGLGSEPMLRISVFMNVFNCHVNRAPMGGTVRRIAYRAGKFVNAELDKASQENERNGLVIETKHGQIGVVQIAGLVARRILCWTRESASLEAGERFGLIRFGSRLDVFLPAGAEPRVTVGQTATGGETVLAEFGSAKGPVISRRA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Important for establishment of root nodule symbiosis with the host plant.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25472
Sequence Length: 232
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q7UTK9 | MKYYRNQDSYWWADADDPFLWRESLPFVRVGLAELIIMTLVSLVLAVIAGWFWWPLAVPFVLVAALVAWFFRNPRRKVPETIGTVVSPADGKLVEIVEVDDPIIGAAVRFGIFLSVFNVHANRIAMPGRVVRVRYRPGKFLNALRSESTKENENIDVELECPEIGGRIVRIRQITGQFARRIVCWARVGDVLQRGEMFGMIKLGSRTELVIPRDEALEIVAQVGEKVCAGSTVFARYQQG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27178
Sequence Length: 240
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q0SES0 | MARKPTPPGTQQPTSVGHILDLVRGAVPPLHPAGLPFVLAPLGVAVLGRKRKWVRRGALTSAAACAAFFRHPHRVPPNRVGVVVAPADGEVALVDSAVPPAELDMGTEPLPRVSIFLSVLDVHVQRSPVGGEVTKVVHRPGQFLSADLADASEVNERNSMLLHTPEGHDVAVVQIAGLLARRIVCDAKVGDTLPIGDTYGLIRFGSRVDTYFPAGTTLLAERGQRTIGAETVIAQLP | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25037
Sequence Length: 237
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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Q6PGN9 | MEDLEEDVRFIVDETLDFGGLSPSDSREEEDITVLVTPEKPLRRGLSHRSDPNAVAPAPQGVRLSLGPLSPEKLEEILDEANRLAAQLEQCALQDRESAGEGLGPRRVKPSPRRETFVLKDSPVRDLLPTVNSLTRSTPSPSSLTPRLRSNDRKGSVRALRATSGKRPSNMKRESPTCNLFPASKSPASSPLTRSTPPVRGRAGPSGRAAASEETRAAKLRVSGSGEFVGLTLKFLHPSPPGPPTPIRSVLAPQPSTSNSQRLPRPQGAAAKSSSQLPIPSAIPRPASRMPLTSRSVPPGRGALPPDSLSTRKGLPRPSTAGHRVRESGHKVPVSQRLNLPVMGATRSNLQPPRKVAVPGPTR | Function: Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A and ANKRD53 to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression.
PTM: Phosphorylated during mitosis.
Sequence Mass (Da): 38796
Sequence Length: 363
Subcellular Location: Cytoplasm
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Q3KR66 | MEDLKEDIKFIVDETLDFGGLSPSDSHEEEDITVLVSPEKPLRRGLSHRSNPNAVAPALQGVRFSLGPLSPEKLEEILDEANRLAAQLEECALKDSENAAAGPGRPSPRGKPSPRRETFVLKDSPVRDLLPTVSSWSAPPPSNLTGLRSSDKKGSARAGRVTAGKKPSSIKKESPTCNLFSASKNPGRSPLAQPTLPPRRKTGSGARTVASPPIPVRPAPQSSASNSQCSSWLQGAAAKSSSRLPFPSAIPKPAIRMPLTGRSIPAGKGALAPDPLPTQKGHPSTVGHRAPVSQRTNLPTIGAARGRTSSAARGRVQPLRKAAVPGPTR | Function: Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A and ANKRD53 to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression (By similarity).
PTM: Phosphorylated during mitosis.
Sequence Mass (Da): 34577
Sequence Length: 329
Subcellular Location: Cytoplasm
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P31077 | MNQMWGSIEQYNTVVWHWPIAVYLFLAGLSAGAIISAIIIKWMKGNESSPWDGIIKAGALIAPLTIGAGLLLLIFDLTRPLHFWKLLIFYNFSSVMTLGVLALFAYFPVVLIFLLGVFKKELCDEGPFGFLAPLANIAYSMARPLEIVTFVLAIGVGAYTGFLLSAMYSYPLLNTPILPLLFLASGISAGISGNLLIGLLFFGKSTKGENVGYLHGLDFKVILFEAFLLFILFVGMYYQGGSTAEVAKAALTTGGLASLFWLGVAGMGLALPVVLNVALPHGIKHSSGFVMLNALIVLAGVMALRFYILYAGQTFVG | Function: Could possibly serve as the membrane anchor of the enzyme.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34137
Sequence Length: 317
Subcellular Location: Cell inner membrane
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P0DH87 | MRGELPNKHHSYTFFVFLFFFLILFPDLSISVNTLSATESLTISSNKTIVSPGGVFELGFFRILGDSWYLGIWYKKISQRTYVWVANRDTPLSNPIGILKISNANLVILDNSDTHVWSTNLTGAVRSSVVAELLDNGNFVLRGSKINESDEFLWQSFDFPTDTLLPQMKLGRDHKRGLNRFVTSWKSSFDPSSGSFMFKLETLGLPEFFGFTSFLEVYRSGPWDGLRFSGILEMQQWDDIIYNFTENREEVAYTFRVTDHNSYSRLTINTVGRLEGFTWEPTQQEWNMFWFMPKDTCDLYGICGPYAYCDMSTSPTCNCIKGFQPLSPQDWASGDVTGRCRRKTQLTCGEDRFFRLMNMKIPATTAAIVDKRIGLKECEEKCKTHCNCTAYANSDIRNGGSGCIIWIGEFRDIRNYAADGQDLFVRLAAAEFGERRTIRGKIIGLIIGISLMLVLSFIIYCFWKKKQKRARATAAPIGYRDRIQELIITNGVVMSSGRRLLGEEEDLELPLTEFETVVMATENFSDSNILGRGGFGIVYKGRLLDG | Function: Truncated and inactivated form of SRK, the female specificity determinant of self-incompatibility when active. Most A.thaliana cultivars contain such an inactive form and thus, are self-fertiles.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 62093
Sequence Length: 546
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
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P75185 | MKQKIKSRLKKDNWLRYLSQTVAVCFLLLFISFFIFLLIEAAKTGPDFTKSLLGLEFNLGAKKASIWFPLLVSFVVSIGSLIIASYIGVRTSIFLVYRCKPRIRKKLLLVIDILSGIPSVIFGLFATQILSSIFRDVLHLPPLSLLNVIVMLSFMIIPIVISLTTNALLHVESSLMTVAISLGENKTSVIYKVIKKEIKAQLVVILVLAFGRAISETMAVNFILQSVNYQEVIANDRFFTSDLKTLGSVISTFIFSENGDEQVSGVLYTFGIIIFVLISFLNFFAIWSTRPKTLERYPFLKKISNFIYQVVWFIPNNIGALFTDLTARRQQVKKITAANVEQRATFFKERMQTNHLNKVYTSWKILQEIFCAVLAFGFVLGILLFVFINGSQAIQRSGSTVFSFGVDTTGRALVNTLVIILVAIGITFPIALLIAIWLNEYTKSRIAKNTFSFVIDSLSSMPSIIYGLFGLSFFLRTLQLSAGGANGTSLMAGILTISVVVLPFLIRTCQEALNNVSWDLRVSAYALGVSKREVIWKIVLPGALKGLIIALILTINRIIAETAPFFITAGLASSNLFDLSLPGQTLTTRIYGQLFSTNSTAVDVMLETALVSIVFLMFLIFLSSYLIPYLFSFNKQKWLQIKSKLQLWKKA | Function: Could be part of a binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72748
Sequence Length: 651
Subcellular Location: Cell membrane
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Q98FL4 | MSTAASLHQSRKRKNGVMMMLCVVAAGIGLAWLALILGALLYKGLAGVSLSVFTEMTPPPGDAGGLLNAIYGSIVMTIIGIIVGTPIGVLAGTYMAEYGRFSKLTTVVRFINDILLSAPSIIIGLFVYELMVRPMGHFSAIAGAVALAILVIPVVVRTTEDMLNLVPNALREAGTAIGAPRWVVIRSVAYRAALSGIVTGILLAIARISGETAPLLFTALNNQFWSSNLNAPMASLPVTIFQFALSPYEEWQQLAWTGALIITLTVLALSIFARSLTGRREDK | Function: Part of a binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30059
Sequence Length: 283
Subcellular Location: Cell inner membrane
