ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A159KM90 | FLFGMWAGMVGTAMSWIIRIELSQPSSFIGDDQIYNVVVTTHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSITLLLVSSLAESGVGTGWTVYPPLSSNLAHSGSSVDLAIFSLHLAGVSSILGAVNFISTIMNMRPTGMIPERIPLFVWSVG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A453MVB2 | MDGFGVNTYTFVSRAGKSHYVKFHWRPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIDAGNFPEWKLFVQVIDPDDEDRFDFDPLDDTKTWPEDLVPLQPVGRLVLDRNVDNFFNENEQLAFGPGLVVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGFKNNHYDGAMNFMHRDEEVDYYPSRHAPLRHAEPASFPVPTRPVVGKREKTRIKKENDFVQPGERYRSWAPDRQDRFVRRFADALAHPKVSHELRVIWIDFLSKVTNYRCMNPWTYAECSS | Catalytic Activity: 2 H2O2 = 2 H2O + O2
EC: 1.11.1.6
Subcellular Location: Glyoxysome
Sequence Length: 291
Sequence Mass (Da): 33786
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A0A954B578 | APLRSRGESPGAAPVYVADTLGELGTLFDLAPVSLVAGSLLPTLKGHNPIEPAKLGSAIITGPYVESFEDLFAEMFAAGAA | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A0R2L0F5 | MAKVVVALGGNALGSSPSEQRQLVKGTATSLIGLINAGNEVVISHGNGPHVGQINLGLNFAAENGKTASFPFPECGAMSQGYIGYHLQQALQNELAHQHLSKSVITTITQVLVDQNDSAFKNPTKPIGDFYTKEVAKKIAEDKGYVFTEDAGRG | Pathway: Metabolic intermediate metabolism; carbamoyl phosphate degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.
EC: 2.7.2.2
Catalytic Activity: ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O
Sequence Length: 154
Sequence Mass (Da): 16252
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A0A0N7B984 | FFFVMPVMVGGFGNWMVPIMMSCPDMAFPRMNNMSFWLLPPSMILLMLSMMIGMGSGTGWTVYPPLSSIMFHNDPSVDLTIFSLHLAGISSIMGSINFISTILNMRTKLMKMTKITLFSWSIFLTTILLLLSLPVLAGAITMLLFDRNINTSFFDPSGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A349N1Q2 | MYWFYNICLVAYWILQIPVLIYRLIFEEGFYDRLKQSAGVMPTPTLEKIAYRNAIWIHAASVGEIVAASPIARELKRRYPNEMVVVSVVTATGHRMAQRIIPEADGHIFFPFDLPVITSRIVRIVSPKVIILVETELWPNFLRFAWNQKIPVMMMNGRISDRSMKRYLLINRYTSRMLTQINRFCMQSAVDARYIISMGAKKDRVTVTGNTKYDQIYAEVTEEEKKELRREFHFEDTYPVLVAGSTHGGEEEILLHTFKKVCAKYPKARMILAVREITRAPAVKFLVRRAGFSVIRRTEMKNTEEDLSPQVLILSLIPL | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A344VDT9 | TLYFIFGAWAGMVGTSLSIMIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLASSMVENGAGTGWTVYPPLSSSIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRSSGITFDRMPLFVWSAGITALLLLLSLPVLAGAITMLLTD | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
F8E0L6 | MPLELLPVTVSTPEPSQTSRYRGAQSAAHGETATPAPANLSGAAAPSVRGLSRWAWIQIFLAVFAAISRLGSLGKPTDAGTPVFDEKHYAPQSWQITRSVDNPLIGGIEDNPGYGLVVHPPLGKQLESLGMQAAGYTPLGWRIASAICAIIVILLIAAIARRITKSDLAGMFAGIFALCEGILFVTGRSAMLDHFQTLFVVAATYFLVRDAQQMEQRFTRVFTEGRIKDHAIGPRMGYRWWRFAAGLALAGAVSVKWSGLYYMAFAGLALVVLDYFRRRRFGVAHPLRGTLVLDCVPSFLSVVIVPAIGYVLSWRAWFAS... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A8X6M467 | MKKTKIFDFFQSQPPVVNVPCPACGISLMKSKLNDHLDSSCSSLVLSTVSVINNSGSVKVKSSRESSRRSRRKNQETTNNVISNRLSLKRPKTKLNKNINRKLIKVDEQTENDDDIKLIEVDEQNESDDDIKLIKVDEQKESDDDIIVLEENLASFDKITKFEISSSACSSQDPKLKTRSPNSEYDIVSYKERNFVVDLKIEVDKCYSDKTLEVCSKTTETYEQSIIVEKNIPDFQAEVDLNHDIAVSEQNSSEKCVVSSRLSLDTMNILKDAKVILENDNVFSELSDSNENEEKKNDVKNYDPYYIANFKHILESVLNE... