UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
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A0A2I7G3B0 | MSSGANGNSKSLAYDIKFTKLFINGEFVDSISGSTFETIDPATEEVLATVAEGREEDVDLAVKAAREAFDNGPWPRLSGEARRKILLKFADLIEENADEIATLEVIDTGKPFQIARYVENSWTSETFRYFAGAADKIRGATLKMSSDFQAYTLREPIGVVGHIIPWNAPAYLFAMKVAPALAAGCTVVIKPAENTPLVGLFMAYLSKLAGVPDGVINVVNGFGSTAGAAVSSHMDIDAVTFTGSTKVGRTIMQAAAASNLKPVSLELGGKSPFIVFDDADIEKAAEIAVLGVLSNKGELCVAGSRVFVHEGIYDAFVKKLEATVKNWATGDRFDAATRHGPQNNKQQYEKVLSYIELGKKEGATLVTGGKPFGNKGYYIEPTLFTNVTDEMTIAKEEIFGPVIMVLKFKTIEEVIRRANATTYGLAAGIMTKNIDIANTVTRSIRAGSVWVNCYLALDRDTPFGGYKMSGFGREQGLEALEHYLQVKTVTTPIYNSPWL | Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Mediates the conversion of trans-chrysanthemal into trans-chrysanthemic acid (PubMed:29122986). Can also use octanal, hept-2-enal, dodecanal, citral, farnesal, citronellal and perillyl aldehyde as substrates (PubMed:29122986). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH H2O + NADP(+) + octanal = 2 H(+) + NADPH + octanoate (1R,3R)-chrysanthemal + H2O + NAD(+) = (1R,3R)-chrysanthemate + 2 H(+) + NADH (1R,3R)-chrysanthemal + H2O + NADP(+) = (1R,3R)-chrysanthemate + 2 H(+) + NADPH (E)-hept-2-enal + H2O + NADP(+) = (E)-hept-2-enoate + 2 H(+) + NADPH dodecanal + H2O + NADP(+) = dodecanoate + 2 H(+) + NADPH citral + H2O + NADP(+) = 3,7-dimethylocta-2,6-dienoate + 2 H(+) + NADPH H2O + NADP(+) + perillyl aldehyde = 2 H(+) + NADPH + perillate (2E,6E)-farnesal + H2O + NADP(+) = (2E,6E)-farnesoate + 2 H(+) + NADPH (S)-(-)-citronellal + H2O + NADP(+) = (S)-(-)-citronellate + 2 H(+) + NADPH kcat is 0.11 sec(-1) with trans-chrysanthemal as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.096 sec(-1) with trans-chrysanthemal as substrate (in the presence of NADP(+)) (PubMed:29122986). kcat is 0.09 sec(-1) with NAD(+) as substrate (in the presence of trans-chrysanthemal) (PubMed:29122986). kcat is 0.086 sec(-1) with NADP(+) as substrate (in the presence of trans-chrysanthemal) (PubMed:29122986). Isoprenoid biosynthesis. Homotetramer. Expressed in flowers and disk florets. Belongs to the aldehyde dehydrogenase family. |
P39616 | MNSIPSIISKHKAYFAAGHTRPLESRLNILRKLKQAVRTHEADLIAALYQDLHKSEQEAYSTEIGIVLEEISFVMKRLRKWSKPKRVKTPLTHLGSKSIIIPEPYGTVLVIAPWNYPLQLALSPLIGAIAAGNTVVLKPSEYTPAVSAILSKLISSVFPTDYVAMAEGGPDVSTALLQQPFDYIFFTGSVAVGKIVMEAAAKQLIPVTLELGGKSPCIVHKDADIQLAAKRIVFGKFTNAGQTCIAPDYLFVHEDIKTKLTEEMKRAIREFYGPQPERNPQYGKIVSERHYQRLLSFLNDGIPLTGGQSDPNHHKIAPTILEQVRDDSPVMQEEIFGPILPLFTYRNIGEVIEKVQSRPKPLALYLFTTNKEIERAVLGNLSFGGGCVNDTLMHVATPYLPFGGVGESGIGSYHGFDSFNTFTHKKSVVKQTNRFDFAFRYPSSKNGLRMIRKILK | an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Belongs to the aldehyde dehydrogenase family. |
Q1LZC6 | MLRAVALAAARLGPRQGRRLLSAATQAVPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDVICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRLLNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGKSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGAKLLCGGGAAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTEVKTVTVRVPQKNS | an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Belongs to the aldehyde dehydrogenase family. |
P45959 | MMSSIAAPKLKEKVEKFLSGKKKMYINGSFVESASGKTFDTPNPATGERLATVYEGDAEDIDRAVKAAREAFD | an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Belongs to the aldehyde dehydrogenase family. |
P12762 | AAAATQAVPAPNQQPEVFYNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAAGDKEDVDRAVKAARAAFQLGSPWRRMDASDRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAAKLGPALATGNVVVMKVAEQTPLTALYVANLTKEAGFPPGVVNVVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGRSNLKKVTLELGGKSPNIIVSDADMDWAVEQAHFALFFNQGQCCGAGSRTFVQEDVYAEFVERSVARAKSRVVGNPFDSQTEQGPQVDETQFNKVLGYIKSGKEEGAKLLCGGGAAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGNGRELGEYGLQAYTEVKTVTIKVPQKNS | an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Belongs to the aldehyde dehydrogenase family. |
Q6IV71 | MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS | an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Genetic variation in ALDH2 is responsible for individual differences in responses to drinking alcohol [MIM:610251]. Allele ALDH2*2 is associated with a very high incidence of acute alcohol intoxication in Orientals and South American Indians, as compared to Caucasians. Belongs to the aldehyde dehydrogenase family. |
Q25417 | MLRATLARLEMAPKVTHIQEKLLINGKFVPAVSGKTFEVVNPADEKVIANVAEAEKADVDLAVKAARHAFESFRMTDCQWRRNLMLRLADILEKNSKEMAALESLDNGKPYEVALNVDVALSVECFRYCAGLADKVNGTVPPRSGNFLGIVKRQPIGVCGQIIPWNFPLLMAAFKLSPALAMGNTVVLKPAEQTPLTAVRLGEMVMEAGYPDGVLNILPGFGATAGSEIARHMDVDKIAFTGSTAVGHQVMQMAAETNLKKVSLELGGKSALIVCEDADLEEAAEVATTRVYFNTGQVCTASSRIYVHESVYDEFVSRLRKNAEARKVGPGNDTGNNMGPLVSKKQHERVLGYIEDGVKAGATVVTGGKKIGDKGYFVQPTIFSDVKEDMRICKEEIFGPVTCVMKYKDMDEVVKRANDSIYGLAAGICTRSMDTALRYSTYLNAGTVWVNTWNNFCPSMPFGGFKQSGIGRELGKEVVDMYTEPKAIHFASRSIVKP | Could have an RNA-binding activity in addition of its catalytic role. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Belongs to the aldehyde dehydrogenase family. |
Q29491 | NLKRVTLELGGKSPCIVFADADLDNAVEFAHRGLFFHQGQCCVAASRLFVEESIYDEFVRRSVERAKKYVLGNPLTPGVSQGPQIDKEQYDKIIDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDEVIKRANNTFYGLAAGVFTKDLDKAVTVSAALQAGTVWVNCYMANSVQCPFGGFKMSGNGRELGEYGLHEYTEVKTVTMKISKKNS | Elephant shrews, in contrast to other mammals, possess both a lens- and a non-lens specific class-1 aldehyde dehydrogenase. Can convert/oxidize retinaldehyde to retinoic acid. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Non-lens specific, predominant form expressed in the liver. Belongs to the aldehyde dehydrogenase family. |
P81178 | SAAATSAVPAPNQQPEVFCNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGSKEDVDKAVKAARAAFQLGSPWRRMDASDRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTIKVPQKNS | an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Belongs to the aldehyde dehydrogenase family. |
P47738 | MLRAALTTVRRGPRLSRLLSAAATSAVPAPNHQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS | Is capable of converting retinaldehyde to retinoic acid. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. By retinoic acid; 3-5 fold increase. Belongs to the aldehyde dehydrogenase family. |
Q2XQV4 | MLRPAALAAARLVLRQGRRLLSAAPTQAVPAPNQQPEIFYNQIFINNEWHDAISKKTFPTVNPSTGDVICHVAEGDKEDVDRAVEAARAAFQLGSPWRRLDASDRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTLPIDGDYFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVSEQTPLTALYVANLIKEAGFPPGVVNIVPGYGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGKSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARARSRVVGNPFDSRTEQGPQIDETQFKKILGYIKSGKEEGAKLLCGGGAAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVIGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTEVKTVTVKVPQKNS | Is capable of converting retinaldehyde to retinoic acid. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Belongs to the aldehyde dehydrogenase family. |
Q5RF00 | MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYNVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS | Is capable of converting retinaldehyde to retinoic acid. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Homotetramer. Belongs to the aldehyde dehydrogenase family. |
Q91ZD7 | MLRAALSTARRGPRLSRLLSAAATSAVPAPNQQPEVFCNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAAQAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS | an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Belongs to the aldehyde dehydrogenase family. |
Q9C2U0 | MPAQDVLTRKTGVIVGDDVKALFDYAKEHKFAIPAINVTSSSTVVAALEAARDNKSPIILQTSNGGAAYFAGKGVSNEGQNASIRGSIAAAHYIRSIAPAYGIPVVLHTDHCAKKLLPWFDGMLKADEEYFAKHGEPLFSSHMLDLSEETDEENIGLCVKYFTRMAKIHQWLEMEIGITGGEEDGVNNEGTSNDKLYTTPETVFSVHEALSKISPNFSIASAFGNVHGVYKIAAALKPELLGTFQDYAAKQLNKKAEDKPLYLVFHGGSGSSTKDFHTAIDFGVVKVNLDTDCQFAYLSGIRDYVLNKKDYLMTPVGNPTGEDSPNKKYYDPRVWVREGEKTMSKRITQALEIFRTKGALE | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homodimer. Belongs to the class II fructose-bisphosphate aldolase family. |
P91759 | HNMFLEGTLLKPNMVTAGQGCPKKYTPEDIARATVTALNRTVPAAVAGITFLSGGQSEEDATINLNAINQFPGRKPWPLTFSYGRALQASVLKAWGGKDEL | beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class I fructose-bisphosphate aldolase family. |