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Q9PBK1 | MSTASQHLYKRRRLINATAITISCIAALFGLFFLIWILWTLISKGLPGIGLDLFTKITPPPMQKGGLANAFFGSAIMCLLAIVIGTPLGIAAGTWLAEYGNTSKTSAVVRFVNDILLSAPSIVLGLFVYTLYVMHTGGHFSAFSGALALVFIVLPIVVRTTDEMLRLVPGQMREAALSLGIPQWKMIIQVLYRSASAGILTGILLALARISGETAPLLFTAFGNQYWSSNIFQPIASLPLVMNQFASSPYKSWQLLAWSGALVLTVFVLLVSLGARTLLLRNKIPNE | Function: Part of a binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31060
Sequence Length: 287
Subcellular Location: Cell inner membrane
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Q8RCU0 | MEIELKNVNYFRDGKYILKNVYFKFEKNGIYTVVGPSGAGKSTMLKLINRLIEPTEGAIFINGVEYKNIDVILLRRKIGMVFQRPFLFEGTVKENIELGPSLRGEKNIDALFYLEAVGLSKDYLFKDVNNLSGGEAQRVSIARALANSPEVLLLDEPTSSLDPTSTSIIEELIKRLNREGIMVILVTHNMEQAKRIGDYTLFLYKGELIEARKTWEFFENPVSEVSKLFLEGKLKEMIK | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27223
Sequence Length: 239
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q834B4 | MGKEIISSKDLHLYYGKKEALKGIDLTFNQGELTAMIGPSGCGKSTYLRCLNRMNDLIPDVTITGSVVYKGKDIYGPKTDNVELRKEIGMVFQQPNPFPFSVYENVIYGLRLKGVKDKQVLDEAVETSLKAAAVWEDVKDKLHKSALSLSGGQQQRVCIARVLAVEPDIILLDEPTSALDPVSSGKIENMLLTLKEKYTMIMVTHNMSQASRISDKTAFFLQGDLIEFNDTKKVFLNPKEKQTEDYISGKFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28092
Sequence Length: 252
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q9HS13 | MTENTAETADESSDGGVTATTGAATTTPTTPPEPVIRARDLDVFYGSERALESVDIDIPEQQVTAIIGPSGCGKSTFLRCINRMNDRIDAARIDGDLTLRGTNVYDAAVDPVALRRRVGMVFQEPNPFPKSIYDNVAYGLEIQDVEGDHDEIVEQSLRRAALWDEVSHQLDSSGVALSGGQQQRLCIARAIAPDPEVLLMDEPASALDPVATSQVEDLIEELAEEYTVVIVTHNMQQAARISDKTAVFLTGGKLVEFGDTDQIFENPEHQRVEEYITGKFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30596
Sequence Length: 281
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q5FM18 | MMQELKQSYIKTFDKDDVALSTNDLSVLYGGKVQKLFDASLQFKKNTITALIGASGSGKSTFLRSLNRMNDKVATVNGEIWFHGLDVNKPNINVYELRKSIGMVFQRPNPFPKSIRENIVYALKANGKTDKQELDKIVEESLRAAALWDEVKDKLDKSALALSGGQQQRLCIARALAVQPQILLLDEPASALDPVSTSKLEDTLKQLRSKYTMVMVTHNMQQASRISDYTAFFHLGHVIEYNSTAEIFTNPKGKITEDYIQGSFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29642
Sequence Length: 265
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q8NMK1 | MSKLKLNDVNIYYGDFHAVQNVNLEVPARSVTAFIGPSGCGKSTVLRSINRMHEVTPGAYVKGEILLDGENIYGSKIDPVAVRNTIGMVFQKANPFPTMSIEDNVVAGLKLSGEKNKKKLKEVAEKSLRGANLWEEVKDRLDKPGGGLSGGQQQRLCIARAIAVEPEILLMDEPCSALDPISTLAVEDLIHELKEEFTIVIVTHNMQQAARVSDQTAFYSLEATGRPGRLVEIGPTKKIFENPDQKETEDYISGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28213
Sequence Length: 257
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q11NG0 | MKIEANDVHVYYGLDHTLKGVSLSVKKNTVTALIGPSGCGKSTFLRCMNRMNDLIDNCQVKGNILIDGVDINSPSVNTNELRKAVGMVFQKPNPFPKSIFENVAYGLRVNGVSNKEYINDKVEWSLKQAALWDEVKDKLKKSALALSGGQQQRLCIARALAVEPSILLMDEPASALDPISTSKIEELIYNLKASYTIMIVTHNMQQASRTSDKTAFFYMGELVEYDDTRTLFTNPKKKRTQNYITGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27808
Sequence Length: 249
Subcellular Location: Cell inner membrane
EC: 7.3.2.1
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Q3ZA58 | MEPKIKIRGVNFFYHRHQVLKNINMDFPDRQITAIIGPSGCGKSTLLRALNRMNDLVSGARLEGEVLLDNENVYSPNLDVVNLRKRVGMVFQQPNPFPKSIFDNVAFGPRMLGITAQSRLNEIVEKSLHQAALWDEVKDNLHKSGMALSGGQQQRLCIARVLAVEPEVILMDEPCSALDPVSTMRIEELMQELKQNYTIAIVTHNMQQAARASDWTGFLLTGDLIEYGRTGEIFSRPKDKRTEDYITGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28330
Sequence Length: 251
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q9PBK2 | MTSTLIPKETSTPGGRDLRDARADYFFKLLLTAAVAFVLIALVSAALSMLWGGRQALQLQGVSFFYSTEWNPVENKYGALTPIYGTIVTALIAMLIAVPVSFGIAFFLTEVAPRWLRRPVGTAIELLAGIPSIIYGMWGLFVLVPVMTDYITPFLNDHIGTLPLIGTLFQGPPLGIGTLSAGFVLAIMVIPFISSIMREVFLTVPTQLKESAYALGSTKWEVSWNIVLPYTRSAVIGGMFLGLGRALGETMAVAFVIGNSVRLSPSLLTPGTTIAALIANDFGEATESYRSALLLLGFVLFIVTFAVLVIARLMLLRLSRKEGN | Function: Part of a binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34973
Sequence Length: 324
Subcellular Location: Cell inner membrane
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Q8IV42 | MKTAENIRGTGSDGPRKRGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQMSVPPNRTEAMWEDFITCLKDQDLIFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFLDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEASLEVTDLLLTALENPVKYAEDNMEQKDTDRIICSTNILHKTDQTLRRIVSQTMKEAKGNQEAFSEMTFKQRWVRANHAAIWRIILGNEHIKCRSAKVGWLQCCRIEKRPLSTG | Function: Specifically phosphorylates seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis.
Catalytic Activity: ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec)
Sequence Mass (Da): 39527
Sequence Length: 348
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 1/2.
EC: 2.7.1.164
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Q58933 | MLIILTGLPGVGKSTFSKNLAKILSKNNIDVIVLGSDLIRESFPVWKEKYEEFIKKSTYRLIDSALKNYWVIVDDTNYYNSMRRDLINIAKKYNKNYAIIYLKASLDVLIRRNIERGEKIPNEVIKKMYEKFDEPGKKYKWDEPFLIIDTTKDIDFNEIAKKLIEKSKEIPKFYVLEENKNKNNNISDKIDKETRKIVSEYIKSKKLDKDKIKEVVELRKEFLKKIKKMEEVDADRVLKEFKDLLNSY | Function: Specifically phosphorylates seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis.
Catalytic Activity: ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec)
Sequence Mass (Da): 29467
Sequence Length: 248
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 1/2.
EC: 2.7.1.164
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Q8TUS5 | MRLLILTGPPGSGKTCFARELARELRQEGWRVAHVEADALRGFLWDEFDPKLEQVARELFLKSVETCLDAELDLVIADDTNYYSSMRRELALLALERKVPWGIVYLRTGLDTCLRRNRERGEPIPEEVVRRIYDRFEPPEPDRWWERATLVLDDSRVSEEVLEFVESGLRVEKPKKRRRRTDPSSVNEVDVRTRQVMGELMRRLSETGAATQELGRKLSELRREIVSSVEDPEKAVREFRRRAEEVIRECLHGDG | Function: Specifically phosphorylates seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis.
Catalytic Activity: ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec)
Sequence Mass (Da): 29790
Sequence Length: 255
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 1/2.