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A8J5FLU7 | MVRGKTQMRRIENLASRQVTFSKHRRGLLKKAFELSMLCDAEHQMSSIPQELNAYFSFLFELIAERGPSVGGKEGRVVKQESKEVSIPQELMIGSLDELFDFIASALAQFVASEGVDFHLPEGKQRELGFTFSFPVKQTSIASGTLIKWTKRFNIKSTVYVSNLEGKIVALYISCNRNCCTEFSPILAQIYKKLKEIGESFEEYKCSTVILIGSDGKTIKECEFEAWEALPFSQEKLHELLEKVKARLES | Catalytic Activity: ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+)
EC: 2.7.1.-
Subcellular Location: Nucleus
Sequence Length: 250
Sequence Mass (Da): 28354
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A0A453P8W0 | MGSTGEPDRKRRLSGSFAQGVDAVPPAKRPALPPSSDDKKLDFAVIKYRNQKLSEQLEVHKSEYHALEGKFDDLKQKQKSHHETQDLVNKSWQHLVRDLKAISVCKSGSQNSSCSAVPSNESTDGACIRKDKDFLSRLVETGATESSGCHLENHVHSSTTDVLQNILFSSNDSWHANEKLPLDHFTALPEDGLFFTFP | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 1... |
A0A453IUQ6 | MVVMMTRHILLFIQQSFRLVKTTGLQITRYIALPNRREISISLTSDYSNFSNLLFLCSANLIMFSMSVSAVQKVYELVVRHFLACCSQPAVGAETTVEVDIAGEQFNASGRVVLAKNYLDVYRYDSWGGSLLPTYTIGQQFVPTSLTLDSGVTRPPPLLAEADLLSCMDKAGIGTDATMHEHIKKLLDRCYATKDANSRFSPTNLGEALVMGYDEMGYELWKPYLRAMMEADMKSVSVGTKSKAQVLEGCLQQMKACFLDARANKVKLLDAMGTFFARSNRPINETQNTIEVVRPCGACNDSEMLLKRRPVNCLPVLLFI... | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by... |
A0A453LEI3 | AVSLARSTAPLPTPPKKKYCSSAAGHPLSRPAPAGSSSALPARSPLHVLHRAIPTRFSAPRRRSLDPSSPLSAKATTSRSGPNPGWEGDLPRCSARSAMENGAEAGGGRPEYSIIVPTYNERLNVALIVYLIFKHLPDSKFEIIIVDDGSPDGTQDVVKQLQQLYGEGRVLLRARPRKLGLGELSCPFLHMVNVMLDVRVNELL | EC: 2.4.1.83
Subcellular Location: Golgi apparatus membrane
Sequence Length: 204
Sequence Mass (Da): 21990
Location Topology: Multi-pass membrane protein
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A0A8J5CF97 | MAEAVVLLDLWVSPFGQRCRIALAEKGVAYEYKEQDLDNKSPLLLQANPVHKKIPVLIHDGKPVCESLIIVQYIDEVWSDGAPLLPVDPYARAQARFWGDFIDKKSSAFCSFSMDQIYEYGTRLWKLKGEAHQEAKKEFIEILKVLEAELGDKKYFGGDAFGYVDIALVPFCPWFYTFETCGGFSVEAEAPKLVAWGKRCLERESVSKVFDDPVKVYEILKQVYGFE | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 25852
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A0A1I7WPQ9 | MLTHKIVNIIRQNILWLFLILFICLSGFLDHLFETSFDHFQWPLYNVDVLAETRRYLAKEPVNSVLINDWQLLHRLVEPHWTCIKNKNSNTLLIIVKSAVQHIRRREAIRNTWGQLVNMDGFEIRTIFVVGRFTDKRVEIEVRKEAEVHNDILIADMLDTYRNNTIKFLFSIGYAFRPVKNCPPADFVFLIDDDYMVSIYNIIRLLEDRNPLEQMYEGWMFDSTPFRFRLHKHSVSIYFYSGIYLDVYLLIWFQVSLADYPFDKYPPYISAGAVLFSQVTIAHFYYAVQFVQLCYIYIYNIT | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 302
Sequence Mass (Da): 36061
Location Topology: Single-pass type II membrane protein
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A0A8J5G6D3 | MASDPKSSGLAFVIMGVSGTGKSTVAEMLAKTLNCSFLEADDFHSKANKDEDRFPWLECLRDAIRIVMISGKSIVLTCSALQKKYREILRSSDPDYKAGQYSNCRVRFICLEAPVEVIADRIRSRSKEGKHFMPVSLLQSQLDLLQIDEVEGITKPSSSGYFNFTSMKTSSQLLFEAVLYTTIVWQGLNFNKAVDTTSSIVLWNSNVTLPGTRLASTASHVVACMLASKPQCGLLLASTCQQATLRGLLLAKWLASSCKLDTWPATWRANKLATWCASKLATLALTCILANKLPYADIPCPD | Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 302