P08440 | MSAYCGKYKDELIKNAAYIGTPGKGILAADESTGTIGKRLSSINVENVEENRRALRELLFCCPGALQYISGVILFEETLYQKTKDGKPFVDVLKEGGVLPGIKVDKGTIEVVGTDKETTTQGHDDLGKRCAKYYEAGARFAKWRAVLKIGPNEPSQLAIDLNAQGLARYAIICQENGLVPIVEPEILVDGPHDIDRCAYVTETVLAACYKALNEHHVLLEGTLLKPNMVTPGSDSKKVTPEVIAEYTVRTLQRTVPAAVPAVLFLSGGQSEEEATRNLNAMNKLSTKKPWSLSFSFGRALQASTLKAWAGKVENLEKARAAFLARCKANSEATLGTYKGDAAADTESLHVKDYKY | beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class I fructose-bisphosphate aldolase family. |
X2BEQ4 | MPIATPEVYAEMLGQAKQNSYAFPAINCTSSETVNAAIKGFADAGSDGIIQFSTGGAEFGSGLGVKDMVTGAVALAEFTHVIAAKYPVNVALHTDHCPKDKLDSYVRPLLAISAQRVSKGGNPLFQSHMWDGSAVPIDENLAIAQELLKAAAAAKIILEIEIGVVGGEEDGVANEINEKLYTSPEDFEKTIEALGAGEHGKYLLAATFGNVHGVYKPGNVKLRPDILAQGQQVAAAKLGLPADAKPFDFVFHGGSGSLKSEIEEALRYGVVKMNVDTDTQYAFTRPIAGHMFTNYDGVLKVDGEVGVKKVYDPRSYLKKAEASMSQRVVQACNDLHCAGKSLTH | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class II fructose-bisphosphate aldolase family. |
P47269 | MLVNFKLMLQKAKLGKYAIPHININNYEWAKAVLTAANQANSPIIVSVSEGALKYMSGYSVVIPLVKGLIESLSVKVPVTLHLDHGSYDACIQALQAGFSSVMFDGSHLPFEENFNKSKKLIEIAQKTNASVELEVGTIGGEEDGVIGQGELANVDECKQIASLKPDALAAGIGNIHGIYPKNWKGLNFPLIETISKITNLPLVLHGGSGILENDVKKAISLGICKLNINTECQLAFAHEIRKYIESNKDLDLNKKGYDPRKLLKEPTQAIVDTCLEKIDLCGSRNKA | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homodimer. Belongs to the class II fructose-bisphosphate aldolase family. |
O69600 | MPIATPEIYAEMLRRAKENSYAFPAINCTSSETVNAAIKGFADAGSDGIIQFSTGGAEFASGLGVKDMVTGAVALAKFTHTIAAKYPINVALHTDHCPKDKLDSYVRPLLAISARRVATGKDPLFGSHMWDGSAIPIDENLAIAQDLLKDAAAAKIILEVEIGVVGGEEDGVAGEINEKLYTTPKDFVKTIDALGAGEHGKYLLAATFGNVHGVYKPGNVKLRPDILAEGQKVAAAKLSQSEGSKPFDFVFHGGSGSEKSEIEEALRYGVVKMNVDTDTQYAFTRPVSGHMFTNYDGVLKVDGDVGNKKVYDPRSYLKKAEASMTERVLEACNDLRCAGKSVAAS | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class II fructose-bisphosphate aldolase family. |
P75089 | MLVNIKQMLQHAKQHHYAVPHININNYEWAKAVLTAAQQAKSPIIVSTSEGALKYISGHQVVVPMVKGLVDALKITVPVALHLDHGSYEGCKAALQAGFSSIMFDGSHLPFQENFTKSKELIELAKQTNASVELEVGTLGGEEDGIVGQGELANIEECKQIATLKPDALAAGIGNIHGLYPDNWKGLNYELIEAIAKATNLPLVLHGGSGIPEADVKKAIGLGISKLNINTECQLAFAKAIREYVEAKKDLDTHNKGYDPRKLLKSPTQAIVDCCLEKMQLCGSTNKA | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homodimer. Belongs to the class II fructose-bisphosphate aldolase family. |
P67475 | MPIATPEVYAEMLGQAKQNSYAFPAINCTSSETVNAAIKGFADAGSDGIIQFSTGGAEFGSGLGVKDMVTGAVALAEFTHVIAAKYPVNVALHTDHCPKDKLDSYVRPLLAISAQRVSKGGNPLFQSHMWDGSAVPIDENLAIAQELLKAAAAAKIILEIEIGVVGGEEDGVANEINEKLYTSPEDFEKTIEALGAGEHGKYLLAATFGNVHGVYKPGNVKLRPDILAQGQQVAAAKLGLPADAKPFDFVFHGGSGSLKSEIEEALRYGVVKMNVDTDTQYAFTRPIAGHMFTNYDGVLKVDGEVGVKKVYDPRSYLKKAEASMSQRVVQACNDLHCAGKSLTH | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Was identified as a high-confidence drug target. Belongs to the class II fructose-bisphosphate aldolase family. |
V5IKX9 | MGIFDELNLPAGVLYGDDVLKLFQYAREKQFAIPACNVTSSSTAVAALEAARDQKAPIILQTSQGGAAFFAGKGIKDSAEKREASVAGAIAAAHYIRSIAPIYGIPVVLHTDHCAKKLLPWLDGMLEEDEKFFKANGVPLFSSHMIDLSEEPVEENISTCVKYLKRMAPMKQWLEMEIGITGGEEDGVDNSEVDNASLYTQPEDIWQIEEAFRPISPYFSIAAGFGNVHGVYAPGNVKLHPELLGKHQAYVSEKLGGKDKKPVFFVFHGGSGSSKEEYREAISNGVVKVNVDTDLQWSYLVGIRDYILNNIDYLRSQVGNPEGPNKPNKKKYDPRVWIREGEKTMKARVEEALKDFNAAGTV | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homodimer. Belongs to the class II fructose-bisphosphate aldolase family. |
Q9XDP3 | MALVPLRLLLDHAAENGYGIPAFNVNNLEQIQAILKAAVETDSPVILQASRGARAYAGENFLRHLILAAVETYPHIPIVMHQDHGNAPATCYSAIKNNFTSVMMDGSLEADAKTPASFEYNVNVTREVVNVAHALGVSVEGELGCLGSLETGAGEAEDGHGFEGTLDHSQLLTDPDEAVEFVEATQVDALAVAIGTSHGAYKFTRKPTGEILAISRIEEIHRRLPNTHLVMHGSSSVPEDLLALINQYGGAIPETYGVPVEEIQKGIKSGVRKVNIDTDNRLAITAAVREACAKKPEEFDPRHFLKPSITYMQKVCAERYQQFGTAGNASKIKQISLEDFAAKYAKGELNVVTKAAAKV | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class II fructose-bisphosphate aldolase family. |
Q8YNK2 | MALVPLRLLLDHAAENGYGIPAFNVNNLEQIQAILKAAAETDSPVILQASRGARNYAGENFLRHLILAAVETYPEIPIVMHQDHGNAPSTCYSAIKNNFTSVMMDGSLEADAKTPASFEYNVNVTREVVNVAHALGVSVEGELGCLGSLETGAGEAEDGHGFEGTLDHSQLLTDPDEAVNFVEATQVDALAVAIGTSHGAYKFTRKPTGEILAISRIEEIHRRLPNTHLVMHGSSSVPEDLIALINEYGGAIPETYGVPVEEIQKGIKSGVRKVNIDTDNRLAITAAVREALAKNPKEFDPRHFLKPSITYMQKVCAERYVQFGTAGNASKIKQVSLETFAAKYAKGELNAISKAAAKV | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class II fructose-bisphosphate aldolase family. |
O22621 | MDPEAFSASLFKWDPRGAMPPPNRLLEAVAPPQPPPPPLPPPQPLPPAYSIRTRELGGLEEMFQAYGIRYYTAAKITELGFTVNTLLDMKDDELDDMMNSLSQIFRWELLVGERYGIKAAIRAERRRLEEEEGRRRHILSDGGTNVLDALSQEGLSEEPVQQQEREAAGSGGGGTAWEVVAPGGGRMRQRRRKKVVVGRERRGSSMEEDEDTEEGQEDNEDYNINNEGGGGISERQREHPFIVTEPGEVARGKKNGLDYLFHLYEQCRDFLIQVQNIAKERGEKCPTKVTNQVFRFAKKAGASYINKPKMRHYVHCYALHCLDEDASNALRRAFKERGENVGAWRQACYKPLVAIAARQGWDIDAIFNGHPRLSIWYVPTKLRQLCHSERSNAAAAASTSVSGGGVDHLPHF | Probable transcription factor required for the specification of floral meristem identity. Expressed in the floral meristem and also in the vegetative meristem. Belongs to the FLO/LFY family. |
A0A144A3T1 | MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY | Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:26289816). Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related anonymous protein (TRAP), the erythrocyte binding ligand (EBL) and reticulocyte binding homolog (RH) protein families; this interaction is probably involved in transducing the motor force across the parasite surface required for sporozoite and ookinete gliding motility and merozoite invasion (PubMed:22991428, PubMed:25261592) (Probable). Stimulates actin polymerisation (PubMed:25261592). beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate The cytoplasmic tail of TRAP and probably other adhesins acts as a competitive inhibitor as the binding sites of the glycolytic substrate fructose 1,6-bisphosphate and TRAP partially overlap. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homotetramer (PubMed:26289816). Interacts with TRAP (via cytoplasmic domain); the interaction prevents substrate binding and thereby inhibits aldolase activity (PubMed:26289816, PubMed:16321976) (Probable). Interacts with MTRAP (via cytoplasmic domain); MTRAP phosphorylation may increase the binding to FBPA (PubMed:16321976). Interact with RH1 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074). Interacts with RH2b (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074). Interacts with RH4 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074). Interacts with AMA1 (via cytoplasmic domain); the interaction is weak, however it may be increased upon AMA1 phosphorylation (PubMed:27607074). Interacts with EBA140 (via cytoplasmic domain); the interaction is weak (PubMed:27607074). Interacts with EBA175 (via cytoplasmic domain); the interaction is weak (PubMed:27607074). Interacts with EBA181 (via cytoplasmic domain); the interaction is weak (PubMed:27607074). Interacts with G-actin and F-actin (PubMed:25261592). May interact with ACT2/actin II; the interaction inhibits FBPA catalytic activity (By similarity). Interacts with human SLC4A1/band 3 (via N-terminus); the interaction inhibits FBPA catalytic activity (By similarity). Expressed during parasite asexual blood stages, including in schizonts (at protein level). Belongs to the class I fructose-bisphosphate aldolase family. |
P14223 | MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY | Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:2190085). Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related anonymous protein (TRAP), the erythrocyte binding ligand (EBL) and reticulocyte binding homolog (RH) protein families; this interaction is probably involved in transducing the motor force across the parasite surface required for sporozoite and ookinete gliding motility and merozoite invasion (By similarity). Stimulates actin polymerisation (By similarity). beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate The cytoplasmic tail of TRAP and probably other adhesins acts as a competitive inhibitor as the binding sites of the glycolytic substrate fructose 1,6-bisphosphate and TRAP partially overlap. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homotetramer (PubMed:9521758). Interacts with TRAP (via cytoplasmic domain); the interaction prevents substrate binding and thereby inhibits aldolase activity (PubMed:17426153). Interacts with MTRAP (via cytoplasmic domain); MTRAP phosphorylation may increase the binding to FBPA (By similarity). Interact with RH1 (via cytoplasmic domain) (By similarity). Interacts with RH2b (via cytoplasmic domain) (By similarity). Interacts with RH4 (via cytoplasmic domain) (By similarity). Interacts with AMA1 (via cytoplasmic domain); the interaction is weak, however it may be increased upon AMA1 phosphorylation (By similarity). Interacts with EBA140 (via cytoplasmic domain); the interaction is weak (By similarity). Interacts with EBA175 (via cytoplasmic domain); the interaction is weak (By similarity). Interacts with EBA181 (via cytoplasmic domain); the interaction is weak (By similarity). Interacts with G-actin and F-actin (By similarity). May interact with ACT2/actin II; the interaction inhibits FBPA catalytic activity (By similarity). Interacts with human SLC4A1/band 3 (via N-terminus); the interaction inhibits FBPA catalytic activity (By similarity). Expressed during parasite asexual blood stages, including in schizonts and free merozoites (at protein level). Belongs to the class I fructose-bisphosphate aldolase family. |