EC: 2.7.1.164
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Q8BP74 | MKTAAARGATRRDGQPKLGLCVLCGLPAAGKSTFARALALRLRRERGWAVGVLSYDDVLPLALPDCDGTQPRPSQWKMFRQELLKHLECFLVAVISGAQMSAPPNRTEAVWEDFITCLKSQDLMIFPTALEAQPCHLLAKPAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFLDCPLETCLKRNGERSQPLPDETIQLMGRKIEKPNPEKNAWEHNSLIIQSSACSLEASLEVTGLLLTALENPIKCVEDNTEQKETDRIICSTNILHKADETLRRTVSQTMREAKDEQIPLNNLKHLAEELNKLKADVLEDLRQGNRKYLCFQQTTDLSDIISSFCKERDTIVQKYFSKQH | Function: Specifically phosphorylates seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis. No activity with other tRNAs has been detected.
Catalytic Activity: ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec)
Sequence Mass (Da): 40763
Sequence Length: 359
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 1/2.
EC: 2.7.1.164
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P9WHW5 | MARVTLVLRYAARSDRGLVRANNEDSVYAGARLLALADGMGGHAAGEVASQLVIAALAHLDDDEPGGDLLAKLDAAVRAGNSAIAAQVEMEPDLEGMGTTLTAILFAGNRLGLVHIGDSRGYLLRDGELTQITKDDTFVQTLVDEGRITPEEAHSHPQRSLIMRALTGHEVEPTLTMREARAGDRYLLCSDGLSDPVSDETILEALQIPEVAESAHRLIELALRGGGPDNVTVVVADVVDYDYGQTQPILAGAVSGDDDQLTLPNTAAGRASAISQRKEIVKRVPPQADTFSRPRWSGRRLAFVVALVTVLMTAGLLIGRAIIRSNYYVADYAGSVSIMRGIQGSLLGMSLHQPYLMGCLSPRNELSQISYGQSGGPLDCHLMKLEDLRPPERAQVRAGLPAGTLDDAIGQLRELAANSLLPPCPAPRATSPPGRPAPPTTSETTEPNVTSSPASPSPTTSAPAPTGTTPAIPTSASPAAPASPPTPWPVTSSPTMAALPPPPPQPGIDCRAAA | Cofactor: Binds 3 Mn(2+) ions per subunit . The third manganese ion is unlikely to be involved in catalysis but contributes instead to stabilize a flap segment, which is partially disordered in the absence of bound metal .
Function: Plays an important role in regulating cell division and growth by reversible phosphorylation signaling . May play important roles in regulating cellular metabolism and signaling pathways, which could mediate the growth and development of the cell . Plays a role in establishing and maintaining infection . Dephosphorylates several proteins, including the kinases PknA, PknB, PknD, PknE, PknF, PknH, PknJ and Pyk, the transcriptional regulatory proteins EmbR and EthR, the osmosensory protein OprA and the dimycocerosyl transferase PapA5 . In vitro, dephosphorylates the phosphorylated Ser/Thr residues of myelin basic protein (MBP), histone and casein phosphorylated at Ser/Thr residues, but fails to dephosphorylate phosphotyrosine residue of these substrates .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
PTM: Phosphorylated on several threonine residues by PknA and PknB.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 53812
Sequence Length: 514
Subcellular Location: Cell membrane
EC: 3.1.3.16
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A0A0H3M950 | MKIRLHTLLAVLTAAPLLLAAAGCGSKPPSGSPETGAGAGTVATTPASSPVTLAETGSTLLYPLFNLWGPAFHERYPNVTITAQGTGSGAGIAQAAAGTVNIGASDAYLSEGDMAAHKGLMNIALAISAQQVNYNLPGVSEHLKLNGKVLAAMYQGTIKTWDDPQIAALNPGVNLPGTAVVPLHRSDGSGDTFLFTQYLSKQDPEGWGKSPGFGTTVDFPAVPGALGENGNGGMVTGCAETPGCVAYIGISFLDQASQRGLGEAQLGNSSGNFLLPDAQSIQAAAAGFASKTPANQAISMIDGPAPDGYPIINYEYAIVNNRQKDAATAQTLQAFLHWAITDGNKASFLDQAHFQPLPPAVVKLSDALIATISS | Function: Functions in inorganic phosphate uptake, a phosphate-binding protein, although probably not the main uptake protein under phosphate starvation (By similarity). Part of the ABC transporter complex PstSACB involved in phosphate import (Probable).
Location Topology: Lipid-anchor
Sequence Mass (Da): 38215
Sequence Length: 374
Subcellular Location: Cell membrane
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Q97Q31 | MKKRKKLALSLIAFWLTACLVGCASWIDRGESITAVGSTALQPLVEVAADEFGTIHVGKTVNVQGGGSGTGLSQVQSGAVDIGNSDVFAEEKDGIDASALVDHKVAVAGLALIVNKEVDVDNLTTEQLRQIFIGEVTNWKEVGGKDLPISVINRAAGSGSRATFDTVIMEGQSAMQSQEQDSNGAVKSIVSKSPGAISYLSLTYIDDSVKSMKLNGYDLSPENISSNNWPLWSYEHMYTLGQPNELAAEFLNFVLSDETQEGIVKGLKYIPIKEMKVEKDAAGTVTVLEGRQ | Function: Part of the ABC transporter complex PstSACB involved in phosphate import.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31201
Sequence Length: 292
Subcellular Location: Cell membrane
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P75168 | MKKLSGIGVSDGMALAKAFLVKTPEFAVNKYLKHQLTKAQAKRLLDSAFKKAVKDLEEIKEITVNNINTEAGMIFDAHIQMLNDPTITEQLEQQLAQNVHPVIAVDTVFSQTATMFSQMQDKYFQERAADILDLRQRLLAYLTGQKPHDLVKIKSDVIIVAHDLTPSQTATLNKKYVKGFLTEIGGRTSHAAIMARSLEIPAVVGIKGITTKVKDGQIVGVDGRKGIAGLDLNSKDTTEWKKQKALEEKYQQELKQYTNKETVTLDGHAVVVAANIGNVKDMELACQYNTNGVGLFRTEFLYMNSQEWPDEETQYQAYKAVLEQAHGDLVIIRTLDIGGDKKLNYYEFPHEDNPFLGYRALRLTLDKQDIFKTQLRALLRAADHGQLGIMFPMVATLDELLQAKQLLNQVHQELGGNKQFKLGIMIEIPAAVLAANTLSHHVDFFSIGTNDLIQYSFAADRMNKNVSYLYQPLNPALLKLIYLTIEGGKVNDIWTGMCGEMAGEPLAIPLLLGLGLKEFSMSASSMFKARMIIAKLNYTECQTLAQKALTLANAKEVEKLVEKFFKKKDIFI | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 63950
Sequence Length: 572
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
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P23533 | MAKQIKGIAASDGVAIAKAYLLVEPDLSFDNESVTDTDAEVAKFNGALNKSKVELTKIRNNAEKQLGADKAAIFDAHLLVLEDPELIQPIEDKIKNESVNAAQALTDVSNQFITIFESMDNEYMAERAADIRDVSKRVLAHILGVELPNPSIVDESVVIIGNDLTPSDTAQLNKEYVQGFVTNIGGRTSHSAIMSRSLEIPAVVGTKSITEEVEAGDTIVVDGMTGDVLINPSDEVIAEYQEKRENFFKDKQELQKLRDAESVTADGHHVELAANIGTPNDLPGVIENGAEGIGLYRTEFLYMGRDQMPTEEEQFEAYKAVLEAMKGKRVVVRTLDIGGDKELPYLDLPEEMNPFLGYRAIRLCLDQPEIFRPQLRALLRASVFGKLNIMFPMVATIQEFRDAKALLEEERANLKNEGYEVADDIELGIMVEIPSTAALADIFAKEVDFFSIGTNDLIQYTMAADRMSERVSYLYQPYNPAILRLVKQVIEASHAEGKWTGMCGEMAGDQTAIPLLLGLGLDEFSMSATSILKARRLIRSLNESEMKELSERAVQCATSEEVVDLVEEYTKNA | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 63299
Sequence Length: 573
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
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Q9KZP1 | METTLRGVGVSHGVAIGEVRHMGTAVLEPPAKQIPAEDAEREQGRARKAVEAVAADLMARGNLAGGEAQAVLEAQAMMAQDPELLADVERRITVGSTAERAVYDAFAAYRALLAGAGEYLAGRVADLDDVRNRIVARLLGVPMPGVPDSDEPYVLIARDLAPADTALLDPTLVLGFVTEEGGPTSHSAILARALGVPAVVALPGAGEIPEGTVVAVDGSTGEIFVNPAEEKKARLAAEAAERKAALAAATGPGATSDGHKVPLLANIGGPADVPAAVEAGAEGVGLFRTEFLFLDDSANAPSEEKQITAYRQVLEAFPEGRVVVRVLDAGADKPLDFLTPGDEPNPALGVRGLRTLLDHPDVLRTQLTALAKAAEGLPVYLEVMAPMVADRADAKAFADACREAGLRAKFGAMVEIPSAALRARSVLQEVEFLSLGTNDLAQYTFAADRQVGAVSRLQDPWQPALLDLVALSAEAAKAEGKSCGVCGEAAADPLLACVLTGLGVTSLSMGAASLPYVRATLAKFTLAQCERAAAAARAADSAEEARTAAQAVLSGE | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 57272