Sequence Mass (Da): 33150
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S6BXV0 | MRKLLIFIILPANLALVGCSTVGEGAEKLVGITDIIPRALDRASFIYRPTIQQGNVVTQEQVNRLKPGMSREQVRFILGSPTLRDVFHDNRWDYPYTIGVGSTPKEIKHLAVFFENDRLARIVGDYRPQAPDEQMPAEKPRVVKVPDWEPEKKTLLGRMAEAVGLDDDG | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 169
Sequence Mass (Da): 19010
Location Topology: Lipid-anchor
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B6RHN3 | IRAELGQPGTLLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLILLLSSATVEGGVGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIYNMRSNGMSLERITLFTWSVKITAVLLLLSLPVLAGAITMLLTDR | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1H9JMC1 | MEVVGVYQGQKVVRYVLQTATGYQLVVLNYGATIVKFLTPDKDGKFKNIIVASEDVAEYFDNAPKWGAAIGPVAGRIAGGKVTIDGKDYQLEQNLLGHHLHSGSIGFSETVFKVSDLQENSITFYSEKADRIGNYPGNLKTWISYTLSDTGALTIDYKITTDKATIVNPTNHSYFNLTGDFRTTILDHKLQLATKALAAIDQTGVPTGELVKDSAALELIRRGIKISELFQEEPFKTAGGIDHPFVLNDTATIKVVLSEATTGRTLSVTTTSPAMVIYTSNGYDNKTSLNAEKPIVHNGIALETQILPDAIHHEGFGDII... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 340
Sequence Mass (Da): 36975
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A0A453HFN8 | MTMYNYLAGSTESNFGSRLDGINVILGRQGESCSSACRAKGQSCVPSRLAELNKCQILQKYMRCKNGCFPSLGPDQPAEVVDEAPKNLNPGACLYMQMDDRLTCDGSHRHTRRLCPCA | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-... |
A0A453BZE4 | TNPMATALLTDQYQFSMAYAYWKAGKHADHAVFDLYFRKNPFGGEFTVFAGLEECIKFIANFKFTEDEISFLQSVMPMCEDAFFDYLRGIDCSDVEVYSIPEGSVVFPKVPLMRVEGPVAVVQLLETPFVNLINYASLVTTNAARHRHVAGKSKVLMEFGLRRAQGPDGAISASKYCFMGGFDATSNVLAGHLFGIPLRGTHSHAYVSSYMSLDEIPDRTLRNKDGSKICKDFVSLVKEWLCKIQVQLQNFAVQFSFVAAFLCYFLLISGSRFIT | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Length: 275
Sequence Mass (Da): 30802
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A0A352TS64 | MMALEEVKQHALAIRVVFGSVEDIDRINIYRATKEAMVAAIKGLDIQPDFILTDAMPIPEYKNLESIIKGDQKSISIAAASIIAKTTRDAYMKNMHTLFPLYGFDQHKGYPTKKHIEALMTLGPTPIHRKSFQPVKDAILKFKK | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 144
Sequence Mass (Da): 16242
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W0M415 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGXXXXDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAXXXXXXXXXXXXXXXXXXXXXXXIVENGAGTGWTVXPPLSSNIAHGGSSVDLAIFSLHXA | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A8J5LK58 | MCASSPQADPNFFYFSDQIVSKGKAEGREQGISESEMASGWGISGNKGRCYDFWNEFSECMSRCREPKECTFLREDYFECLHHAKEVIPQIQPLFSYYLLMHFSLPKSFA | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A516ZAD8 | MNNLSVPSIEYQQFEDGYIVKKEGKTITYCESIKGARQFTNFFWLVLLFLFGIGFLVAGFSSYFNFNFLFFSNFSNIEFIPQGILLLFYGTCAILLSFLILNLINWDIGSGTNNYDIESSVVRLSRRGFPSLTKDFKFEQRNLYLVYPFSDILNLELEIIDGLNPTRVIYLRLKDNRRIPLTPSNQLKDLRYLENRAMFLARLLKTDLKLEVNNS | Function: Seems to be required for the assembly of the photosystem I complex.