Q27744 | MNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSNHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY | Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:3285469, PubMed:2204832). Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related anonymous protein (TRAP), the erythrocyte binding ligand (EBL) and reticulocyte binding homolog (RH) protein families; this interaction is probably involved in transducing the motor force across the parasite surface required for sporozoite and ookinete gliding motility and merozoite invasion (By similarity). Stimulates actin polymerisation (By similarity). beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate The cytoplasmic tail of TRAP and probably other adhesins acts as a competitive inhibitor as the binding sites of the glycolytic substrate fructose 1,6-bisphosphate and TRAP partially overlap (By similarity). Inhibited by suramin, an antiparasitic drug used to treat Trypanosome-mediated infection (PubMed:2204832). Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homotetramer (PubMed:3285469, PubMed:2204832). Interacts with TRAP (via cytoplasmic domain); the interaction prevents substrate binding and thereby inhibits aldolase activity (By similarity). Interacts with MTRAP (via cytoplasmic domain); MTRAP phosphorylation may increase the binding to FBPA (By similarity). Interact with RH1 (via cytoplasmic domain) (By similarity). Interacts with RH2b (via cytoplasmic domain) (By similarity). Interacts with RH4 (via cytoplasmic domain) (By similarity). Interacts with AMA1 (via cytoplasmic domain); the interaction is weak, however it may be increased upon AMA1 phosphorylation (By similarity). Interacts with EBA140 (via cytoplasmic domain); the interaction is weak (By similarity). Interacts with EBA175 (via cytoplasmic domain); the interaction is weak (By similarity). Interacts with EBA181 (via cytoplasmic domain); the interaction is weak (By similarity). Interacts with G-actin and F-actin (By similarity). May interact with ACT2/actin II; the interaction inhibits FBPA catalytic activity (PubMed:2204832). Interacts with human SLC4A1/band 3 (via N-terminus); the interaction inhibits FBPA catalytic activity (PubMed:2204832). Expressed during parasite asexual blood stages (at protein level). May be an effective malaria vaccine as determined by epitope response in sera (PubMed:3285469). Antibodies against FBPA inhibit its catalytic activity (PubMed:3285469, PubMed:2204832). Belongs to the class I fructose-bisphosphate aldolase family. |
Q9I5Y1 | MALISMRQMLDHAAEFGYGVPAFNVNNLEQMRAIMEAADKTDSPVIVQASAGARKYAGAPFLRHLILAAIEEFPHIPVVMHQDHGTSPDVCQRSIQLGFSSVMMDGSLREDGKTPADYDYNVRVTQQTVAFAHACGVSVEGELGCLGSLETGMAGEEDGVGAEGVLDHSQLLTDPEEAADFVKKTKVDALAIAIGTSHGAYKFTKPPTGDTLSIQRIKEIHARIPDTHLVMHGSSSVPQDWLAIINEYGGEIKETYGVPVEEIVEGIKYGVRKVNIDTDLRLASTGAIRRFLAQNPSEFDPRKYFSKTVEAMRDICIARYEAFGTAGNASKIKPISLEGMFQRYARGELDPKVN | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class II fructose-bisphosphate aldolase family. |
O87796 | MALISMRQMLDHAAEFGYGVPAFNVNNLEQMRAIMEAADKTDSPVIVQASAGARKYAGAPFLRHLILAAIEEFPHIPVCMHQDHGTSPDVCQRSIQLGFSSVMMDGSLREDGKTPADYDYNVRVTQQTVAFAHACGVSVEGELGCLGSLETGMAGEEDGVGAEGVLDHSQLLTDPEEAADFVAKTKVDALAIAIGTSHGAYKFTNPPTGDTLSIQRIKEIHARIPDTHLVMHGSSSVPQEWLKIINEYGGEIGETYGVPVEEIVEGIKYGVRKVNIDTDLRLASTGAIREFLAKNPSEFDPRKYFAKTVAAMRDICIARYEAFGTAGNASKIKPISLEGMFQRYASGELDPKIN | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class II fructose-bisphosphate aldolase family. |
P58336 | MARITLRQLLDHAAERSYGVPAFNINNMEQGLAIMEAARASDAPVILQVSRGARSYANDVMLAKMMEALEEMYPDIPLCIHQDHGNNVATCLTAIQHGFTSVMMDGSLKEDAKTPADYDYNVSITAEVSRLAHMVGASVEGELGCLGSLETGHGEAEDGHGFEGALDRSQLLTDPDEAARFVAETGVDALAVAIGTSHGAYKFTRKPTGEVLAMDVIEKIHERLPDTHIVMHGSSSVPQEWQDVFNAHGGQMRETYGVPVEEIVRGIRFGVRKVNIDTDLRLAAAAAFRRVADTSRSEFDPRKFLKPAMDAMSAVCKARFEAFGTAGNASRIKVVPMPEMARRYASGSLKPQSARSEAA | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Carbohydrate biosynthesis; Calvin cycle. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homodimer. Belongs to the class II fructose-bisphosphate aldolase family. |
P53442 | MSRFQPYLTEAQENDLRRIAQAICAPGKGILAADESTATMGKRLQQIGVENNEENRRLYRQLLFSADHKLAENISGVILFEETLHQKSDDGKTLPTLLAERNIIPGIKVDKGVVPLAGTDNETTTQGLDDLASRCAEYWRLGCRFAKWRCVLKISSHTPSYLAMLENANVLARYASICQQNGLVPIVEPEVLPDGDHDLLTAQRVTEQVLAFVYKALADHHVYLEGTLLKPNMVTAGQACKKAYTPQENALATVRALQRTVPPAVPGITFLSGGQSELDATKNLNEINKIPGPKPWALTFSFGRALQASVLATWKGKKENVHAAQEELLKLAKANGAAAVGKFEGNMGTTLGDKSLFVANHAY | beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Belongs to the class I fructose-bisphosphate aldolase family. |
Q02E40 | MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF | Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity. Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme. alpha-D-mannose 1-phosphate = D-mannose 6-phosphate alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate Binds 1 Mg(2+) ion per subunit. Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Monomer. Belongs to the phosphohexose mutase family. Extended N-terminus. |
P26276 | MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF | Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). alpha-D-mannose 1-phosphate = D-mannose 6-phosphate alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate Binds 1 Mg(2+) ion per subunit (PubMed:23517223). Zn(2+) can substitute, but yields a catalytically inactive enzyme (PubMed:14725765, PubMed:16880541, PubMed:16595672). Requires glucose 1,6-bisphosphate (G1,6P) as an activator (PubMed:8050998, PubMed:11716469). Reaction making glucose 6-phosphate is subject to substrate inhibition, reactions making mannose 1-phosphate or glucose 1-phosphate are not. 1-deoxyglucose 6-phosphate competitively inhibits glucose 1-phosphate (PubMed:11716469). Inhibited by xylose 1-phosphate (PubMed:16880541). kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate. TM is 66 degrees Celsius for phosphorylated protein and 62 degrees Celsius for unphosphorylated protein. Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Monomer. By D-mannose 6-phosphate. Consists of 4 domains; domains 1-3 have a similar toplological core while domain 4 folds over and closes the active site from a hinge region. Mutants in the hinge region (residues 262 and 368-369) generally increase KM for glucose 1-phosphate 2-fold while reducing kcat about 10-fold (PubMed:18690721). May be phosphorylated, protein expressed in E.coli. No longer expresses O-antigen LPS side chain or A-band LPS, sensitive to serum, resistant to virus E79. Has no phosphomannomutase nor phosphoglucomutase activities (PubMed:7515870, PubMed:8050998). Does not make rhamnolipid (PubMed:10481091). Most crystals have Zn(2+) rather than Mg(2+) and are catalytically inactive. Belongs to the phosphohexose mutase family. |