Sequence Length: 556
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
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Q0VCS0 | MAESWLLLLLALGCPALPTEVTTLLRPAQQGMGSTPFPSLAPPITLLVDGKQQTLVVCLVLDVAPPGFESPIWFSAGNGSSLDAFTYGPSPAEDGTWTRLAQLSLYSEELAAWDTLVCHTGPGAGDHGQSTQPLQLSGDASSARTCLWEPLRGTRALVLRLGALRLLLFKLLLLDVLLTCGRLHAPPAARGDPAGASGPGAPSLPAPHEVPRADSRLLPQPPPPRGSSSGPADRIRRNHGGTTGRGLSVSASPPLEPRDRRRRVHTRRPRRDPRNPVWEEGPPVLRAWSSGPSFSLSTSSLGAFLCNLPPPADPSFPGG | Function: The pre-T-cell receptor complex (composed of PTCRA, TCRB and the CD3 complex) regulates early T-cell development.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 33670
Sequence Length: 319
Subcellular Location: Membrane
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Q6ISU1 | MAGTWLLLLLALGCPALPTGVGGTPFPSLAPPIMLLVDGKQQMVVVCLVLDVAPPGLDSPIWFSAGNGSALDAFTYGPSPATDGTWTNLAHLSLPSEELASWEPLVCHTGPGAEGHSRSTQPMHLSGEASTARTCPQEPLRGTPGGALWLGVLRLLLFKLLLFDLLLTCSCLCDPAGPLPSPATTTRLRALGSHRLHPATETGGREATSSPRPQPRDRRWGDTPPGRKPGSPVWGEGSYLSSYPTCPAQAWCSRSALRAPSSSLGAFFAGDLPPPLQAGAA | Function: The pre-T-cell receptor complex (composed of PTCRA, TCRB and the CD3 complex) regulates early T-cell development.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29266
Sequence Length: 281
Subcellular Location: Membrane
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P0C6B2 | MARTWLLLLLGVRCQALPSGIAGTPFPSLAPPITLLVDGRQHMLVVCLVLDAAPPGLDNPVWFSAGNGSALDAFTYGPSLAPDGTWTSLAQLSLPSEELEAWEPLVCHTRPGAGGQNRSTHPLQLSGESSTARSCFPEPLGGTQRQVLWLSLLRLLLFKLLLLDVLLTCSHLRLHVLAGQHLQPPPSRKSLPPTHRIWT | Function: The pre-T-cell receptor complex (composed of PTCRA, TCRB and the CD3 complex) regulates early T-cell development. Isoform 1 acts to retain most TCRB intracellularly, while isoform 2 permits higher levels of cell surface TCRB expression and facilitates signaling from the CD3-TCRB complex.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 21491
Sequence Length: 199
Subcellular Location: Membrane
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Q837U7 | MKRDYVTTETYTKEEMHYLVDLSLKIKEAIKNGYYPQLLKNKSLGMIFQQSSTRTRVSFETAMEQLGGHGEYLAPGQIQLGGHETIEDTSRVLSRLVDILMARVERHHSIVDLANCATIPVINGMSDYNHPTQELGDLCTMVEHLPEGKKLEDCKVVFVGDATQVCFSLGLITTKMGMNFVHFGPEGFQLNEEHQAKLAKNCEVSGGSFLVTDDASSVEGADFLYTDVWYGLYEAELSEEERMKVFYPKYQVNQEMMDRAGANCKFMHCLPATRGEEVTDEVIDGKNSICFDEAENRLTSIRGLLVYLMNDYEAKNPYDLIKQAEAKKELEVFLDTQSI | Function: Catalyzes the phosphorolysis of N-carbamoylputrescine to form carbamoyl phosphate and putrescine. Is involved in the degradation pathway of the polyamine agmatine. Also has weak activity with ornithine and cadaverine.
Catalytic Activity: carbamoyl phosphate + putrescine = H(+) + N-carbamoylputrescine + phosphate
Sequence Mass (Da): 38343
Sequence Length: 339
Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from N-carbamoylputrescine (transferase route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.6
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Q6MSR6 | MNKVRHFIDTQDLSKKEIFEIFRLMKMLKEARYCGAVPELLKNKTLAMIFEEPSTRTRVSFEAAMTLLGGHAQYLKPGELHLGVRESLYDTTKVLSHMCDGIMCRALKNETVLNLAKYADVPVLNGLTDYNHPTQAICDVFTMLEYMPATKNLEYEDIKFEDIKVVFIGDRTNVCSSTMHITTKLGMNFVHISPKRYQSPQEWIDIANENIKQANSGSVLVTDDLEQVRGADIVYTDLWWWVDQEDEAEERVKAFKPTYQVTPELMEKAGKQALFMHCLPASRNVEVYDEVIDSDQSIAFEQAENRLTAQMGLLVYYLYPQIDKSSNAVKDYYRGKVEAFMEHQDRSWKQRYTYNNDYAETKNKK | Function: Catalyzes the phosphorolysis of N-carbamoylputrescine to form carbamoyl phosphate and putrescine. Is involved in the degradation pathway of the polyamine agmatine.
Catalytic Activity: carbamoyl phosphate + putrescine = H(+) + N-carbamoylputrescine + phosphate
Sequence Mass (Da): 42280
Sequence Length: 365
Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from N-carbamoylputrescine (transferase route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.6
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C0HLE0 | GLVSGLLNSVTGLLGNLAGGGL | Function: Has no antimicrobial activity against Gram-negative bacterium E.coli ATCC 25922, Gram-positive bacterium S.epidermidis ATCC 12228 and against fungus C.albicans ATCC 24433 at concentrations up to 100 uM . Has an anti-inflammatory effect, since it inhibits the production of the pro-inflammatory cytokines TNF-alpha and IL-1 beta . Has high activity of stimulation of insulin release, which may protect the species from being eaten by predators by causing fatal hypoglycemia . Is not cytotoxic to cancer line cells . Does not show hemolysis on mouse erythrocytes . Adopts a mixture of alpha-helical and beta-sheet structures .
Sequence Mass (Da): 1982
Sequence Length: 22
Domain: Plasticins have huge conformational plasticity. They can display random coil, alpha-helical, beta-sheet or beta-harpin structures.
Subcellular Location: Secreted
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Q9JM51 | MPSPGLVMESGQVLPAFLLCSTLLVIKMYAVAVITGQMRLRKKAFANPEDALKRGGLQYYRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPLIAWIHFLVVLTGRVVHTVAYLGKLNPRLRSGAYVLAQFSCFSMALQILWEVAHHL | Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway . Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli . Plays a key role in inflammation response, fever and pain . Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity).
Catalytic Activity: prostaglandin H2 = prostaglandin E2
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17286
Sequence Length: 153
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subcellular Location: Membrane
EC: 5.3.99.3
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F1RE08 | MMWTALLLVGLSILVIVLYGRRTRRRNEPPLDKGMIPWLGHALEFGKDAAKFLTRMKEKHGDIFTVRAAGLYITVLLDSNCYDAVLSDVASLDQTSYAQVLMKRIFNMILPSHNPESEKKRAEMHFQGASLTQLSNSMQNNLRLLMTPSEMGLKTSEWKKDGLFNLCYSLLFKTGYLTVFGAENNDSAALTQIYEEFRRFDKLLPKLARTTINKEEKQIASAAREKLWKWLTPSGLDRKPREQSWLGSYVKQLQDEGIDAEMQRRAMLLQLWVTQGNAGPAAFWVMGYLLTHPEALRAVREEIQGGKHLRLEERQKNTPVFDSVLWETLRLTAAALITRDVTQDKKIRLSNGQEYHLRRGDRLCVFPFISPQMDPQIHQQPEMFQFDRFLNADRTEKKDFFKNGARVKYPSVPWGTEDNLCPGRHFAVHAIKELVFTILTRFDVELCDKNATVPLVDPSRYGFGILQPAGDLEIRYRIRF | Function: Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2).