Subcellular Location: Membrane
Sequence Length: 215
Sequence Mass (Da): 25077
Location Topology: Multi-pass membrane protein
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A0A7X7YYM9 | MTKIKICGLTRTEDIEMVNEFLPDYIGFVFAKSRRQVSAEQAKELKNKLRPAIKAVGVFVNEKPENIAEIANQGIIDLIQIHGDEDAAYCAQLRKLTQAPIIKVVRVEREDDFAGIEAFDCDYYLFDTLSSKDYGGTGKAFDHSLLYNKEIKKPFFVAGGLNQDNVAAVIEVIKPFGVDTSGGVETDGIKDVNKIKEFTKQGRIVGKND | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 209
Sequence Mass (Da): 23239
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A0A453IKZ9 | IHALREEDIDEKFFKALLHVQEIHSNCKVLLRTHHQRAGLELMDMMSVYQEGAYERLCRWVQVECKKPGDTDNPEVSELLKKAVRCLKERPVLFKYCAEEVANMRHHALFRQFISALTRGGPGGLPRPIEVHAHDPLRYVGDMLGWLHQALASERELIAALLDPDAISDSGPANHRHSVREGDSSKGESDFTFVLDRIFEGACRPFKVRVEQVLQSQPSLIVSYKLSNTLEFYGYTVSLKF | Function: Required for normal Golgi function.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 241
Sequence Mass (Da): 27528
Location Topology: Peripheral membrane protein
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A0A453A6G2 | MLLILVVLDGSNNGKPHWVQTTVNLDDHIILPRLDPAVSASDPDKAVEDYVSSLSTLPMDRSRPLWEFHFLDFATSEATSTTVLRLHHSIGDGMSIMTLLMASSRSTADRARLPAMPPLPRRTGAIYQQRTRPPLSSIGDYLAWIWSYFVLVWHTLVDIALLNATLLFLRDPRTMFTRVPDKVKSPRRKRLVHRSLNLDDVKLMKTAMNCTINDVLVGVTSAALSKYYFRKSGDAKTKRIHLRSILPVNIRPLSSRQTYVTKVETGNQVSILICPFHIALHDDLLEYVHKAC | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 292
Sequence Mass (Da): 33023
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A0A8X6LDT7 | MMPDLTYKESFTKIFVKHYGLISKMLSKSKDSETLSNRVVHVSVQLFSNEDLAYQMTKDYDLLQIMVDSLSCMMLSISQKSTLQCPEKNEHLVVDCGHHIMKEHCYWPLVSDLNNVLTHAAVAYEFLSDSNLLNQWFKFLSLFQGMNVNQRELKTHVEFESNTYYAAFSAELEASATPMWALISHLKSPVIVYNACLWTLRNVVYIICPKAAINNSRLPYILQTPDCWLFKKPKCY | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A3D4TMW1 | MSGKIIARVVDRAQAAIDPAEGIAAVSDPGFGGIDVFIGKVRDVNIGRPVTGITYDLFEPLVLNEFKRLAAEVEATFGPKLKLYVAHAKGRLGIGDVAVVVAA | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Lengt... |
A0A8J5KM52 | MGGNDPPINLVVSLIESPDRLLASMILLEIVKEDSRRGGAQRRYSHEGSSCWLGYNGLQTFLSEDAPMPLMNCRVVSEDFTLFEDVPNGVVPNLLPIGVYEDLTFWGCTWGSYCKKYVLVANCCEFNSDCLGFAGKVVFLILDEIALIVSEWVVLTDLCYRVIRFGYWCLTPKTRLVSCMSIQFSAGARISEDCFASCRSIVFSLVLESGLTFSCLPPDLPINSDEEKREELFENLKLDDSIGWEVDVIDPWELSAKMTKINLNEISHNSTMGLVKRVLDVGVLLTEVKRVCDTVGDAEKYRVKLSERFPGIQFVVAKKV... | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 351
Sequence Mass (Da): 39257
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A0A453A0M7 | TSMVDYILGVADPLQWHSENLARNPTHYSSWMARRGPEAVTWLADRVGVGVYFNPFVEWGDKRIKYGVVAMKDLATDILTWDQFYLSGRLQKPVRVLVDNWDIRMVNTVNLKMAAAASLLLLPKEFTEHDLYAKICSLSYMGDIRMLFAEDKYKVKKIVDGSFQPFQLMYRPLIQDYISEGILKMSDYRQQKAFKQV | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 197
Sequence Mass (Da): 22872
Location Topology: Peripheral membrane protein
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A0A453I8S5 | MLIRPHPNECSGGDLDGDLYFITWDEKLIPEKVDSPMDYTAARPRIMDHVVTLEEIQKYFVDYMINDSLGAISTAHLVHADRHPMKARSPECLQLAGLHSMAVDFAKSGAPAEMPRSLRPKEYPDFMERWDKPTYISDGALGKLYRAAASRMQSAPATSSSAQLSPAYDPDLEVPGFEEFLASAEECYDLYEEKLSTLMGYYGAEHEDEILTGNIRNRLLYLKKDNKRYFEMKDRIIDSVEGLHKEVRGWFTSRPKAETARRASAWYRVTYHPDHRRPGKKQFWSFPWIVCDELLKIKESNKQRSSRGTTLRPDSSGQVI... | Function: Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs).