Q88C93 | MAHLVPAALPDSIFRAYDIRGVVGKTLHAETAYWIGRAIGAQSLAQGEPQVSVGRDGRLSGPMLVEQLIKGLVDAGCNVSDVGLVPTPALYYAANVLAGKSGVMLTGSHNPSDYNGFKIVIAGDTLANEQIQALLTRLKTNDLTLAQGRVEKVEILDRYFKQIVGDVKLAKKLKVVVDCGNGAAGVVAPQLIEALGCEVIPLFCEVDGNFPNHHPDPGKPENLEDLIAKVKETGADIGLAFDGDGDRVGVVTNTGSIVYPDRLLMLFAQDVLSRNPGAEIIFDVKCTRRLTPLIEQHGGRALMWKTGHSLIKKKMKQTGSLLAGEMSGHIFIKERWYGFDDGIYSAARLLEILSKTEQSAENLFAAFPNDISTPEINIDVTDEGKFSIIDALQRDADWGEANLTTIDGVRVDYANGWGLVRASNTTPVLVLRFEADSDAELQRIKDVFRTQLLRVEPELQLPF | The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for biofilm production (By similarity). alpha-D-mannose 1-phosphate = D-mannose 6-phosphate alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate Binds 1 Mg(2+) ion per subunit. Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Monomer. Belongs to the phosphohexose mutase family. |
Q88BD4 | MNSPASVAPILPDTIFRAYDIRGVVEDTLNAETAYWIGRAIGSESLAQNEPNVSVGRDGRLSGPELVQQLIQGLHDSGCHVSDVGLVPTPALYYAANVLAGKTGVMLTGSHNPKDYNGFKIVIAGDTLANEQIQALHERIKTNNLTSQKGSITQVNILDRYFKQIKDDIVMARKLKVVVDCGNGAAGVIAPQLIEALGCEVISLFAEVDGNFPNHHPDPGKLENLQDLIAKVKETGADLGLAFDGDGDRVGVVTNAGNVVYPDRLLMLFALDVLKRNPGADIIFDVKCTRRLTPLISEHGGRPVMWKTGHSLIKKEMKKSGALLAGEMSGHIFFKERWFGFDDGIYSAARLLEILSQEPANAEDLFETFPNDISTPEINIKVTDVTKFSIIEALEKDAQWGDAKLTTIDGVRVDYPKGWGLVRASNTTPVLVLRFEAETQAELERIQGVFHAELKKVAPDLDLPF | The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for biofilm production (By similarity). alpha-D-mannose 1-phosphate = D-mannose 6-phosphate alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate Binds 1 Mg(2+) ion per subunit. Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Monomer. Belongs to the phosphohexose mutase family. |
P51585 | MRISIFGLGYVGAVCAGCLSGRGHEVVGVDISAAKIDMINQGKSPIVEPGLGELLAEGVKTGRLRGTTNVTEAVLATELSMLCVGTPSKLNGDLELDYIEEVCRQMGSALRDKTERHTVVVRSTVLPGTVHNVVIPILEEFSGKKAGVDFGVAVNPEFLRESTAIKDYNFPPMTVIGELDKASGRRLASIYAELDAPIVRKGIAVAEMIKYTCNVWHATKVTFANEIGNIAKAAGVDGREVMEVVCMDNKLNLSQYYMRPGLAFGGSCLPKDVSALSYRAHLWDIEAPLISSLMRSNAAQVQKAYDMIDKHGSRKVALLGLSFKAGTDDLRESPQLELAEMLIGKGFKLSIFDSNVEYARDHGANGHYIKNEIPHVSALLQSDLDKVVAEADVIVLGNADPRFEKLAKDVPAGKKVIDLVGFMPQRTAGAAEGICW | Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and is essential for cyst formation. GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH Glycan biosynthesis; alginate biosynthesis. Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. |
Q9HY71 | MRISIFGLGYVGAVCAGCLSARGHEVIGVDVSSTKIDLINQGKSPIVEPGLEALLQQGRQTGRLSGTTDFKKAVLDSDVSFICVGTPSKKNGDLDLGYIETVCREIGFAIREKSERHTVVVRSTVLPGTVNNVVIPLIEDCSGKKAGVDFGVGTNPEFLRESTAIKDYDFPPMTVIGELDKQTGDLLEEIYRELDAPIIRKTVEVAEMIKYTCNVWHAAKVTFANEIGNIAKAVGVDGREVMDVICQDHKLNLSRYYMRPGFAFGGSCLPKDVRALTYRASQLDVEHPMLGSLMRSNSNQVQKAFDLITSHDTRKVGLLGLSFKAGTDDLRESPLVELAEMLIGKGYELRIFDRNVEYARVHGANKEYIESKIPHVSSLLVSDLDEVVASSDVLVLGNGDELFVDLVNKTPSGKKLVDLVGFMPHTTTAQAEGICW | Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (Probable). Other sugars are not used as substrates (PubMed:2470755). GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH Inhibited by GMP, ATP, GDP-D-glucose and maltose (PubMed:2470755). Inhibited by GMP and deamidoNAD (PubMed:12135385). Optimum pH is 7.7. Optimum temperature is 50 degrees Celsius. Stable at 57.5 degrees Celsius, pH 5.0 for 10 minutes, used to purify protein. Glycan biosynthesis; alginate biosynthesis. Forms a domain-swapped dimer with each peptide contributing to each active site. The dimers assemble further (PubMed:12705829). X-ray structures indicate this enzyme exists as a homotetramer PubMed:12705829, but kinetic and physical results obtained in PubMed:2470755 and PubMed:12135385 indicate that it is probably a homohexamer (Probable). Highly expressed in mucoid but not non-mucoid cells, probably activated by algR. The N-terminus (about 270 residues) binds NAD(+) and GDP-alpha-D-mannose and is joined to C-terminal domain by an exposed linker. Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. Slime with a design - Issue 37 of August 2003 |
Q88NC4 | MRISIFGLGYVGAVCAGCLTARGHEVIGVDVSSTKIDLINQGKSPIVEPGLEALLQQGIANGRLRGTTDFAEAIRASDVSMICVGTPSKKNGDLGLEYIESVCREIGYVLRDTTRRHTIVVRSTVLPGTVKNVVIPILEDCSGKKAGVDFGVAVNPEFLRESTAIKDYDQPPMTVIGELDSASGDILQALYEELDAPIIRKPIEVAEMIKYTCNVWHATKVTFANEIGNIAKAVGVDGREVMDVVCQDKVLNLSQYYMRPGFAFGGSCLPKDVRALTYRAASLDVRAPLLDSLMRSNESQVQNAFELIEAHDKRKVALLGLSFKAGTDDLRESPLVELAERLIGKGYQLDIYDENVQYARVHGANKDYIESKIPHVSSLLNANLQQVIDNADIIVLGNRDEQFRALALQAPAGKQVIDLVGFMNKPTSTTARTEGICW | Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (By similarity). GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH Glycan biosynthesis; alginate biosynthesis. Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. |
O07299 | MRISIFGLGYVGAVCAGCLSARGHDVVGVDISSTKIDLINNGKSPIVEPGLEELLQKGISTGKLRGTTDFAEAIRATDLSMICVGTPSKKNGDLELDYIESVCREIGYVLRDKATRHTIVVRSTVLPGTVANVVIPILEDCSGKKAGVDFGVAVNPEFLRESTAIKDYDLPPMTVIGEFDKASGDVLQSLYEELDAPIIRKDIAVAEMIKYTCNVWHATKVTFANEIGNIAKAVGVDGREVMDVVCQDKALNLSQYYMRPGFAFGGSCLPKDVRALTYRASSLDVEAPLLNSLMRSNTSQVQNAFDMVASYDTRKVALLGLSFKAGTDDLRESPLVELAEMLIGKGFDLSIFDSNVEYARVHGANKDYIESKIPHVSSLLNSDFDQVINDSDVIILGNRDERFRALANKTPEGKRVIDLVGFMTNATSEDGRAEGICW | Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (By similarity). GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH Glycan biosynthesis; alginate biosynthesis. Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. |
Q887P8 | MRISIFGLGYVGAVCAGCLSARGHDVVGVDISSTKIDLINNGKSPIVEPGLEELLQKGLATGKLRGTTDFAEAIRATDLSMICVGTPSKKNGDLELDYIESVCREIGYVLRDKNTRHTIVVRSTVLPGTVANVVIPILEDCSGKKAGVDFGVAVNPEFLRESTAIKDYDLPPMTVIGEFDKASGDVLQSLYEELDAPIIRKDIAVAEMIKYTCNVWHATKVTFANEIGNIAKAVGVDGREVMDVVCQDKALNLSQYYMRPGFAFGGSCLPKDVRALTYRAGSLDVDAPLLNSLMRSNTSQVQNAFDMVASYDTRKVALLGLSFKAGTDDLRESPLVELAEMLIGKGFDLSIFDSNVEYARVHGANKDYIESKIPHVSSLLNSDFDQVINDSDVIILGNRDERFRSLANKTPEGKRVIDLVGFMTNATTEDGRAEGICW | Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (By similarity). GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH Glycan biosynthesis; alginate biosynthesis. By oxidative compounds such as H(2)O(2). Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. |
P59793 | MRISIFGLGYVGAVCAGCLSARGHEVVGVDISSTKIDLINNGKSPIVEPGLEELLQKGISTGKLRGTTDFAEAIRATDLSMICVGTPSKKNGDLELDYIESVCREIGYVLRDKATRHTIVVRSTVLPGTVANVVIPILEDCSGKKAGVDFGVAVNPEFLRESTAIKDYDLPPMTVIGEFDKASGDVLQSLYEELDAPIIRKDIAVAEMIKYTCNVWHATKVTFANEIGNIAKAVGVDGREVMDVVCQDKALNLSQYYMRPGFAFGGSCLPKDVRALTYRAGSLDVEAPLLNSLMRSNTSQVQNAFDMVASYDARKVALLGLSFKAGTDDLRESPLVELAEMLIGKGFDLSIFDSNVEYARVHGANKDYIESKIPHVSSLLNSDFDQVINDSDVIILGNRDERFRALANKTPEGKRVIDLVGFMANATSEDGRAEGICW | Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (By similarity). GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH Glycan biosynthesis; alginate biosynthesis. Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. |
Q44494 | MDYNVKDFGALGDGVSDDTAAIQAAIDAAHAAGGGTVYLPAGEYRVSGGEEPSDGCLTIKSNVHIVGAGMGETVIKMVDGWTQNVTGMVRSAYGEETSNFGMSDLTLDGNRDNLSAKVDGWFNGYIPGQDGADRDVTLERVEIREMSGYGFDPHEQTINLTIRDSVAHDNSLDGFVADYQVGGVFENNVSYNNDRHGFNIVTSTNDFVLSNNVAYGNGGAGLVVQRGSYDLPHPYDILIDGGAYYDNALEGVQLKMAHDVTLQNAEIYGNGLYGVRVYGAQDVQILDNQIHDNSQNGAYAEVLLQSYDDTAGVSGNFYVTTGTWLEGNVISGSANSTYGIQERADGTDYSSLYANSIDGVQTGAVRLYGANSTVSSQSGSGQQATLEGSAGNDALSGTEAHETLLGQAGDDRLNGDAGNDILDGGAGRDNLTGGAGADTFRFSARTDSYRTDSASFNDLITDFDADEDSIDLSALGFTGLGDGYNGTLLLKTNAEGTRTYLKSYEADAQGRRFEIALDGNFTGLFNDNNLLFDAAPATGTEGSDNLLGTDAGETLLGYGGNDTLNGGAGDDILVGGAGRDSLTGGAGADVFRFDALSDSQRNYTTGDNQADRILDFDPTLDRIDVSALGFTGLGNGRNGTLAVVLNSAGDRTDLKSYDTDANGYSFELSLAGNYQGQLSAEQFVFATSQGGQMTIIEGTDGNDTLQGTEANERLLGLDGRDNLNGGAGDDILDGGAGRDTLTGGTGADTFLFSTRTDSYRTDSASFNDLITDFDPTQDRIDLSGLGFSGFGNGYDGTLLLQVNAAGTRTYLKSFEADANGQRFEIALDGDFSGQLDSGNVIFEPAVFNAKDFGALGDGASDDRPAIQAAIDAAYAAGGGTVYLPAGEYRVSPTGEPGDGCLMLKDGVYLAGDGIGETVIKLIDGSDQKITGMVRSAYGEETSNFGMSDLTLDGNRDNTSGKVDGWFNGYIPGQDGADRNVTIERVEIREMSGYGFDPHEQTINLTIRDSVAHDNGLDGFVADYLVDSVFENNVAYNNDRHGFNIVTSTYDFVMTNNVAYGNGGAGLTIQRGSEDLAQPTDILIDGGAYYDNALEGVLFKMTNNVTLQNAEIYGNGSSGVRLYGTEDVQILDNQIHDNSQNGTYPEVLLQAFDDSQVTGELYETLNTRIEGNLIDASDNANYAVRERDDGSDYTTLVDNDISGGQVASVQLSGAHSSLSGGTVEVPQGTDGNDVLVGSDANDQLYGGAGDDRLDGGAGDDLLDGGAGRDDLTGGTGADTFVFAARTDSYRTDAGVFNDLILDFDASEDRIDLSALGFSGFGDGYNGTLLVQLSSAGTRTYLKSYEEDLEGRRFEVALDGDHTGDLSAANVVFADDGSAAVASSDPAATQLEVVGSSGTQTDQLA | Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), producing a polymer with gel-forming capacity, required for the formation of the cyst coat. [(1->4)-beta-D-mannuronosyl](n) = [alginate](n) Inhibited by zinc. Glycan biosynthesis; alginate biosynthesis. Probably exported via the hemolysin-type secretion pathway. Produced during vegetative growth and in encysting cells. Composed of two catalytically active A modules and four R modules. The N-terminal A domain introduces a mixture of MG-blocks and G- blocks, whereas the C-terminal A domain only generates MG-blocks. Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle. Belongs to the D-mannuronate C5-epimerase family. |