Catalytic Activity: prostaglandin H2 = prostaglandin I2
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55308
Sequence Length: 480
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.3.99.4
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Q16647 | MAWAALLGLLAALLLLLLLSRRRTRRPGEPPLDLGSIPWLGYALDFGKDAASFLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKARMKLTLLHRELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLDRLLPKLARGSLSVGDKDHMCSVKSRLWKLLSPARLARRAHRSKWLESYLLHLEEMGVSEEMQARALVLQLWATQGNMGPAAFWLLLFLLKNPEALAAVRGELESILWQAEQPVSQTTTLPQKVLDSTPVLDSVLSESLRLTAAPFITREVVVDLAMPMADGREFNLRRGDRLLLFPFLSPQRDPEIYTDPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNMPWGAGHNHCLGRSYAVNSIKQFVFLVLVHLDLELINADVEIPEFDLSRYGFGLMQPEHDVPVRYRIRP | Function: Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation . Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) .
Catalytic Activity: prostaglandin H2 = prostaglandin I2
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57104
Sequence Length: 500
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.3.99.4
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Q9EQZ5 | MVKAKSWTLKKHFQGKPTQSDFELKTVELPPLKNGEVLLEALFLSVDPYMRIASKRLKEGAVMMGQQVARVVESKNSAFPAGSIVLAQSGWTTHFISDGKGLEKLLTEWPDKLPLSLALGTIGMPGLTAYFGLLEVCGVKGGETVLVSAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKIAYLKQIGFDAAFNYKTVNSLEEALKKASPDGYDCYFDNVGGEFLNTVLSQMKDFGKIAICGAISVYNRMDQLPPGPSPESIIYKQLRIEGFIVYRWQGDVREKALRDLMKWVLEGKIQYHEHVTKGFENMPAAFIEMLNGANLGKAVVTA | Function: NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX) . Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha (By similarity). Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites (By similarity). Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the inflammatory site (By similarity). Plays a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one (By similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity).
Catalytic Activity: 13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH
Sequence Mass (Da): 35730
Sequence Length: 329
Subcellular Location: Cytoplasm
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Q14914 | MVRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEGDTMMGQQVAKVVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTGPLPPGPPPEIVIYQELRMEAFVVYRWQGDARQKALKDLLKWVLEGKIQYKEYIIEGFENMPAAFMGMLKGDNLGKTIVKA | Function: NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX) . Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha . Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites (By similarity). Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the inflammatory site (By similarity). May play a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one . May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity).
Catalytic Activity: 13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH
Sequence Mass (Da): 35870
Sequence Length: 329
Subcellular Location: Cytoplasm
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Q29073 | MVRAKSWTLKKHFVGYPTPSNFELKTVELPPLKNGEVLLEALFLTVDPYMRIAARKLKEGDMMMGEQVARVIESKNAAFPTGTIVVALLGWTTHSISDGKNLERLLAEWPDTLPLSLTLGTVGMPGLTAYFGLLDICGLKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVACLKKYGFDVAFNYKTIESLEETLKKASPEGYDCYFDNVGGEFSNAVTSQMKKFGRIAICGAISTYNRTGPPPPGPPPEVVIYNELCFQGFIVTRWQGEVRQKALRDLLKWVSEGKIQYHEHITEGFENMPAAFMGMLKGENLGKAIVKA | Function: NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX) . Preferentially uses NADPH over NADH as cofactor . Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha . Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites . Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4 and may promote neutrophil recruitment at the inflammatory site . Plays a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one (By similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity).
Catalytic Activity: 13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH
Sequence Mass (Da): 35762
Sequence Length: 329
Subcellular Location: Cytoplasm
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Q8N8N7 | MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIGIIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGIQEKGHITAGSNKTMVVSGAAGACGSVAGQIGHFLGCSRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISQYNKDVPYPPPLSPAIEAIQKERNITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIVCISEEISL | Function: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest activity towards 15-keto-PGE2 . Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation (By similarity).
Catalytic Activity: 13,14-dihydro-15-oxo-prostaglandin E2 + NAD(+) = 15-oxoprostaglandin E2 + H(+) + NADH
Sequence Mass (Da): 38499
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 1.3.1.48
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Q8VDQ1 | MIIQRVVLNSRPGKNGNPVAENFRVEEFSLPDALNEGQVQVRTLYLSVDPYMRCKMNEDTGTDYLAPWQLAQVADGGGIGVVEESKHQKLTKGDFVTSFYWPWQTKAILDGNGLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGVQEKGHISAGSNQTMVVSGAAGACGSLAGQIGHLLGCSRVVGICGTQEKCLFLTSELGFDAAVNYKTGNVAEQLREACPGGVDVYFDNVGGDISNAVISQMNENSHIILCGQISQYSNDVPYPPPLPPAVEAIRKERNITRERFTVLNYKDKFEPGILQLSQWFKEGKLKVKETMAKGLENMGVAFQSMMTGGNVGKQIVCISEDSSL | Function: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation.
Catalytic Activity: 13,14-dihydro-15-oxo-prostaglandin E2 + NAD(+) = 15-oxoprostaglandin E2 + H(+) + NADH
Sequence Mass (Da): 38015
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 1.3.1.48
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Q24K16 | MQRLALAGTRAIVDMSYARHFLDFQGSAIPSKMQKLVVTRLSPNFREAVTLRRDCPVPLPGDGDLLVRNRFVGVNASDINYSAGRYDPSVKTPFDAGFEGVGEVVALGLSASAAFMVGQAVAYMAPGSFAEYTVVPARVAIPVPGLKPEYLTLLVSGTTAYISLKELGGLSEGKKVLVTAAAGGTGQFAVQLAKKAKCHVIGTCSSAEKSAFLKSVGCDRPINYNTEHVGTVLRQEYPQGVDVVYESVGGAMFDLAVDALATRGRLIVIGFVSGYQTPTGLSPVKAGTLPAKLLKKSASVQGFFLNHYLPEFRGAMDHLLKMYAGGELVCEVDTGGLSAEGRFTGLESVFRAVDYMYMRKNTGKIVVELPPSVNSKL | Function: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest efficiency towards 15-keto-PGE2-alpha. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation.