EC: 2.7.7.48
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 321
Sequence Mass (Da): 36821
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A0A453RHT8 | QRSNKSMITVQLLLISYKQTFTGQRTSSRLTSKRLPTQHSSNNKHFPYQDKLEDPKLHHYALFSDNVLAAAVVVNSTLIHAKKPADHVFHIVTDKLNYAAMRMWFLANPPVKAAIQVQKIEEFTWLNSSYSPVLKQLASQFMINYYFRTPQNKPDRNPKFRNPKYLSILNHLRFYLPEIFPKLNKVLFVDDDIVVQQDLSPLWSVDLKGRVNAAVKTCGEVFHRFDRYLNFSNPLIAKKFDRHACGWAYGMNMFDLSEWRRQNITAVYHYWQEQVSIRELFNNV | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 284
Sequence Mass (Da): 33386
Location Topology: Single-pass type II membrane protein
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A0A6L5X9F6 | MENNRLYKREKLCSRTAIARTFDCGHSLMAYPLRAVYHMGPSRPEAPARFMITIPKKKIHTAVQRVALRRRTREAYRLNRQLLLPALEAAGRSLDVAFIYLAKDEVAPYAVIEEKMRDILTRIAQATHD | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
W4U862 | MICLAVQYASQEAPFLFVVQIIVYTGAILMLFLFVVMLVGVDSTDSLKETLKGHKVAAMIAALAFVVLLILAVGNAVTTGVIGTDYPVGLGQANTAGGNNVKSLAELVFTKYVIVFEATSALLITAAVGTMVLAHGEADKKKSQRERVTDRMAAYAEHGSHPGVRPNSGVYARTNQIGAPALLPDGTVAQDSISGTWRPAVPLSTPVS | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A8I6S0B0 | MNSLYKKHTKFFKVVGLLFHFSGALQFTVGIVFDYQLIVPGQTFYLLQRLQYMTYWNLYLQWFYFTKRTINDIMTFDDNDEDETPKCVDYIKTSLAIPNALTVSILFWTIYTLDPSLIHGGEPLPRYLNFVVHTSVSLLNLIELAIVKQRICPQKKCLWINFCFSLVFTAWFIAYNMTENKWTYPFLDHLDILRKAVFFSSCCLMNFSLCILGQNLQYLIWG | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 222
Sequence Mass (Da): 26243
Location Topology: Multi-pass membrane protein
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A0A453FFF4 | ADVIEELEQTLATPTPLLRGIADAMVEEMERGLRADPHAPLKMLISYVDNLPTGDEHGLFYALDLGGTNFRVLRVQLGGKEKRAVQQYEEVPIPPHLMVGTSTELFDFIAAELERFVETEGDDFHLPEGRHRELGFTFSFPVHQTSISSGTLVKWTKGFCINGTVGEDVVAELSSAMERQGLDMKVTALVNDTVGTLAGGIYADNDVVAAVILGTGTNAAYVEHVDAIPKWKGPLPRSGNMVINMEWGNFKSDKLPRSDYDIALDFESLNPGEQMYEKMISGMYLGEVVRRILLRLAHDASLFGDVVPSKLEKLFVLRTP... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4.
EC: 2.7.1.-
Catalytic Activity: ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+)
Sequence Length: 390
Sequence Mass (Da): 43091
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S6CGI3 | MITIDDRARAFINRFQGGFPLAERPFSIVAADIGLSEVALIQLVERLLEEGLLSRFGPLYDAEAMGGGLTLATLSVPDSLFDAVAERVNALPEVAHNYRRDHRLNMWFVVASSRPDGVARTLRRIQHETGFPVYDFPRRRAFYLGLWLELREDGFVSTVPVPGEVACKSTLSVRLDTLDRLLISATQAGLPRVARPYRAVGEAIGIDEEQVIVRLQRLLDGGVIRRIGAVPNHYRLGLRANGMTVWGVPEQWTEELGQQLGGMEAVSHCYERPRHSGIWSYNLFAMVHGHDRHEVLNKMERLRCELGEPVRGHEVLFSTA... | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 331
Sequence Mass (Da): 37128
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A0A8J5M264 | MNDTVDKLVVFLAKRDGIDKLVKTFQYVSKLVHWQAEASRPDLARRAKSWEVASGLSRKAFRSGRFLTGFNALRRSPGSTPLFRFLAVFANAGEMVYFFFDHFLWLSRVGVLDAGLARRMSYVSAFGEALGYVFFVAMDAIMIKKGLAEEATAAKEEEVRRIRAAWSQRGLVGEIRHESFYFLVAVAHHASTLQNIICDVKANRYQNQDATIYIRTFVQIYVLWFRQTCLG | Function: Involved in peroxisomal proliferation.