Q44495 | MDYNVKDFGALGDGVSDDTAAIQAAIDAAYAAGGGTVYLPAGEYRVSGGEEPSDGCLTIKSNVHIVGAGMGETVIKLVDGWDQDVTGIVRSAYGEETSNFGMSDLTLDGNRDNTSGKVDGWFNGYIPGEDGADRDVTLERVEIREMSGYGFDPHEQTINLTIRDSVAHDNGLDGFVADFQIGGVFENNVSYNNDRHGFNIVTSTNDFVLSNNVAYGNGGAGLVVQRGSSDVAHPYDILIDGGAYYDNGLEGVQIKMAHDVTLQNAEIYGNGLYGVRVYGAEDVQILDNYIHDNSQNGSYAEILLQSYDDTAGVSGNFYTTTGTWIEGNTIVGSANSTYGIQERDDGTDYSSLYANSVSNVQNGSVRLYGANSVVSDLPGTGQQATLEGTAGNDTLGGSDAHETLLGLDGNDRLNGGAGNDILDGGAGRDNLTGGAGADLFRVSARTDSYRTDSASFNDLITDFDASQDRIDLSALGFTGLGDGYNGTLLLQVSADGSRTYLKSLEADAEGRRFEIALDGNFAGLLGAGNLLFERTAIEGDAGDNALLGTSAAETLLGHAGNDTLDGGAGDDILVGGAGRDSLTGGAGADVFRFDALSDSQRNYDIGDNQGDRIADFAVGEDKLDVSALGFTGLGDGYNGTLALVLNSAGDRTYVKSYENGADGYRFEFSLDGNYLELLGNEDFIFATPSGQQLLEGSAGNDSLQGTAADEVIHGGGGRDTLAGGAGADVFRFSELTDSYRDSASYADLITDFDASEDRIDLSGLGFSGLGNGYGGTLALQVNSAGTRTYLKSFETNAAGERFEIALDGDLSALGGANLILDARTVLAGGDGNDTLSGSSAAEELLGGVGNDSLDGGAGNDILDGGAGRDTLSGGSGSDIFRFGGALDSFRNYASGTNGTDSITDFTPGEDLIDLSVLGYTGLGDGYNGTLAIVLNDAGTKTYLKNRESDAEGNQFEIALEGNHADQLDASDFIFATAAATTGIEVVGGSGTQTDQLA | Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), producing a polymer with gel-forming capacity, required for the formation of the cyst coat. [(1->4)-beta-D-mannuronosyl](n) = [alginate](n) Inhibited by zinc. Glycan biosynthesis; alginate biosynthesis. Probably exported via the hemolysin-type secretion pathway. Produced mainly in encysting cells. Composed of one catalytically active A module and four R modules. Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle. Belongs to the D-mannuronate C5-epimerase family. |
Q44496 | MDFNVKDFGALGDGASDDTAAIQAAIDAAHAAGGGTVYLPAGEYRVSGGEEPSDGALTIKSNVYIVGAGMGETVIKMVDGWTQNVTGMVRSAYGEETSNFGMSDLTLDGNRDNLSAKVDGWFNGYIPGQDGADRDVTLERVEIREMSGYGFDPHEQTINLTIRDSVAHDNGLDGFVADYQVGGVFENNVSYNNDRHGFNIVTSTNDFVLSNNVAYGNGGAGLVVQRGSYDLPHPYDILIDGGAYYDNALEGVQLKMTHDVTLQNAEIYGNGLYGVRVYGAQDVQLLDNQIHDNSQNGAYAEVLLQSYDDTAGVSGNFYVTTGTWLEGNVISGSANSTFGIQERADGTDYSSLYANTIDGVQNGTVRLYGANSTVSEQPSSGQQATLEGTAGNDVLSGTGAHELILGLAGNDRLDGGAGDDTLDGGAGRDTLTGGAGADTFRFSAREDSHRTDSASFTDLITDFDASQDRIDLSALGFTGLGNGYDGTLAVTTGSGGTRTYLKSYEVDAQGRRFEIALDGNFVGQFNDGNLLFDAAPVTGTEGNDNLSGTDAGETLLGYGGNDTLNGGAGNDILVGGAGRDTLTGGAGADVFRFEALSDSQRNYTAGDNQGDYIIDFAVGEDRIDVSALGYTGLGNGRNGTLAVVLNSAGDRTYVKSYDTDANGYNFELSLAGNYQGLLGAEQFVFATPPEQATIEGTDGNDSLQGTGADELLLGLGGRDSLNGGAGDDVLDGGAERDTLTGGTGADTFLFSARTDSYRTDSASFTDLITDFDPAQDRIDLSGLGFSGFGNGYDGTLLLQVNAAGTRTYLKSLEADADGQRFEIALDGDFSGQLDSGNVIFEAGVFNAKDFGALGDGASDDRPAIQAAIDAAYAAGGGTVYLPAGEYRVSPTGDPGDGCLMLKDGVYLVGAGMGETVIKLIDGSDQKITGMVRSAYGEETSNFGMSDLTLDGNRDNTSGKVDGWFNGYIPGQDGADRNVTLERVEIREMSGYGFDPHEQTINLTIRDSVAHDNGLDGFVADYLVDSVFENNVAYNNDRHGFNVVTSTYDFTLSNNVAYGNGGAGLVIQRGAEDLAQPTDILIDGGAYYDNALEGVLLKMTNNITLQNAEIYGNGYSGVRLYGTEDVQILNNQIHDNAQNVAYAEVLLQSFNDVGVSGNFYATTGTWIEGNVISGSANSTYGIEERNDGTDYSSLYANTIDGVQTGAVRLNGAHSIVSDQPGTGQQATLEGTTGNDTLGGSDAHETLLGLDGDDRLDGGAGNDILDGGVGRDTLTGGAGADTFRFSAREDSYRTASTSFTDLITDFDPAQDRIDLSALGFTGLGDGYDGTLLVTTGSGGSRTYLKSLEADAEGRRFEIALDGDFVGLLDASNLIFERPAIEGDAGDNALLGTSVAETLLGHAGNDTLDGAGGDDILVGGAGSDSLTGGAGADVFRFDALSDSQRNYDTGDNQGDRITDFAVGEDKLDVSALGFTGLGDGYNGTLVLVLNSAGDRTYVKSYENGADGYRFEFSLDGNYQGLLGNEDFIFATPSGQQLLEGTAGNDSLQGTAADEVIHGGSGRDTLAGGAGADVFRFSELTDSYRTDSASYADLITDFDASEDRIDLSGLGFSGLGNGYGGTLALQVNSAGTRTYLKSYEANAAGERFELSLDGDLSGLDESHLVFDERVVLAGGDGNDTLSGGSAAEELLGGAGNDSLSGGAGNDILDGGAGRDTLSGGSGSDIFRFGDALDSFRNYNSGANVTDSIADFTHGADLIDLSALGYTGLGDGYNGTLAIVLNDAGTKTYLKDRGGDAEGNRFEIALEGNHADQLDASDFIFATAAAATGIEVVGSTPAEEQPVV | Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), producing a polymer with gel-forming capacity, required for the formation of the cyst coat. [(1->4)-beta-D-mannuronosyl](n) = [alginate](n) Inhibited by zinc. Glycan biosynthesis; alginate biosynthesis. Probably exported via the hemolysin-type secretion pathway. Composed of two catalytically active A modules and four R modules. The N-terminal A domain introduces a mixture of MG-blocks and G-blocks, whereas the C-terminal A domain only generates MG-blocks. Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle. Belongs to the D-mannuronate C5-epimerase family. |
Q44493 | MDYNVKDFGALGDGVSDDRASIQAAIDAAYAAGGGTVYLPAGEYRVSAAGEPGDGCLMLKDGVYLAGAGMGETVIKLIDGSDQKITGMVRSAYGEETSNFGMRDLTLDGNRDNTSGKVDGWFNGYIPGGDGADRDVTIERVEVREMSGYGFDPHEQTINLTIRDSVAHDNGLDGFVADYLVDSVFENNVAYANDRHGFNVVTSTHDFVMTNNVAYGNGSSGLVVQRGLEDLALPSNILIDGGAYYDNAREGVLLKMTSDITLQNADIHGNGSSGVRVYGAQDVQILDNQIHDNAQAAAVPEVLLQSFDDTAGASGTYYTTLNTRIEGNTISGSANSTYGIQERNDGTDYSSLIDNDIAGVQQPIQLYGPHSTVSGEPGATPQQPSTGSDGEPLVGGDTDDQLQGGSGADRLDGGAGDDILDGGAGRDRLSGGAGADTFVFSAREDSYRTDTAVFNDLILDFEASEDRIDLSALGFSGLGDGYGGTLLLKTNAEGTRTYLKSFEADAEGRRFEVALDGDHTGDLSAANVVFAATGTTTELEVLGDSGTQAGAIV | Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), but introduces almost exclusively MG blocks, producing a polymer with non-gel-forming capacity. [(1->4)-beta-D-mannuronosyl](n) = [alginate](n) Inhibited by zinc. kcat is 14 sec(-1). Optimum pH is 6.5-7.0. Optimum temperature is 37 degrees Celsius. Glycan biosynthesis; alginate biosynthesis. Probably exported via the hemolysin-type secretion pathway. Produced in encysting cells. Composed of one catalytically active A module and one R module. Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle. Belongs to the D-mannuronate C5-epimerase family. |
Q44492 | MDYNVKDFGALGDGVSDDTAAIQAAIDAAYAAGGGTVYLPAGEYRVSGGEEPSDGCLTIKSNVYIVGAGMGETVIKLVDGWDQDVTGIVRSAYGEETSNFGMSDLTLDGNRDNTSGKVDGWFNGYIPGEDGADRDVTLERVEIREMSGYGFDPHEQTINLTIRDSVAHDNGLDGFVADFQIGGVFENNVSYNNDRHGFNIVTSTNDFVLSNNVAYGNGGAGLVIQRGSYDVAHPYGILIDGGAYYDNGLEGVQIKMAHDVTLQNAEIYGNGLYGVRVYGAEDVQILDNYIHDNSQSGSYAEILLQSYDDTAGVSGNFYTTTGTWIEGNTIVGSANSTYGIQERADGTDYSSLYANSVSNVQSGSVRLYGTNSVVSDLPGTGQQATLEGTTGNDTLTGSEAHETLLGLDGNDRLNGGAGNDILDGGAGRDNLTGGAGADLFRVSARTDSYRTDSASFNDLITDFDPAQDRIDLSALGFTGLGDGYNGTLAVVLNSAGTRTYLKSYEADAEGRRFEIALDGNFAGLLDDGNLIFERPVIEGDAGNNALLGTSAAETLLGHAGNDTLDGAGGDDILVGGAGRDTLTGGAGADLFRFDALSDSQRNYTTGDNQGDRIVDFSVGEDKLDVSALGFTGLGDGYNGTLAVVVNSAGDRTYVKSYETDADGYRFEFSLEGNYQDLGSESFVFATPSGQQLLEGSAGNDSLQGTAADEIVHGGAGRDTLSGGAGADVFRFSELTDSYRTASTSFADLITDFDLADDRIDLSGLGFSGLGDGYDGTLAVVVNSTGTRTYLKSYEANAAGERFEIALDGDLSAFTGANLILDERVVLEGSDGNDTLDGGSAAEELLGGAGNDSLDGGAGNDILDGGAGRDTLSGGSGSDIFRYDDALDSFRNYGTGVTGTDTITDFTPGEDLIDLSALGYTGLGDGYNGTLAVVLNGDGTRTYLKDRESDAEGNQFEIALDGDLVDRLDAGDFIFAEAAATTAIEVVGGTPTEEQLVA | Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), producing a polymer with gel-forming capacity, required for the formation of the cyst coat. [(1->4)-beta-D-mannuronosyl](n) = [alginate](n) Inhibited by zinc. Glycan biosynthesis; alginate biosynthesis. Probably exported via the hemolysin-type secretion pathway. Produced during vegetative growth and in encysting cells. Composed of one catalytically active A module and four R modules. Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle. Belongs to the D-mannuronate C5-epimerase family. |
Q9ZFH0 | MDYNVKDFGALGDGVSDDRVAIQAAIDAAHAAGGGTVYLPPGEYRVSAAGEPSDGCLTLRDNVYLAGAGMGQTVIKLVDGSAQKITGIVRSPFGEETSNFGMRDLTLDGNRANTVDKVDGWFNGYAPGQPGADRNVTIERVEVREMSGYGFDPHEQTINLVLRDSVAHHNGLDGFVADYQIGGTFENNVAYANDRHGFNIVTSTNDFVMRNNVAYGNGGNGLVVQRGSENLAHPENILIDGGSYYDNGLEGVLVKMSNNVTVQNADIHGNGSSGVRVYGAQGVQILGNQIHDNAKTAVAPEVLLQSYDDTLGVSGNYYTTLNTRVEGNTITGSANSTYGVQERNDGTDFSSLVGNTINGVQEAAHLYGPNSTVSGTVSAPPQGTDGNDVLIGSDVGEQISGGAGDDRLDGGAGDDLLDGGAGRDRLTGGLGADTFRFALREDSHRSPLGTFSDLILDFDPSQDKIDVSALGFIGLGNGYAGTLAVSLSADGLRTYLKSYDADAQGRSFELALDGNHAATLSAGNIVFAAATPVDPSAEAQPIVGSDLDDQLHGTLLGEEISGGGGADQLYGYGGGDLLDGGAGRDRLTGGEGADTFRFALREDSHRSAAGTFSDLILDFDPTQDKLDVSALGFTGLGNGYAGTLAVSVSDDGTRTYLKSYETDAEGRSFEVSLQGNHAAALSADNILFATPVPVDPGVEGTPVVGSDLDDELHGTLGSEQILGGGGADQLYGYAGNDLLDGGAGRDKLSGGEGADTFRFALREDSHRSPLGTFGDRILDFDPSQDRIDVSALGFSGLGNGYAGSLAVSVSDDGTRTYLKSYEADAQGLSFEVALEGDHAAALSADNIVFAATDAAAAGELGVIGASGQPDDPAV | Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), producing a polymer with gel-forming capacity, required for the formation of the cyst coat. [(1->4)-beta-D-mannuronosyl](n) = [alginate](n) Inhibited by zinc. Glycan biosynthesis; alginate biosynthesis. Probably exported via the hemolysin-type secretion pathway. Produced in encysting cells. Composed of one catalytically active A module and three R modules. Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle. Belongs to the D-mannuronate C5-epimerase family. |