Catalytic Activity: 13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-oxoprostaglandin E2 + H(+) + NADPH
Sequence Mass (Da): 40119
Sequence Length: 377
Subcellular Location: Peroxisome
EC: 1.3.1.48
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B0TZF5 | MPKIKMIVGLGNIGKEYENTRHNVGEWFIAKIAKDNNENFSLNSKLNCNIAKVNINYNNIILVFPTTFMNNSGLAVSKVANFYKIEPEEILVVHDELDIDSGEIRLKKGGGHGGHNGLRSIHQHLGTNDYLRLRIGIGHPGHKSKVSNYVLSNPSVAQKNDIDNAIDNGICVLDDIINYKLEPAMQRLHTK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21311
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q8RIJ5 | MKVVIGLGNPGKKYEKTRHNIGFIAVDNLRKKFNISDEREKFQALVSEKNIDGEKVIFFKPQTFMNLSGNSVIEIINFYKLDPKKDIIVIYDDMDLSFGDIRIREKGSSGGHNGIKSIISHIGEEFIRIKCGIGAKERDAVEHVLGEFNQTEQKDLDEILEKINNCVIEMLSVQNLDRIMQKYNKKKEISK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21906
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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C1A7P9 | MKVIVGLGNPGREYENTRHNVGWWLIDTLKERWHFEPWRKDGDAVSTTGLVGTKKVKLVKPQTYMNLSGSVLRPYLKREGWTAAQDLMVLVDEVAVPVGEYRLRAAGSPGGHNGLKSIEAHLKSPTYPRLRVGIKPVDERRQIGDLADFVLHTMPRDERALVDDITPRMIDAIELWIAEGTEKAVSSMGR | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21367
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q5L3U7 | MKLFVGLGNPGKEYEQTRHNVGFFVIDELAKRWNVSLKTAKFRGLFGTASVSGEKVALCKPLTYMNLSGECVRPLMDYYDIAIDDVIVIYDDLDLPPGKIRLRLKGSSGGHNGVKSLIHHLGTEQFKRIRIGIGRPAGGQPVTDYVLGRFTEEEKPAVDKAVLRAADACEQAVKAPFIQVMNDFNE | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20598
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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A2BUN1 | MKDNEVFIIGLGNPGKQYIKSRHNIGFLLLETFSKKYDAQFTLKNKLKSRYTEFKINDSIYKLFMPHTYMNNSGDAVKAIVDWYKISLDKVFIIVDDIDLPLGKIRFRKKGSSGGHNGLKDIINKLQTENFNRIKIGIGSPPINETKKQLNTISHVLGNISSQENSTLEKVYQKVIESLEELDIKNEDYIISELNSFHK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 22873
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q7VDT7 | MSSGNFQLLAGLGNPGSKYTSTRHNVGFMALERLAKKESVQFAMNKKIFGHIANIEIGANKRKLLMPNTYMNESGRSISAAIKWFDLEINQILIFVDDMDLPLGKLRFREGGGSGGHNGLKDIIKHLGSQDFCRLRIGIGPPSINQGDRKQKTIPHVLGKFDQAESKVITKVLDKVIKGLEVIEQYGLVKGTSFLNSSLTATDG | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 22373
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q15SQ2 | MSNIQLIVGLGNPGLEYKYTRHNAGTWLVENLARMHNCTLSLQSKFFGYTGRVTIGGQDIRLLIPTTYMNKSGQAVAALAGFYRIPPESILVAYDELDLPPGIAKFKLGGSSSQNGIRDIVSSLGNNKDFYRLRVGIGHPGHKGKVSGYVLGKAPAKEQEQMDAAIDEGVRCIEILIKDDMKKAMNRLHSFKAE | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21283
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B5ZAQ7 | MEKYLIVGLGNPGSNYAKTRHNAGFMVINEICNKLNLFLDNSKFNGMFAKTIYNNCVVFFCQPTTYMNLSGEFVSKMLKFYDIPIKNLIVIYDDVDTKLGVIKLRKKGSSGGQNGIKNIINLLKTEEIKRIRVGIGKDPHAKLDQYVLSNFKIDELVIIKPAIIKGALAALEAIGEDFDKVMNKFN | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20904
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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A5CVE8 | MTIKLIVGLGNPGKNYKYHRHNVGFWFCDALAKLYAGNFKKRTKFFGEVTQINIFNHKIQLLKPTTFMNCSGQSIQSIANFYQINADEILIVHDELNINPGIAKIKSGGSHGGHNGLKNTIKILETKAFYRLRIGIGHPGNKLPIVDFVLNTPSKDELDKIQNALNNSLQVIEDVIKNNLDKVIKTLQKKEII | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21725
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q8D2K4 | MKLKLIVGLSNPINLYYNTRHNIGSWYIKFLAKKYKKNLIKNKKYCFYYIDVKIGDYYSKLVIPDTYMNVNGTIIYNITNFYKIYSNEMLIVHDDLDLDTGIARFKFNHKNSTHNGIKSIYKSFGAKCIFNTLRIGIGRPKLNKNINSYLLNNPSPKEEILIKKTITKCIKCTDVLIKKNKDHAMNILHKK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 22384
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q7M7U8 | MVLVVGLGNPGKTYESTRHNIGFRVIDALLERRSALNATKSTFKGELHKEGENLFLKPTTYMNLSGESALPVSTFYKPEKILVIHDDLDLPFGAIRLKRGGGNGGHNGLKSLDKLLGNDYYRLRIGIGKPPLGWEVADYVLARFSQEEEQELEERLFPHAKEAIESFLEGKMEWDRLVSRYSLKPSTPKEKV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21645
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q5GTI9 | MHLIVGLGNPGSQYELTYHNIGFIIVDAICKHWNFQSFSKKADCLITSSVINDNKIMLMKPYSFMNNSGIPVARIRNFYKFSLDNVIVIHDDADLEPGRIKIKKGGGSAGHNGLKSIDSSIGNDYWRLRFGIGRSDSQRSLADYVLSKFSNLDDVIPLVERIAQNIHLMLQGNNIAFTNSIV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20347
Sequence Length: 182
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q9KJ75 | MERKSSLKVRVQKLGTSLSNMVMPNIGAFIAWGVAASLFIATGYLPNKALDTNVVGPMLKYVLPLLIGYTGGYNIHKQRGGVIGAIASFGAIAGSTVTMFIGAMIMGPLSAWILKKFDEKVQPKIRTGFEMLVNNFSLGLIGFALMVLAFFVIGPVVAQLTEWVGIGVEAIVKVHLLPLANLIIEPAKILFLNNALNHGIFTPLGTEQVAKVGKSVLFLLEANPGPGLGVLIAYAMFGKGSAKSSSWGAMIIHFFGGIHEIYFPYVMMKPAMFLAVIAGGLTGTFTFQTLGAGLTAPASPGSIIAIMGMSPKGWGPHLVVLAGVFAAAVASFLVASIILKSDNSDDDSLETAQAVTQAAKAESKGQAVTEPNLHSDITTDNIHQIIFACDAGMGSSAMGASILRDKVKKAGLDISVSNQAISNLQDTANTLIVTQEELADRAGQKTPRAVHVAVDNFLATSKYDDIIASLTNGKASGSENAAHSTQADSAEIDLNQIDAVVFAYGIAKGSATMGQETLRSIFKQNNVKIPVSTASYAHLSDYNAKNILLVTTIAQQGQAQQAAPNAQILVVDSLVTTPEYDKLVARMHK | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
Catalytic Activity: D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannitol 1-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62035
Sequence Length: 589
Domain: The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell membrane
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Q97SH4 | MEEKVSLKVRVQKLGTSLSNMVMPNIGAFIAWGVLTALFIADGYLPNEQLATVVGPMLTYLLPILIGYTGGYMIHGQRGAVVGAIATVGAITGSSVPMFIGAMVMGPLGGWTIKKFDEKFQEKIRPGFEMLVNNFSAGLVGFALLLLAFYAIGPVVSTLTGAVGNGVEAIVNARLLPMANIIIEPAKVLFLNNALNHGIFTPLGVEQVAQAGKSILFLLEANPGPGLGILLAYAVFGKGSAKSSSWGAMVIHFFGGIHEIYFPYVMMKPTLFLAAMAGGISGTFTFQLLDAGLKSPASPGSIIAIIATAPKGVWPHLNVLLGVLVAAVVSFLVAALILHADKSTEDSLEAAQAATQAAKAQSKGQLVSTSVDAVVSTDSVEKIIFACDAGMGSSAMGASILRDKVKKAGLEIPVSNQAISNLLDTPKTLIVTQEELTPRAKDKSPSAIHVSVDNFLASSRYDEIVASLTGASPIAEIEGDIPTSAPVDSQESDLNHIDAVVVAYGKAQGTATMGCETIRAIFRNKNIRIPVSTAKISELGEFNSKNIMIVTTISLQAEVQQAAPNSQFLIVDSLVTTPEYDKMAARMYK | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