Subcellular Location: Peroxisome membrane
Sequence Length: 231
Sequence Mass (Da): 26369
Location Topology: Multi-pass membrane protein
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A0A3D2VYZ5 | GASTITQQVAGNMLTGRAAACEGGIGGLFCAVYTKFREGLMAQRIEKALDKDRILELYLNQIYLGNRAYGVAAAALNYFDKPLSELTIGEAAYLAVLPKGPANYDPRDPRKRERAIERRNYVIGRMLDRGDITAAEAEAARAEELVSHDRLAGDQYIAASHFVEEIRRQVQQQYGESALYDGGLSIRSTLDTRLQLAAARVMRAGLEQYDRRHEWRGPIASGDVAGDVQAQLRDAPAPPQLSNWVRAMVTRTGNGAITLTDENAATGRLVDGDAQWAAQGARRQRARALARGAIVYVTRASGRYTLRQIPEVQGALVAMD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 716
Sequence Mass (Da): 7... |
A0A8J5ERZ5 | MNSTSGEATKGVGRRPPFTEVQWQELEHQAMIYKYFMAGLPVPPELIVPVQRSFEVLPGRYYHRPARFIVINRFISIPRVFNLLKPKVSILFPFSFCALFAVILLPFLISNISRLSRPVCFCLTHYCSYYGRKLDPEPGRCRRTDGKKWRCSKDAHPDSKYCIHHMHRGRNRSRKPVESQSISQLQLSSSTGTTTSPTAGSSVPQHSITERSDTSSLFLASSSSLQLHMDPGPLESRYLSSTKPGMAEHTFLTETSGSARGQGIYSIDNLWHLTSPRVSSWPSTKFSTPYSVQTTYPQFPVVQHLSQATLSPVSRQQHSF... | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 401
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 45034
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S6CF46 | MHTMRRLAGLLVLAVFALAGCQSQPKRDPAFAPVPPEVPKPAAQANGAIYQAGFEHRWFENVRARRVGDILLVTLVENTEAKHTNAGKVKKSNTSSITNPTLLGKPFSFVLPGVTGGKDADLGASLSSSSDFSGSGENTQNNQFNGSISVMVTEVLPNGYLRVRGEKRIAMTGGNEYIRVSGIVRPEDIDVDNSIASTKIADATLTYVGDGQTGMASTMGWLAKFFISAVMPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 233
Sequence Mass (Da): 24834
Location Topology: Lipid-anchor
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A0A452YN37 | MEVFYYLVFGGLAAVVAALELGKSGKDRVATPTAFNSFKNNYVLVYSLMMSGDWLQGPYVYYLYSQYGFDKGDIGRLFIAGFGSSMLFGTIVGSLADKQGRKRACITYCITYILSCITKHSPQYRILMIGRVLGGIATSLLFSAFESWLVAEHNKVTARTQIYVPISALCCPAPASFRNDPSVPA | Function: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum.
Subcellular Location: Cell membrane
Sequence Length: 185
Sequence Mass (Da): 20311
Location Topology: Multi-pass membrane protein
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A0A7S3DLB5 | MWQSFLLSLALRVLMACHGHSGEGNPPMYGDFEAQRHWMEITLHLPVRDWYKNTTDNDLQYWGLDYPPLTAYGSYLWGYIFDQIEPDMVALHTSRGYETVLSKVLMRLSVIVSDLLVYYPAVFLFVSVVDLTDEKVKVGESQRSFSTKSVVTHALLFFPSLIFIDHGHFQYNGVSLGLFIAAVAFFFAKRETGGAVDMMCDFLAAVCFSLALNYKQMCLYYALPVFCLCLRKVFDMPSMVTKVLRFFTFAAAVLLTFGVVWAPFLVETKKELGAGVKMTETTVGWVLHRVFPVARGLFEDKVSNFWCAFNPVLKTRERLS... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 550
Sequence Mass (Da): 61770
Location Topology: Multi-pass membrane protein
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Q0CBT4 | MIANPANSVRAEEDFRQYVKELEDENDLLPITKEVDPHLELAAITRKVYETEEKAPLYENIKGRKESGLFRVLGAPVGLSRQPGRRFGRIAKSLGLPSTATGEEIVNRINECKRKPPVPPIEVPPDRAPVKQYKLFGDEIDLTALPVPLHHDADGGKYLQTFGMHIVKTPDGRWVNWSITRGMVHDKRALVGPVIPKQDIGVIWQMWKEKGRDMPWALCFGVPPAAIMASGMPIPKWTDEAGFRYIKGVVSVTEVGPEGPMAEYHGMVFPGETQNKPLFKVNAITYRHDPILPLCVAGRAAEENHTVWGIMQAAEVLNVC... | Cofactor: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Function: Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of ... |
A0A8J5GH82 | MQSKVTTKVYFDISIGKLVGKDVGRIVIGLYGDDVPQTAENFRALCTGEKGFGYKGSAFHRVIKDFMIQGGDFDKGKKIRTLCGDMELPEWCKLLPKIELHAHLNGSVRDSTLLELAKVLGDEGVINFEDVVHVIMKSPIAKCNRVNEGEKMDFEEFCAAAISPHHLEVLDGWEQMTSTTFEHFELEGNRAITVKELAQFTNLKYSRVEIDEVRFEWAECMLDYI | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 225
Sequence Mass (Da): 25472