Q9ZFG9 | MEYNVKDFGAKGDGKTDDTDAIQAAIDAAHKAGGGTVYLPSGEYRVSGGDEASDGALIIKSNVYIVGAGMGETVIKLVDGWDEKLTGIIRSANGEKTHDYGISDLTIDGNQDNTEGEVDGFYTGYIPGKNGADYNVTVERVEIREVSRYAFDPHEQTINLTIRDSVAHDNGKDGFVADFQIGAVFENNVSYNNGRHGFNIVTSSHDIVFTNNVAYGNGANGLVVQRGSEDRDFVYNVEIEGGSFHDNGQEGVLIKMSTDVTLQGAEIYGNGYAGVRVQGVEDVRILDNYIHDNAQSKANAEVIVESYDDRDGPSDDYYETQNVTVKGNTIVGSANSTYGIQERADGTDYTSIGNNSVSGTQRGIVQLSGTNSTFSGRSGDAYQFIDGSTGNDLLTGTPIADLIVGGSGNDTLSGDAGNDVLEGGAGSDRLTGGEGADIFRFTAVSDSYYTASSSVADQILDFDASNDRIDLTGLGFTGLGDGYGGTLAVLANSDGSRTYLRSYEKDADGRYFSLTLDGNFVGRLDDSNLVFRHKTIAGTEGDDSLTGNAMAEILDGGSGNDSLAGGLGNDVLRGGAGDDILNGGLGRDQLSGGEGADIFRFTSVADSYQNSGDNFSDLILDFDPGEDRIDLSGLGFSGLGDGHNGTLLLWTSSETNRTYLKNFDTDADGRRFEIALEGVFSDLSEKQLVFERLVLEGTRLGDQLSGTELNEELLGGAGRDILNGGAGDDILDGGSERDTLTGGSGADVFRFNATLDSFRNYDNGTSRVDDITDFTVGEDLIDLSALGYSGLGNGYDGTLAVLLNADGTKTYLKDRESDADGNHFEIALDGNYADQLSNGDFIFTNLEVIGSSSQAA | Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G). Has both epimerase and lyase activities. Contributes to abortive encystment by degrading the coat from inside the cyst. Important for cyst germination. Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end. [(1->4)-beta-D-mannuronosyl](n) = [alginate](n) Inhibited by zinc. Glycan biosynthesis; alginate biosynthesis. Probably exported via the hemolysin-type secretion pathway. Produced mainly in germinating cells. Composed of one catalytically active A module and three R modules. Each enzyme of this family of C5 epimerases introduces its own characteristic sequence distribution of G-blocks in their substrates, explaining the extensive sequence variability of alginates. These alginates of varying composition have different physical properties and are necessary at different stages of the bacterium life cycle. Belongs to the D-mannuronate C5-epimerase family. |
P94201 | MSRKQRISAGLGLGASLLCCNPLFAGPVGPDRNFGMEVKVTAQSEDDRDLDTRSGGDAEGIALDLRPWVYGQRGNWGAMVMLQAVAATDIIETDPTDPNEEPGGDPANGFSRDSSRDPDKSYLALREFELGTIGRQRIRSLTNEGTWWDIHMESVNWTMDTSLLRAQAGVAKRFDEYRTDLDNLSAEDKDRTHVFGGLDYQWRQGHWAGFKVHHTSDDGDLPDSQMDVYEDRQSKSYTGDLTWLSVHLDRDFFNPRSTLPINYWGEFTWLTGEMDRSHFASDGSADHYKDVDVDAWAVDLGLRWNISDRWNVGAAYARGQAGEGDDESEQFMQTGLQSNRSTFTGLQTRIHRFGEASRGELTNLQVGTLFTSWKPREDLETSLIYHKFWRVDDDEDLGQNGISPIEKDGKPALKAGEKDLGQEVDLIITRYFNQGMLPANWGGELDEQSALIRLRSGLFFPSNAYASKGDSKMHRVFVDMIWRF | Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore. Glycan biosynthesis; alginate biosynthesis. Belongs to the AlgE family. |
P18895 | MNSSRSVNPRPSFAPRALSLAIALLLGAPAFAANSGEAPKNFGLDVKITGESENDRDLGTAPGGTLNDIGIDLRPWAFGQWGDWSAYFMGQAVAATDTIETDTLQSDTDDGNNSRNDGREPDKSYLAAREFWVDYAGLTAYPGEHLRFGRQRLREDSGQWQDTNIEALNWSFETTLLNAHAGVAQRFSEYRTDLDELAPEDKDRTHVFGDISTQWAPHHRIGVRIHHADDSGHLRRPGEEVDNLDKTYTGQLTWLGIEATGDAYNYRSSMPLNYWASATWLTGDRDNLTTTTVDDRRIATGKQSGDVNAFGVDLGLRWNIDEQWKAGVGYARGSGGGKDGEEQFQQTGLESNRSNFTGTRSRVHRFGEAFRGELSNLQAATLFGSWQLREDYDASLVYHKFWRVDDDSDIGTSGINAALQPGEKDIGQELDLVVTKYFKQGLLPASMSQYVDEPSALIRFRGGLFKPGDAYGPGTDSTMHRAFVDFIWRF | Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore. Glycan biosynthesis; alginate biosynthesis. Belongs to the AlgE family. |
Q88NC8 | MTLNPFVKAGIGLSFALLWSCPTLAEMTAEKNFGLDVKITGQSEDDRDLGTRSGGDVNGLGLDLRPWVYGERGNWSAYAMGQAVAATDTIETDTLRQNDDGTSTDTGDDSRQPDKSYLAMREFWVGYSGLTAYPGEQLRFGRQRLRSDDGMWRDTNIEALNWTFDTTLLKADLGVAQRFSEYRTDLTELAPEDKDRTHIYGNVATQWTPGHWVGLRAHHTHDSGSLKNPGETVDALDKTRTGDLTWLGLEANSDAYNWRNDHTVNYWGSVTWLTGDRDKLSTQQVGDDQVATGKQSGDVNAWATDLGIRLRLDPQWQVGAAYARGSGGGGDDGSNNFEQTGLESNRSNFTGTRSRVHRFGEAFRGELGNLQAATLFASWQLRDDYDASLIYHKFWRVDGNQNIGSSGINAVVDDNGVNRQLVDGEKDLGQEMDVVVTKYFKQGLLPASMSQAIDEPSALVRLRAGVFKPGDAYGKETDSYMHRAFVDVIWRF | Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore. Glycan biosynthesis; alginate biosynthesis. Belongs to the AlgE family. |
P14004 | MKFIIAFFVATLAVMTVSGEDKKHDYQNEFDFLLMERIHEQIKKGELALFYLQEQINHFEEKPTKEMKDKIVAEMDTIIAMIDGVRGVLDRLMQRKDLDIFEQYNLEMAKKSGDILERDLKKEEARVKKIEV | Monomer. Trimer of homodimers. Oligomerizes in a concentration-dependent manner. Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. Binds to IgE in patients allergic to house dust mite (HDM) (PubMed:7798547, PubMed:2794865, PubMed:18445190, PubMed:24874917, PubMed:29319884, PubMed:20534590). Recombinant protein binds to IgE in 52% of the 25 patients tested (PubMed:7798547). Recombinant protein binds to IgE in 31% of the 117 patients tested living in urban area in Austria allergic to European HDM (PubMed:18445190). Recombinant protein binds to IgE in 69% of the 96 patients tested living in Bangkok allergic to European HDM (PubMed:24874917). Recombinant protein of 34-132 binds to IgE in 35% of the 62 patients tested (PubMed:20534590). In the skin tests, the recombinant protein produces positive reactions in 67% of the 15 patients tested with asthma and allergic rhinitis, in 58% of the 13 patients tested with asthma alone and in 29% of the 17 patients tested with allergic rhinitis alone (PubMed:7798547). No relevant cross-reactivity with Der p 21 allergen (PubMed:29319884). Causes histamine release from human peripheral blood mononuclear leukocytes. Up-regulates expression of CD203c activation marker on basophils (PubMed:18445190). Non-allergenic peptides identified from the mapped major conformational IgE epitope-containing areas could be used for the engineering of house dust mite allergy vaccine. Belongs to the mite group 5 allergen family. Extended N-terminus. |
Q39967 | MASVEVESAATALPKNETPEVTKAEETKTEEPAAPPASEQETADATPEKEEPTAAPAEPEAPAPETEKAEEVEKIEKTEEPAPEADQTTPEEKPAEPEPVAEEEPKHETKETETEAPAAPAEGEKPAEEEKPITEAAETATTEVPVEKTEE | The N-terminus is blocked. Causes an allergic reaction in human. Major latex allergen, a major cause of anaphylaxis in susceptible individuals, especially health care workers. 92% of health care workers with latex allergy have IgE specific to the Hev b 5 protein. To kiwi fruit protein PKIWI501. |
Q9U5P2 | DDFRNEFDRLLIHMTEEQFAKLEQALAHLSHQVTELEKSKSKELKAQILREISIGLDFIDSAKGHFERELKRADLNLAEKFNFESALSTGAVLHKDLTALATKVKAIETK | Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. Belongs to the mite group 5 allergen family. |
A0A2R4SV19 | MPRLVLVSFLFLAIFSVFIGGFAKSKCPRNEIFTRCHAACQPSCARLARKPFCIKICKPGCICTSGYLRNKNNVCVPRSRCFSGRLL | Antifibrinolytic and antimicrobial serine protease inhibitor. Inhibits trypsin, plasmin and microbial serine proteases but not chymotrypsin, thrombin and elastase. Inhibits the plasmin-mediated degradation of fibrin to fibrin degradation products. Also binds to bacterial and fungal surfaces and exhibits antimicrobial activity against fungi as well as Gram-positive and Gram-negative bacteria. Specifically expressed by the venom gland. Belongs to the serine protease inhibitor-like (TIL domain-containing) family. |
Q27SJ8 | MSRLVLASFLLLAIFSMLVGGFGGFGGFGGLGGRGKCPSNEIFSRCDGRCQRFCPNVVPKPLCIKICAPGCVCRLGYLRNKKKVCVPRSKCG | May act as a protease inhibitor. Expressed by the venom gland. in Api m 6.01. in Api m 6.02. in Api m 6.03. in Api m 6.04. Causes an allergic reaction in human (PubMed:11344362, PubMed:23397669). Binds to IgE (42% responsiveness) (PubMed:11344362, PubMed:23397669). Belongs to the serine protease inhibitor-like (TIL domain-containing) family. Four isoforms exist; 6.01 (without 4 N-ter AA and 2 extra C-ter AA), 6.02 (without 4 N-ter AA but with 2 extra C-ter AA), 6.03 (with 4 N-ter AA but without 2 extra C-ter AA) and 6.04 (with 4 N-ter AA and with 2 extra C-ter AA) (PubMed:17069633, PubMed:11344362). The sequence displayed corresponds to isoform 6.03. It is unknown if the variants api m 6.01 and api m 6.02 (without 4 N-ter AA) are the result of different transcript, an alternative splicing, or an enzymatic cleavage. |
P82157 | LPLYNFGL | Belongs to the allatostatin family. |
Q84UC2 | DEAQFKECYDTCHKECSDKGNGFTFCEMKCDTDCSVKDVKEKLENYKPKN | Expressed in pollen. Causes an allergic reaction in human. Major allergen from olive pollen. |
D4B2H3 | MAPQFLKALTVATALGATLATALPVQPKPTVWHTTTQVVVKTITKTATVHGTPGPDYTVPPAYTTPAAPTVPTDAPQQPSYTPVPSAPTPSSSSSYSAPAEPSSSSVPAPPPPPPTTTSTPAPEPTTSTTPPPPPPAMTTPPPPPPPPATKPPVVSIPPIGGGGSTYTGPCAAGSPCTGEITFYDGGLGACGTNIDTNGEDAIALPIELMGPLSNNNPYCGKQVQISYKGKTATATVKDKCAGCTGNNIDMTRFLFYKLIRFPVAFTNSSNSGVEADGRIHGVEWHFI | May cause an allergic reaction in human. |