Catalytic Activity: D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannitol 1-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61855
Sequence Length: 589
Domain: The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell membrane
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A0A140JWT3 | MTTMLTTPLSGWSQLSLSFLTLTVGALALIVVLYISIDRFPAPRWLSKKYQLIGQKDPASTTSLECPYSYIRQIYGHYHWAPFVHKLSPTLQYDDPAKYKMVLEIMDAIHLCLMLVDDISDGSDFRKGRPAAHRIYGPSETANRAYLRVTQILNQTTSGFPHLAPWLMRDLENILEGQDLSLVWRRDGLKNFPTAPLERAAAYQRMASLKTGSLFRLLGHLVLEDRSMDDTMTLVAWYSQLQNDCKNVYSTEYAKMKGAIAEDLSNGELSYPIVLAMNAPDGHWVDLALQSPSPWNVRNALRVIRSDKVHQMCMAEMAESSSSIQDWLALWGRKEKLDLKSV | Function: Prenyl transferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 38790
Sequence Length: 342
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 2.5.1.-
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A0A140JWS2 | MLFLAPGYIFPHVATPVTVAIDFAQAVKEGAYSFLDLKASPVPNPELFQPPSRVSIGMTGGREERNEEIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLSTIKEIIVILHTASLLIDDIQDSSQLRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSSFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDQQLIQILKLKTNDEVIKQYAVRYIESTGSFIYCREKLDLYLQEANETFQGLELLLGPSKGIRAILNFLRTR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 40178
Sequence Length: 356
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
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A0A140JWT8 | MMRDSLGPFRTFTLLTVGLLLSLFVIKTVKHRRRYHGLPTPPHNMLLGNLGVVLAEILASPEGFFHLFCVENIRRKYNMPSVFYLDLWPILPSIMVVAEPVVAKHMTQVQPLQRERFSPNLFSPLLTAEFILAMEQKNWKKENPALNAALTSTRVNEATSLLFPSLHSLRSRLHSISQSGKQYPIKDLLISYIIEVGGVIQLGGSFDLLAETSALDPIIKQSLDMMGWNPVKRYICSKEIKQRTDCLNRVLVATVQNTVQTGESGMMSQSPIYLAHVEQLASGRMDHAESIAYLVNTMKVIILASVVTAGAASYCYLFLHKYPDCLREMREEHDRVFSPDRTQTWELLQKEPHRINSLHFTLAVVKETLRLIGVGGVFKKLKTEEFLETEGNVYPVVCNVAFICHLAMGRRADLFPDPDAFRPHRFLPGANPPIPADSFRPFEKGQLSCPGQTLALKSLVLLLLTTSREFDLVPVFPKGAPRAAEYLGGEGYPEFHIGPHVNKGMPVMVHTRVDA | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57838
Sequence Length: 515
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A140JWU1 | MAIPKTMEAPFTHLFLNLTVMTLGQILVIPVALLVVYICIRIGSIRRQFRDLPKPPHHAFLGHFPILLRELRTLPRDIFAPLVVDLVRRKFDLPAVFFLDLYPLFNPIVFISDPGLARKITQEDRSLRYPGVFETLYPAIPTRWFRTVADRAWTKWHPVVGVSFTAAHFVRMVPQMAEDLRAMLDQLNDWSDRDEIFCMERVATDAILAMTGRAYFGMELDCFAPKSQWTSAFRAATTPVVAARNPLRKPFVLPSWKRHARTFHAVIREKVQHTFDKDENHEAGVPSLLASSFAVYRKNGFPEFPRVSQEALSTEYLEELTSTGAAFLIGATSGASVISYAFLLLHQHPNILDDLRREHGQVCGFNRQSILLALQSRPRLLNDLKLTHAVLKETLRLFPMGPVLRKCPSETMEYEGRTYDIRNHIVAISHNSLHRRPDLFPNPDAFNPYRFLPGAAIPIPADAWRPFEKGNGYCVGQELAMIQMKVMLLLTLTEFDFQPKYAREAARGPDIYGGYAYTTGSGIGPTPAGGLPMRVDKRMK | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61327
Sequence Length: 540
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A140JWS7 | MKVAVIGGGPSGLVTLKYLLAAHHFQPVDPIEVQLFESEDRVGGTFSYRTYDRAELVSSAQLTTFSDYRWHDKSVDYLSAAEYVEYLEGYCDRFGLWPHIRLSTQVEKVERTGKGKHRITVSHDGQTSTWDCDAVAVCSGLHVKPNIPSIPGLDRVPVVFHSSEYKHVRQLGQNTNVMVLGTGETGMDIAYFSVTADSTKSTTVCHRNGFVIGPKRLPEIKLFGRVTSKTPGKALPVDLSRPYLFVNSYVHRKVRGTLQTTLSRWTVKAGSWLVTGTTRGFDQWVGSLPKDKYDESHYFYCKSTKAMPYISAPYRSHSWVHRLRSSIIQAVLPDTGSRKIDLAPWPEYIDEDGVVHFEKNSHPDSKVLLQERRFRPDVLVLATGYTQSFPFLGSDYCTPDHADQRGIWRTGDESVGYIGFVRPSFGAIPPLAEMQVQVWVLNLINRLPGPLVADDSYRLFSNPSGRIEYGVDHDMFAHRLALDIGAAPSFFQALAHGWQVTVFWAMGGTLNTKFRLVGPWAWSGAPRIICDELLDTVTGRRSTIELLTQLIMTAIVCGIPSILLFLADLLVALSIRIYQAISVVSSRPSKGDSAVTENRG | Function: Monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
Sequence Mass (Da): 66951
Sequence Length: 600
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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A0A140JWT7 | MKHNLPADLVTLWRDSPGYESARSRTFNQRIPPELPYAIVRPKNMEQIQHAVQLAVDLDKQIRIRSGGHSLAGWTLCADSILIDLVDFRHLEYDATTAIASASPSATSAQLNDLLVPHGRFVPVGHCGDVGLGGFFLQGGMGLNCRSYGWACEYLVGVDLITADGEYKHCSESENADLFWAARGAGPEFPAIVTRFFIRTRPAAAKYEKSTFIWPVACSDAVVSWILKILPELHADIEPLVVSTIVPGLNVAAILVQFLVFLSTNETGAEKLGPSLTAMPDGTLMEFKGVPTSIQQEYVSQEGTMPRDSRYICDSVWFKDGIDFVTVTRRMFREFPRDRSMVYWEPKYPTSRRQLPDMAFSLQADQYLALFAIFEDSQQDEEQGIRIQEFIQEIEPYVLGTFAADGMPAVRKTQYWSAEVIERLYSVCQKWDPAHRLGCTLLDPTRKVKS | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
Sequence Mass (Da): 50474
Sequence Length: 450
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.1.-
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Q39491 | MTSHAANPKEEQDQRLPFKSDISGPIAPSQAPAHTVQAHDSQPKPSDDSSDEHLSFYEAKARIVRAFAASRAPQPAAPAAKALEGDASVIVPGKLILSSCEVEESSELLTKLGVTHILQVGEELKPSHPGRFTYLSLPILDMEGQDIVALLPSCFQFLQQAQASGGVCLVHCLAGISRSASVVIAYLMWTQGMPYTEARAMVRRARSKVYPNTGFTLQLQELDRLRESGAIQWGDTPSLASSLEQHRQPWNLIRYLEVKEKQAQEEGWTWGRTLVI | Function: Could be involved in tyrosine phosphatase signalling pathways, having MAP-kinases as substrates.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 30310
Sequence Length: 276
EC: 3.1.3.16
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P54637 | MISSSMSYRHSTNSVYTLNPHLNIPISTSTTIPPTSFYANNTPEMIQSQSENTNTNNINNSSSNINNNNNNTPDSMSMSTSLSSSPSVSFNHLDLNSINNKINNNTTTNNNNNNNNNNDDKFDTNALKLSNTMIIKNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNSNIEINVPSIQFDNEPAMEVDSVAPLNVPSNHTRTTLAMHNTKSLSTSNIGLLNILPNQQSSSSSSLSSTTTTTTTTSSSLLMPQSLFNNSTYNNHHNNNNSSNAGIVGGLNGSTSSLPTQAQVQLQQMQQQMQQHQQHQYKKANLSSLSTVVDNNLNNNPMNTSTSSPAQPNASPFSFSSSSLFSNSSLSNSGSGSASTTSTSTSSSNSMSSSPPPSLKTSFSQLDEDREKMRLEFEMIKKPEMASKKSHKHHQRHYSHNDLDNRKHDEEKFFSALQPNNYGKNRYHDVLPNESTRVRLTPIESGDGDYINANYINGEVPNSYRYYIACQAPLPSTIKDFWRMVWEERSSVIVCLTKLEENGKKKADVYYPETSQAQEYGSFWIHLHKKVMFKDIGVSSLHLYKKGEEFPREVVLLHYTQWPDCGAPPSSSHIRTLSVMVNTFKARGSAKNTNGPVIVHCSAGIGRSGTFISININMAKIERFGNDPSQMNISIKDSVLELRRQRRGMVQTLDQYIFIFKVINDVLTDMGIRSLSSPSKRRSCEMIKSTPMPRLDISIPPPLTFTPKDFQSSISPSTDMIASLSIITQMTQTLKFPPQQQQDNPFSKSSIKISPSPLNSTNISIPKNQQFQHPFQIQPQLDLNLQQQQQQSSQQLNDNPPLNMSSNSIKFPPVTSLSSCHLFEDSKNNDNNNKQQQQQQQQQQKNNQQCSGFSHFLNNNNNNDNNGSSGGGFNGSFLFNSNNSGSSSTNSECSNNNKNNNNNSNNNNNNNNNKNSDNNGTKDKDENDSCESPRVTPIKCF | Function: Seems to dephosphorylate a protein of 130 kDa (p130).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 110110