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A0A8J5GEF4 | MASSTGFSLASAASRFAPASGLPSAGNSPFRTLTFSKPSRKLVVRAEDESAPPPPPPPPPPPPPAEGEAPKAAAKQPPPPPPPIGPKRGTEVKILRKESYWYKGVGSVVTVDQDPKTRYPVVVRFTKVNYAGVSTNNYALDEIQELQWISDLQPNKCGLFGLFLSTVFYTASFFGIIMMYYVYALDSTCIINIFIITWTTALVTVIMIVSLHSKVNAGLLSSAIMGSYIVFLCWSAIHSEPAMEKCNKRKRTDRDDMTTILSFFIAIGAIVMATFSTGTDSNSFQLKKNEVQSADDAPYNYATFHFIFSMGSMYFAMLFI... | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Subcellular Location: Membrane
Sequence Length: 382
Sequence Mass (Da): 42214
Location Topology: Multi-pass membrane protein
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A0A8I6RKW6 | MYKILVLIALYGVAYGSATCTNPEVTATSYTTKDGTVITNVAFVAEFTLKCSNGASDLPLYAEINGKTFPAVQFDKDHYQVSWVDEISKARSGTYTISLYDEEGYALLRKALRNAEAPSKVSPLFKVELFHPGTYQGPWLNSEFLAVTLSVSVWYLAFSAKSKLLL | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 166
Sequence Mass (Da): 18301
Location Topology: Single-pass type I membrane protein
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A0A345R8C1 | MKVLSDLVNADELCMKNPSAEVFVGELGESSVNIFCRPWVKSENYWTVYWGLTGRAKERFDAEGISIPFPQRDVHLYQSSTGSS | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A349N1D9 | MEKLCACRKNSLKDWKKFPGKTEMDNRPIGVMDSGIGGLTVVHSILELCPRESILYLGDTARNPYGEKADSWIMKCGEELKNFLIARGVKMVVVACNTITFHEPPLFYQDTVPVIGMSTDYSSAGAARKVGIFATPASIRTHAHKKALQSVWPDMETAEVPCEGLAHAIESGEGRAVLKNMLEEAVYQYDAGDIDMILFGCTHYPLIEDLFRELFPSAVFFDPGAVTAERASGILKTCHMEADGDGESHFCFTKKSEQESCLIKKFLHRKEKAEEIRIAGE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 281
Sequence Mass (Da): 31159
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A0A383WDF1 | MFRSRVLARSGNSGNGDAQPTHDASHEFQGYTDRIKDELADAGRLKKNLLISDVVSSDGNGEQLQWVDLVLAGGGLLGIAHVGFVCVLEEAGVRFRGIGGTSAGAINAVIVAASRKDDKGKFDPSQESWEKTLDILTHAKFESFQDGEGVKNSNALLKLALGASGEAKPSKLSLAWAVAKALPELPRIWQNRGLHPGNEFQDWVKKQLEDKGIENVAGLHEAMSLDRLSNKVHLREGVQRSAEELAGISRATLKLVASDISTQTKVVFPDMANLYYAKADDAHPSDFVRASMSVPLFFQPYEIPKLDIKIPKQLQSVQDA... | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 502
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 54555
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A0A453IV09 | MVVDRLTGKSVMSQVRTSSGTFLPKKQDRVVATIEERIAAWTMLPQENGESIQVLRYESGQKYEPHVDFIRHTAKGYHSRGGHRVATVLMYLSDVKMGGETVFPNSDAETLQPKDDTWSECARRGYAVKNL | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 131
Sequence Mass (Da): 14775
Location Topology: Single-pass type II membrane protein
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A0A7G6DZR7 | MSEIVWPNLVKFIQDMVPERSGLLKELEMECQAEHIPMIQPQVGQFLLLLLSIHKPVRILEIGTAIGYSTLWFTQALQDTRGHITTIELDKDRYERACANFLRAGVAGRITPLLGDANELLPTLKGPYDFIFIDAAKGQYGEFFAKAWALLAPAGVIVMDNIFLNGWVIDMTWPHRRKKTMVVRVRDLLENITSHPDLLTSLIPLGDGLSVSIRRNAHEKS | Function: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
EC: 2.1.1.-
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 221
Sequence Mass (Da): 24945
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A0A383W3M4 | MQCVRCNVCAELVAVDEIMLHSAMCALRAMGVEPMNAAQYYEVAAAYDEWDEPESSFSDYEYYTELAERMGGPVEIGVADLDAAAPRVKPEARSPKPGECCCPVCFEDLASSEIKARQTMSMTTDKSAHLSEEEFDKLTWTVVEELFAHNQGAQLVKHQTDSYNDFVLRKMEQVIEGFNTVEVHHQYLPDLEGFRYTLRINVQNPVLSKPVILEKDGSSKIMTPADARQRNLVYAMPLHVDVRVNASTMQDDGSTRTETKTLRGVNIGKLPIMVGSKYSVLTSMRSVEQNECKHELGGYFIINGNEKVVISQDRIAENKT... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Plastid
Sequence Length: 606
Sequence Mass (Da): 68469