Q4WNR3 | MAPIFKSLALVSALFAAISSAAPVNLDKREVDVVWTTVTTVVWTTIDVTTTIYPTPQAPTPPVVESTPTPTPSAAPEQAEPIETSTQPETTKSQPTQPSVATFIPVAAAAAAADSAAPIPEEPAPQPATTAAPSTSTTTQAAPSAPPAANSGSTEKAASSGYSGPCSKGSPCVGQLTYYDTATSASAPSSCGLTNDGFSENVVALPVGIMTDADCGKTVTITYNGITKTATVVDKCMGCKPTDLDASRHLFGELADFSAGRIDGMSWYFN | Causes an allergic reaction in human. |
P81810 | ASPYAFGL | May act as a neurotransmitter or neuromodulator. Belongs to the allatostatin family. |
P82158 | KMYDFGL | Belongs to the allatostatin family. |
Q26456 | MMKFLLIAAVAFVAVSADPIHYDKITEEINKAIDDAIAAIEQSETIDPMKVPDHADKFERHVGIVDFKGELAMRNIEARGLKQMKRQGDANVKGEEGIVKAHLLIGVHDDIVSMEYDLAYKLGDLHPTTHVISDIQDFVVALSLEISDEGNITMTSFEVRQFANVVNHIGGLSILDPIFGVLSDVLTAIFQDTVRKEMTKVLAPAFKRELEKN | Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. Belongs to the mite group 7 allergen family. |
P49273 | MMKLLLIAAAAFVAVSADPIHYDKITEEINKAVDEAVAAIEKSETFDPMKVPDHSDKFERHIGIIDLKGELDMRNIQVRGLKQMKRVGDANVKSEDGVVKAHLLVGVHDDVVSMEYDLAYKLGDLHPNTHVISDIQDFVVELSLEVSEEGNMTLTSFEVRQFANVVNHIGGLSILDPIFAVLSDVLTAIFQDTVRAEMTKVLAPAFKKELERNNQ | Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. Belongs to the mite group 7 allergen family. |
Q9U1G2 | MQYLAIAVIVALAGLSAAAHKPAYYDDNMANQMVDQIVKSLTTKKELDPFKIEQTKVPIDKKIGLIHIKGSATIKNAVITGLSHISRRGDAKIDTDGGAFAATLKLGDKNIRIKTDLHLDLGKIIHPNLKFEGHIGDIDMKLKLKLDAEGKPSLDQFEIDEFEQVELFIHGLGPLDPLVDVIADSFVKYFNPQARKLVTDMLKPILVEEIKKLKLN | Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. Belongs to the mite group 7 allergen family. |
P81430 | APSQSTVTALLTSCVSYIDDQ | Many isoforms of the allergen exist due to polymorphism. They can be classified as isoforms of type A (shown here) and isoforms of type B. A microheterogeneity is detected at positions 4 and 11 of isoforms of type A and at positions 4, 5, 10 and 11 of isoforms of type B. Causes an allergic reaction in human. Allergen from olive pollen. Important in Mediterranean countries and California. Its prevalence is related to the geographic area. |
P81811 | AGPYAFGL | May act as a neurotransmitter or neuromodulator. Belongs to the allatostatin family. |
Q9M7Q9 | MAANTDRNSKPSVYLQEPNEVQGVFNRFDANGDGKISGDELAGVLKALGSNTSKEEIGRIMEEIDTDKDGFINVQEFAAFVKAETDPYPSSGGENELKEAFELYDQDHNGLISSVELHKILTRLGERYAEHDCVEMIKSVDSDGDGYVSFEEFKKMMTNKSGNNSQAEPPK | Homodimer. Expressed in pollen. Several isoforms of the allergen exist due to polymorphism. Causes an allergic reaction in human. |
P81812 | GGPYAFGL | May act as a neurotransmitter or neuromodulator. Belongs to the allatostatin family. |
Q94G86 | MAANVQTSSLLFLVFLLLQNFYSANSQSFLGVNYGQLSDNLPSLQATVNLLKSTTIQKVRLFGAEPAVIKAFANTGVEIVIGFDNGDIPTLASNPNVASQFVKSNVMSFYPASNIIAITVGNEVLTSGDQKLISQLLPAMQNVQNALNAASLGGKVKVSTVHAMAVLSQSYPPSSGVFNPGLGDTMKALLQFQSANDAPFMISPYPYFAYKNQPTPDTLAFCLFQPNAGQVDSGNGHKYTNMFDAQVDAVHSALNAMGFKDIEIVVAETGWPHGGDSNEVGPSLDNAKAYVGNLINHLKSKVGTPLMPGKSIDTYLFSLYDEDKKTGASSEKYFGLFKPDGSTTYDVGLLKNTQNPTTPATPTPTPKAAGSWCVPKPGVSDDQLTGNINYACGQGIDCGPIQPGGACFEPNTVKAHAAYVMNLYYQSAGRNSWNCDFSQTATLTNTNPSYGACNFPSGSN | Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. Optimum pH is 4.5-6.0. Homodimer. Expressed only in pollen. The N-terminal region (1-350) contains the enzymatic activity while the C-terminal region (360-460) can bind laminarin. Both regions are allergenic by themselves. Glycosylated. Contains two additional disulfide bonds, but it is unclear if they are between the pairs Cys-392-Cys-398 and Cys-407-Cys-453 (PudMed:18096638) or between the pairs Cys-392-Cys-453 and Cys-398-Cys-407 (PudMed:12392450). Causes an allergic reaction in human. Major allergen from olive pollen. Important in Mediterranean countries. Belongs to the glycosyl hydrolase 17 family. The sequences determined for the two internal peptides of Ole e 4 are identical to internal fragments of Ole e 9. However, the apparent molecular weight of the two proteins is different and they are still classified as two separate allergens (PubMed:22385802), even though we may be facing two different isoforms of the same allergen. |
B3EWI2 | ARPYSFGL | May act as a neurotransmitter or neuromodulator. In larvae, expressed in the CNS and midgut but not in the ring gland, thoracic perisymapthetic organs (tPSO) or abdominal perisymapthetic organs (aPSO) (at protein level). In adults, expressed in the corpora cardiaca, corpora allata, brain and the thoracic-abdominal ganglion (at protein level). Detected in larvae and adults. Belongs to the allatostatin family. |
B1XGB0 | MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
A7ZXG5 | MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKSEGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHICHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDAEFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
A1A8H7 | MSFDLIIKNGTVILENEARVVDIAVKDGKIAAIGQDLGDAKDVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
Q0TKD0 | MSFDLIIKNGTVILENEARVVDIAVKDGKIAAIGQDLGDAKDVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
Q8FK60 | MSFDLIIKNGTVILENEARVVDIAVKDGKIAAIGQDLGDAKDVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B1IZ89 | MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKSEGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHICHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
Q2MBR6 | MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Can also use Ni(2+), Co(2+) or Mn(2+). Severely inhibited by copper, and competitively inhibited by dithiothreitol (DTT). Zinc concentrations above 2.5 mM and cobalt or nickel concentrations above 1 mM are inhibitors. Optimum pH is 7.5-8.0. The optimal activity is at pH 8.8 for zinc-containing form and pH 9.0 for cobalt-containing form. Optimum temperature is 40-45 degrees Celsius. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. By glyoxylate. Carboxylation allows a single lysine to coordinate two zinc ions. The zinc-containing form utilizes only the (S)-isomer of allantoin, whereas the cobalt-containing form prefers the (S)-isomer, but also hydrolyzes the (R)-isomer at about 1/10 the rate. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B7N966 | MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKSEGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHICHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTEQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B6I0G2 | MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B1LKD0 | MSFDLIIKNGTVILENEARVVDVAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
Q1RF23 | MSFDLIIKNGTVILENEARVVDIAVKDGKIAAIGQDLGDAKDVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
Q82ZQ1 | MQAELVIKNGLVILETGEVITDVAVQGGKIVAIGQDLSGERVIDATGLVVSPGMVDAHVHITDPGGGYRDEWEGYVTGTAACAKGGVTTFMEMPLNQIPATVDKTSLEIKYKAGENKLKVDVGSFGGVVPTNLADGIQELDEGGVSGYKCFLGTCGDRSIEGDFQNVDDYSLYEGMKQVAKTGKVLAIHAENAPITDKLGAVAYQNGETTLAAYVATRPVFTEVEAIQKAILFAKETGCRIHICHVACQEGVEEVLKAQAEGVDVTCETCTHYLYFTTDELDAIGPVVKCSPPIRDADQQAALWNHVQTGGIAFVTSDHSPCTPDLKDTTNAFEAWGGISGVQNNVDVLFDEAVQKRGLSLKQFADMIAANPADRYHLAQKGRISIGKDADFVLIKPNAPYILKAEDLEYRNKISPYIGREIGAQVIQTILRGETIYAQETGVTEAFNGVFIKN | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
Q1AS71 | MSAFDLIVRGGTVVRGGCEVADVGVADGVISAVGPDLEGGAREEIDARGLLVLPGAIDAHVHFNEPGRTRWEGFASGTRALAAGGTTLCVEMPLNAHPPTTDGESFDLKLAAAKASAHVDFALWGGIVPGRVGRMEELAGRGVAGFKAFMSATGTPDFEAADDLTLYEGMQEAARLGLPVLVHAENRQITDALARRATSALRTTMRDYLASRPAVAELEAIGRAILLASEAGCSLHIVHVSTGRGVALVAAARERGVDVTCETCPHYLLFTDEDAVRIGAAAKCAPPLRPREEVESLWEQVLAGNVAFVTSDHSPCPPDMKAGEDMFRAWGGISGCQSLLPALLDEGYHGRGLPPERLAELLSANVARRFGFAGKGGIEEGNDADLALVDPSGEHVLREEDLHYRHPISPYVGRSFRGRVVRTILRGRTVFEGGRVVSGPAGRFVRPQREKGER | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B5EYC3 | MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
Q57S43 | MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLEEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B5FLN3 | MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B5QUT6 | MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B5R646 | MSFDLIIKNGTVILENEARVIDIAAQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEVQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B4T9L5 | MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