Sequence Length: 990
Subcellular Location: Cytoplasm
EC: 3.1.3.48
|
P40048 | MKDSVDCPSILPTDRTSVLSETSTLVGSSSHVYSRHAPMNSYHNSMNSNIYHSPKASSPLVSYKTSSPVLLKRATAPVLPSFKPKEQRYNKPQGCSLITAVELGKIIETLPDEKVLLLDVRPFTEHAKSIITNSIHVCLPSTLLRRKNFTFSKLLDNLTPSEQSVLKSKLAIDNLRIIIYDSTANQTESSVSLPCYGIASKLIEFDTNVKKTVSILMCGFPQFKILFPDHINTNTFNSDCISSAEPKSPKTNLMNSLHNTAPHMTATTPLSSPQMNLKLKVPDDSRSDHSNFSSSPSPRNVLSDSPMSSSSPISALFKFQLPAPQTNINQMFKFSQNEEIMGLETYLSAVNIKEEHERWYNNDSAKKSLQNFQFPKNQNSLEKDTNKDKLGFQIRYENLSKNYEKEVIDSVIPEWFQHLMSIPKIELVSQFQKLDFLEKRRLNHSVSFRKKENSFILEKPSSYPEQLTSTSSSTIMPPKFPDVNKVQKRSHSQPIFTQYSKYKSMLSLESDSDSESDDVIISSGVELGAKNRYKDIFPYEHSRVILKKGLQSSKGIKHSHSTSDGGILDNYINANYLSLPRFSVEQNSSFQTTTTTTRRVRYIATQAPMPSTVHDFYTCILNNGVPLVLSLTNDFENGIEKCYRYWQEGNYNGIHVKLLEKKILKMPSTTSMRKNTMGTQNSSLYSAGVQGNSSNYSTDNDNDNDNNNNNNNNSNIAVTAAACDDDDDDDDDAILIRKILLTYHDQEKPYELLQIQVKNWPDLGTLLNPISILQAINVKNHIIDTLFARNYYQNDQLPTILVHCSAGCGRTGTLCTIDSILSNFEMFEMLQKEFVKLKYPAKLFDPISWTINIFRKQRISMVQNINQFIFIYDCLLFYFRLRLDDITERTDGDGSNKDNISLSALIEQIEKLEILQTFVDDKLKELPQ | Function: Major phosphatase responsible for tyrosine dephosphorylation of MAP kinases FUS3 and HOG1 to inactivate their activity; it also has important roles, along with MSG5, in the inactivation of FUS3 following pheromone stimulation.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 105224
Sequence Length: 928
Subcellular Location: Cytoplasm
EC: 3.1.3.48
|
Q9W0G1 | MSEQKTSGSGSAAAARLQIEAEYKDKGPQWHRFYKEICETCDREAKEKQFSTSESERHTNRGLNRYRDVNPYDHSRIVLKRGSVDYINANLVQLERAERQYILTQGPLVDTVGHFWLMVWEQKSRAVLMLNKLMEKKQIKCHLYWPNEMGADKALKLPHVKLTVELVRLETYQNFVRRWFKLTDLETQQSREVMQFHYTTWPDFGIPSSPNAFLKFLQQVRDSGCLSRDVGPAVVHCSAGIGRSGTFCLVDCCLVLIDKYGECNVSKVLCELRSYRMGLIQTADQLDFSYQAIIEGIKKLHDPTFLDAEEPLISNDTETHTLDELPPPLPPRVQSLNLPLAPNSGGILSLNMRAAQANGAESIGKELSKDALNNFINQHDMIHDAEVADSRPLPPLPVRAFNDSDSDEDYLLDDDDEDDTDEDEEYETINEHDADPVNGHVPATTQPHADDVNANNEKPAVPVDEQHKANGIDPIPGQLPASPENELKRRKRNEYQASLEQKVNDMKRKQRENEDKQLAAKKRRSLLTYIAAGVVVGVICAYAYTKLG | Function: Non-receptor protein tyrosine phosphatase required for maintaining Dock in its non-phosphorylated state.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 62105
Sequence Length: 548
Subcellular Location: Cytoplasm
EC: 3.1.3.48
|
Q753L9 | MEFSVEGTQFSPPVKRIFDTAGTHDFQKSLTMYRLQSHLERYLKLVQGQKIPKSSQNRAVVRFVCILERLDALMDETPPRTGSARRFGDLACRDWHDRMQGELDGLLETLLPEAARRSAAELRYYLGSAFGSRERLDYGTGHELAFLAVVVALDMLGLWTEDKFTGEDMLYVWARYYALVHRLILTYNLEPAGSHGVWGLDDHLHLAYILGASQWAQDRNVPMQPSDILDPKAVARYSETNLYCNSIAFLLRVKTGHFAQHSPMLHDIAQTVPTWSKVTTGLIKMYRVEVLNKFPVVQHFWFGTGFFPWVDMAHGMSLPNYEAPSETSEKPAAGTAHTTTTTMPPPRMTANCGYGPLGRLVTPRR | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 41327
Sequence Length: 365
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q4WMU5 | MANSFPLRVLPTIDPSAGHTFITPSKRIHESEDVSEFLISKAYVDIMTFLLQLNRAMIPVKLADGTVQSWPINTDAVEFSAPVRQLQQLLTKLEELLAEAPPDTGPRRFGNISFRRWYELVESRASELLGECLPSELLQAKSSDPNSVTAEAELKAYFLGSWGSPQRLDYGTGHELSFLAFLAGIWKLNGFPKTTPGVEERAIVLGVIQPYLELVRTIIKRYTLEPAGSHGVWGLDDHSFIPYILGSAQLAPAISETDPTPEEGSLPGAPSPNGVTKAHIVERERLTNMYFSAIGFIYDVKKGPFWEHSPMLYDISGIQAGWGKINKGMIKMYNAEVLSKFPVVQHFPFGSLFSWDRDPNAVPPPTSAHMSTTQSQSRGPAVPSAGQTPPSGTRAPWATATQAAPPAGAGTAAPWAAKRDGCTPGKPPTSLPDTSRLPPGPMAPTRAPWAASSTGQAPGGDPTHVPTKAPWAK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 51135
Sequence Length: 473
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q5ADP9 | MNWKTPSKKIYDSADLKNFEKSIAFEKLQKTLQQIILSVENHKIPPGILNVDIVTRPGRIGSIPLPSLIEPTTTTTTRENKIGPSNGNVEILIELFQYLNKLIDETPPLKGPTRFGNFACRDWHDKIDIIPILKKFKFPQELSSSNNSSSKSNIDGFLLESSYYLLNSFGSKIRLDYGTGHELSFLAFIGSLIEFKILNHPTTTEEINGKEILIIFANYYDLVRRLILVYNLEPAGSHGVWGLDDHFHLIYILGASQFINDKLAPIVQRSLSSQVINSCKLTNFYINAIAFIFRLKTGPFNEHSPIIFDIHNKVFSWTKVRQGLIKMYMVEVFNKFPVLQHFWCGEVLYPWKDHQGNDLPVNEKEETELDKPPETTLNSTTTTTTTTKVSSSTSKIPFTPAPWANTTTTHAVPRNTRNTRNPRS | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48232
Sequence Length: 424
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
O02058 | MFRMPIVTMERVDSFSAAHRLHSEKLSDAENKETFGKCNNSNGHGHNYVWKVKLRGEVDPTSGMVYDLAKLKKEMSLVLDTVDHRNLDKDVEFFKTTVSTSENVAIYMFEKLKSVMSNPSVLYKVTIEETPKNIFTYKGC | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin (By similarity).
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Mass (Da): 16046
Sequence Length: 140
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
|
Q1ZXI0 | MSRTVILTRREVFSSSHRLYSDKLSLEENKKIYGKCINSHGHNYVLEVSIKGAVKEDIGMFMNITELKEILKEKVMDKLDHKNLENDVPELKGIVTTTENLSIFIWDQLFPSLKDFLYEVKILETENNFVVYRGE | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin (By similarity).
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Mass (Da): 15771
Sequence Length: 135
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
|
P48611 | MSQQPVAFLTRRETFSACHRLHSPQLSDAENLEVFGKCNNFHGHGHNYTVEITVRGPIDRRTGMVLNITELKEAIETVIMKRLDHKNLDKDVEYFANTPSTTENLAVYIWDNIRLQLKKPELLYEVKIHETPKNIISYRGPYPLNGIYNPINKRIAHDSCTNISSDSD | Cofactor: Binds 1 zinc ion per subunit.
Function: Required for pigment and biopterin synthesis.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Mass (Da): 19337
Sequence Length: 168
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
|
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