B4SXM8 | MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (S)-allantoin + H2O = allantoate + H(+) Binds 2 Zn(2+) ions per subunit. Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family. |
O42618 | MSTIPFRKNYVFKNWAGIYSAKPERYFQPSSIDEVVELVKSARLAEKSLVTVGSGHSPSNMCVTDEWLVNLDRLDKVQKFVEYPELHYADVTVDAGMRLYQLNEFLGAKGYSIQNLGSISEQSVAGIISTGSHGSSPYHGLISSQYVNLTIVNGKGELKFLDAENDPEVFKAALLSVGKIGIIVSATIRVVPGFNIKSTQEVITFENLLKQWDTLWTSSEFIRVWWYPYTRKCVLWRGNKTTDAQNGPAKSWWGTKLGRFFYETLLWISTKIYAPLTPFVEKFVFNRQYGKLEKSSTGDVNVTDSISGFNMDCLFSQFVDEWGCPMDNGLEVLRSLDHSIAQAAINKEFYVHVPMEVRCSNTTLPSEPLDTSKRTNTSPGPVYGNVCRPFLDNTPSHCRFAPLENVTNSQLTLYINATIYRPFGCNTPIHKWFTLFENTMMVAGGKPHWAKNFLGSTTLAAGPVKKDTDYDDFEMRGMALKVEEWYGEDLKKFRKIRKEQDPDNVFLANKQWAIINGIIDPSELSD | Can oxidize L-gulono-1,4-lactone as well as D-arabinono-1,4-lactone and L-galactono-1,4-lactone. D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H(+) + H2O2 Cofactor biosynthesis; D-erythroascorbate biosynthesis; dehydro-D-arabinono-1,4-lactone from D-arabinose: step 2/2. Monomer. Membrane-embedded. The N-terminus is blocked. Present with 6190 molecules/cell in log phase SD medium. Belongs to the oxygen-dependent FAD-linked oxidoreductase family. |
Q9UTM6 | MNEITLFIKSSSANAERRINPQWTVSQLKTKLVPIVGTPEQYQKLTYEPASSTVPGHVFTSEEENLDLGEFKLQPLGTIVVEDTRPPHLRLDFDDLSQVDKYVMPREQYENRTDSVYAWKKRNQLGRFNPDFEASKASRQESLKRELVDLQKNLNSRCCAAGERYGTIRYIGLVPEINNDNLWVGVEFDEPVGKNDGTVSGKRYFNAKNKHGSFLRSSEVEVGDFPPEDILEGL | Required for microtubule function and cell polarity. Involved in the proper folding of alpha-tubulin. Binds to monomeric alpha-tubulin. Interacts with alp21. Belongs to the TBCB family. |
O94534 | MSQDQEEDYSKLPLESRIVHKVWKVRLSAYEECSKSFSLSADGSDNCFELWNNQSELWKSVLTDSNVAAQEAGTAAFVAYCRFSDPSHLLKAREISVLSISEKCLTSPRAGTRENALEALMLLVEADSAAPVIESIIPSLSARSPKVIASNVAAIASLVEQFGAKVIPSKMIIPHISNLFGHADKNVRKEASRLTVNIYRWTGDPLKDLLFKDLRPVQTKELESLFAELPTEPPKQTRFLKSQQPTSEPNVETQVEEQPALENEESEPEPSDDQFDLVEEVDVLPNVDPNLETLMASSKWKDRKEALDKLLPVLSQPKIKDNDFFNLVAILTKSVSKDANIMVVINAAHCIQAMAKGLRSNFSKYASTSINALLERSKEKKANVIESLSSAMDAVLATSSLDDLAELIASFAGNKNPQIKSSCFSLFSRSFSNMTSLPSKFTVDTCAKACVPGVSDTFEPVRSAAAEALGVLMKLVGERAINQYLSPLDDIRKSKIRSFYETATVKAKAPTKKSKVKPSKQEESKVVVPSNAKAVKKSVVPSSPVVPSPRKATNKSLSMDVSKGNAFENGPLLPRPTTRPVSRGLSRGTSSSLQQKVKASTPLNSGALNETVQNLKNMELDDPAPQPAKHSRVDRYEHPKVLEDNDSTISSLESLKRENEELREQLKVEHEENISMQKQLSELKGELNTLRSARKASPIGDRKPAFMRRANTDFLELSTSPSFQRSVREFEPTRPKLYSSIDVNQRSPLASAKTNGNFTFHAELPRSPFSSRANNINPDWTKAIDLAAKLKQKITEMKQTDQRHQGLIH | Required for bipolar spindle formation and proper chromosome segregation. Has a role in connecting the kinetochores and the plus end of pole to chromosome microtubules. Also required for the activation of the spindle checkpoint pathway. Interacts with alp14. Kinetochore periphery. Spindle localization is alp7-dependent. Belongs to the TOG/XMAP215 family. |
P87244 | MDGIMKNDLLWFGNHVFDLTPNSFDSDFVEQLSKFEGKEGLKRKLFDSSEYFQNFSFQVNDDLLGKDVILDISNQQLTPAVPGCETSSNSKLISASKEITSERKRAKSSVSPSYLTDSSPSDLSVENKVLLTCPSWDGENFKNLEARSPFISEAPSRVYDYFLHNQDWSPKPLFSALQVYPLATIFNCVAGLPQGFESTVFPWNKTSSTFELDPTISVSGMSDECFASIVQKFSAIGGLIKKALNEFSLYKTNISFYLSNFIVNGVLQYRKEFQRWLRLYEFRRFGLIGLSNFVNSFSSFFELISHFLIKSAQNLKGDSLLDFLFDYARSCQNTISYPIALQCLIYCSNPYFKRLELALKVSCAYGHIDSSLFLSLPRFFPSELCVSIEQCIQFLSLIREQKEIFNKNNKEFINPLNIRFAYSFNDINQACVIEERCNFSSLSFGNLEQTSVNNDSEEFETLLAKMNMTPDFNDNLLQLKFTDDVRNVCPLNLNVCCCIAEPIQSFILSFLRSTYKVLKNDFQVFDLLNFFHSTFLFQNYEFSDNVISLLKSRRLDKSDRNELAEDLNSDDRYNFISRLKKFIFMEKEKNGLSRSLSKSITFTLDSASVSEFEDVYPDLQFQCQVIGALRILFTDNSLNYYSKTFSYVLHLFQAQSDFESSVELKDRSIVTKTTIMSWSKYQGTKESLFQFLSIYIPECMLPFTKLLKSIYSPDCPTNIQNSAIKNAASVHEQCTKAIYQKVKELFDTMKLWESSIKVS | Component of the gamma tubule complex that is required for the regulation of both interphase microtubules and mitotic bipolar spindles. Interacts with gamma-tubulin. And the microtubule organizing center (MTOC). |
Q9M1W3 | MAPVKQKKKNKKKPLDKAKKLAKNKEKKRVNAVPLDPEAIDCDWWDTFWLRNSSPSVPSDEDYAFKHFFRASKTTFSYICSLVREDLISRPPSGLINIEGRLLSVEKQVAIALRRLASGDSQVSVGAAFGVGQSTVSQVTWRFIEALEERAKHHLRWPDSDRIEEIKSKFEEMYGLPNCCGAIDTTHIIMTLPAVQASDDWCDQEKNYSMFLQGVFDHEMRFLNMVTGWPGGMTVSKLLKFSGFFKLCENAQILDGNPKTLSQGAQIREYVVGGISYPLLPWLITPHDSDHPSDSMVAFNERHEKVRSVAATAFQQLKGSWRILSKVMWRPDRRKLPSIILVCCLLHNIIIDCGDYLQEDVPLSGHHDSGYADRYCKQTEPLGSELRGCLTEHLLR | Transposase-derived protein that may have nuclease activity (Probable). Antagonist of polycomb-group (PcG) protein-mediated chromatin silencing, probably by preventing the association of POLYCOMB REPRESSIVE COMPLEX 2 (PRC2) with its accessory components. Needed for full reactivation of several floral homeotic genes that are repressed by PcG (PubMed:26642436). Interacts with core components of POLYCOMB REPRESSIVE COMPLEX 2 (PRC2), a PcG protein complex with H3K27me3 histone methyltransferase activity. Associates with plant-specific PRC2 accessory components such as MSI1, EMF2, VRN2, FIE and CLF. Expressed in roots, inflorescence stems, seedlings, leaves, flower buds, inflorescences, and siliques. Suppression of PcG defects in several PRC1 and PRC2 components including lhp1 (in alp1-2 and alp1-3 mutants) and clf (in alp1-3 and alp1-4 mutants) phenotypes (PubMed:26642436, PubMed:22837357). In alp1-4, weak downward curling and slightly late flowering in short days. Increases synergistically ult1 and ult2 floral organ defects in double mutants alp1-3 ult1 and alp1-3 ult2. The double mutant alp1-3 efs has a stronger dwarf, branched phenotype than efs single mutant (PubMed:26642436). Belongs to the HARBI1 family. |
P78749 | MEEEESLEGIISIDESLITSRLSQILDDVLDDRSSSHSVEKLKDVAVKYLQFCQFQPTLLDKLLSKYVPNLASYLLKVKNIGKCNSITVILYQFCKIRGYKAVRVLFPVGVQYIKELYTLLNESSNNTWHFHYIVLLWLSQALNTPFPLNSLDDSLDVKKTIYTIAIKYLENSGIDKEASCLVLSRLFSRDDGLDLLLGFLHHCESSWFKRSIFYKIGCLFSLSSFLKICPRNDCLQTVDVAFQFLNVAREDLVGQENSALRKLLCKCYTRLGIVLLPVNSSPNWKYSISNPDSFFQLPDDSNEEVHIYLEVIVDFLLSSVSDIDSFVRWSAAKGLAKIISRLPWNLAEQVIDAIIELMTENMFLNPIENTVNISITSPLVWHGAILFFAKLAGAGLIKYSKCLHILPLIEVGLSYEVRYGTRVTGQSIRDASCYFVWSFYHCYSKSAIEGLQTNLILCLLQTVLFDNEINVRRAATAALFEVIGRHASIPDGLSLISHINYVSVTDISNCYGDLCMKVAHFPQFRSCVFQRLFTNLQHWDVKVQQLSAFSLRQLSIKYPKELSIYLPPILDYLSVGNADFIFGYTIGLASIIGGFLSISFPFDINRIHDLLSHKNLLSLKKFSRQQQTKIILGILKGIQQIFANDIRVDRAFFSEAFSVIIAAIDLQEETIIKDISDAYSVLVKFDDMEETLEVLLDYIRKCSTSKEARIVYIILQNLPNISFRYQKKICKLLLDIYPQLHSIDYQAPVANALQNIIPFTYEKTESIEEFVKELLQVCSNYLTDTRGDVGSWIRKPAMKAISSLLVKDSSGKKLSEDIVWCCISYIIRQTFDKIDSLRGLAYQALEQIRVHYLIRRCEALTNIINRIRNNPNMDGEVLNELNISLLEIPNLRLQAFYGITVFTADGFGSDLAVKCFEFYLSYVYQLEDSFKKSNSRYGKRDLLQLYIDILSSEDEIARFYFPIMKSFTSLLAYGCFTDFQNVKGMSKAIFIVQRRALTCKSPGGLSAILELYRTLFLSKNELLRHHALKYTANLLLNPIEKVRYQAADTLLYAKSIGLLTFLPNELNQKLLTLDWFVPVSQNATFVKQLRNIIQKQIDKLIADR | Has a function in the folding of beta-tubulin. Microtubule-associated protein that is essential to direct polarized cell growth and to position the nucleus and septum to the center of the cell during mitosis. Interacts with alp21. Microtubule-associated. |
D6W0S4 | MDETVNIQMSKEGQYEINSSSIIKEEEFVDEQYSGENVTKAITTERKVEDDAAKETESSPQERREVKRKLKQRHIGMIALGGTIGTGLIIGIGPPLAHAGPVGALISYLFMGTVIYSVTQSLGEMVTFIPVTSSFSVFAQRFLSPALGATNGYMYWLSWCFTFALELSVLGKVIQYWTEAVPLAAWIVIFWCLLTSMNMFPVKYYGEFEFCIASIKVIALLGFIIFSFCVVCGAGQSDGPIGFRYWRNPGAWGPGIISSDKNEGRFLGWVSSLINAAFTYQGTELVGITAGEAANPRKALPRAIKKVVVRILVFYILSLFFIGLLVPYNDPKLDSDGIFVSSSPFMISIENSGTKVLPDIFNAVVLITILSAGNSNVYIGSRVLYSLSKNSLAPRFLSNVTRGGVPYFSVLSTSVFGFLAFLEVSAGSGKAFNWLLNITGVAGFFAWLLISFSHIRFMQAIRKRGISRDDLPYKAQMMPFLAYYASFFIALIVLIQGFTAFAPTFQPIDFVAAYISIFLFLAIWLSFQVWFKCRLLWKLQDIDIDSDRRQIEELVWIEPECKTRWQRVWDVLS | High-affinity permease for basic amino acids. Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family. |
Q10303 | MHISTGMVRASISNTLVTLTIEGNNDRYQVILDKNVNAKQFVKTCWRNKKPLIVKEGKIFVDKGFPFDPCRTFLEALYEKYSYSSPLPSSVEFKSGKQVEFCGFEKIQSKQRDLKSLRVIILDNYRIEDIEIEYEYSKILPEVIDLDLSRNLFHEFFPILKLCSQLPSLRNLTLDSNLFSNFISSNTVLLIPHLTQLSVNGCGLNSKDVQWITETFPSLEVLYLEANEIILSKATSFKNLQFLQTLSLANNLNLYSADGYAVDVFQGINNLNLSSTSLADVAELPVHTLHKLTFLDISENNIRDIRSLDHLRTLENLKHLRITLSYFNKPTDIAKLLVIARIPSLVKLNDVNISPNERLDAELYYTSCIRKLVIDNEIKDVEELTKIEPFWEEIWKSHELPSIQFHLEASINDWTSGILKNRITKGIKISSINSGATMLLKLHYNWKLLDIKALISYHFAIPVHTSTFVFASSERDVSFSPKTVRDDQKRLFELPFTCTFIDVYAKESGNV | Required for microtubule and spindle assembly. Involved in the proper folding of alpha-tubulin. Interacts with alp1 and alp11. |
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