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A0A453L6U4 | MCLLKAHIHRHLAQEARGCTYLVLWLDCDREGENICFEVINCTGIPENEVGRRIFRARFSSVTEKDISNAMDNLVLPNKDEALAVDARQEIDLKVGVAFTRFQTRYFQGKYGNLDSRVISYGPCQTPTLGFCVQRYQQINTFKPEKFWSLRTYIIKDGDEIQLEWDRKKLFDFDVTVMFQKMVPSDGALKITDISVKEECKARPPGLNTVNLLKVASSALGIGPQTAMHMAERLYIQGYISYPRTESTAYPASFDFRSVLSTLAHNPLWSNNVRTLMDAGFVKPRQGHDVGDHPPITPMRLAPEEALETDAWRLYQYICQ... | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by... |
A0A453J164 | GLVPARPGQEAPEDAATAPARGAVSERAARKESERRTYLVAALMSSLGITSMAAAAVYYRFAWQMEGGEIPVTEMLGTLALSVGAAVGMEFWARWAHRALWHASLWDMHESHHLPRDGPFELNDVFAIVNAVPAMALLAFGFFNRGLLPGLCFGAGLGITLFGMAYMFVHDGLVHRRFPVGPIENVPYFRRVAAAHQVRPSAPNRTKLYPSFGSEL | Catalytic Activity: a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+)
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 216
Sequence Mass (Da): 23551
Location Topology: Multi-pass membrane protein
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A0A357AIY6 | MRNLIWFNEDHCDRIQYTGGKGASLSKMHKFRLNVPNGFVISAPFFFEYRKENNLDEKIIKLIDTIDFDDCACIEKVSEEIRKMVINTPISAELENDILSYYGMLGGEIQPVAVRSSSTAEDLDDASFAGQQETFLYVMGKDDLIEKIKECWASLYNGRAVFYRKQRGFCE | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 171
Sequence Mass (Da): 19680
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A0A8J5FW91 | MASSTGFSLASAASRFAPASGLPSASNSPFRTLTFSKPSRKLVVRAEDESAPPPPPPPPAEGGAPKAAAKQPPPPPPPIGPKRGAEVKILRKESYWYKGVGSVVTVDQDPKTRYPVVVRFTKVNYAGVSTNNYALDEIQELTKKKRLRFLWGNSGSEFLRAGAAQRSPVSAAERNGSFFSGGSGDRLIEQVNAQIHGRGIPLCALVGLFKGLLRGDGEEKCTFQLRIGTFSAYNVTLVLIRIHFFMRNMLSPLESISPQSVNWISDLQPNKCGLFGLFLSTVFYTASFFGIIMMYYVYALDSTCIINIFIITWTTGLVTV... | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Subcellular Location: Membrane
Sequence Length: 523
Sequence Mass (Da): 57984
Location Topology: Multi-pass membrane protein
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A0A0A7JXZ4 | MSGTSEAELWQLMRSLGISSSFLGTFDCSFPGFIKADRKQTAIINTGSRQSGGMHWIAMAWEPRGKVLYLFDPLGWKDRDLMRYYGFSYKAMVARSALSTPSHCVTLEKNTQAVQCTCSGACGLFCVVFLYCFNVCPTAPATVKVLEAMEGTASALRPADPAKLHWNQKVMYKFLSANSSYFRKHQRTLVYNTRLGLIKTHS | Function: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to ... |
A0A7C6Y603 | MKLKLYPSDLAGFIKAPSSKSYTHRALICAALAPGKSVIKEPLLADDIFETIACLKKIGATFKIYPQEISVFGAALKTHDKITLEIKDSASTLRFLIPLLSCLTKEIEIKTTKRMWERINTSDLNGLRGLYFSYNKGILKITGKLKEGLLNLSLKFTSQWLSGLIFALPLLPKLSLQTDLPFSDLSYPDITLEVASKFGISFLKKTNSISYREGIYQATCYSIEGDYSAAANWLAASCFSEKLKVGNLEPGSMQADYKFFDYTKKLGIEFQFENGAYSFLSRKAQSAVLDLFFSPDLFPVLAALAATSGVEVRFAGLGKL... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
EC: 2.5.1.19
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Length: 421
Sequence Mass (Da): 46897... |
A0A1F4XKG6 | MKLVITGGGSGGHIQPLVAVLSQLKKKAISSTNGLTVYWLGSKTGSEMKTSQDQGVPFHHVPAGKWRRYFSLYNFTDLFKTAVGIIKAWWLLGKLQPDLIFSKGGYVSFPVVYAGHLRKIPIIAHESDVVPGLTTRLCFPFVTKQFLGFETSKKYFKNHPEKLVFTGIPLRESILHGSGESGLQFLQIAQKSKPILLILGGSLGAASLNKFITQNVSALLQKFTVVHSTGPNKNTLHTHPEGYHPFEFLGPELADLYQAADIIVSRAGATTLAEILTLRKKALLVPLTQAQSRGDQIVNARLVKDLTNIAVLEEQDITTD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A452YKX1 | MKFGTGILDDNDMNHLKNKRIRSVADLLQDQFGLALGRLQHAVQKTIRRVFLRQSKPTPQTLVTPTSTSILLITTYETFFGTYPLSQVFDQTNPLTQPVHGRKVSCLGPGGLTGRTASFRSRDIHPSHYGRICPIDTSEGINVGLTGSLAIHARIDHLWGSIESPFYEISAEKAKEKKERQVVYLSPNRDEYYMIAAGNSLSLNQGIQEEHVVPARYRQEFLTIAWEQIHVRSIFLFQYFSIGGSLIPFVEHNDANRALMSSNMQRQAVPLSRSEKCIVGTRLECQTALDSRVSIIAEREGKIISTDSHKILLSSSGKTI... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 371
Sequence Mass (Da): 41912
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A0A7C6Y3Z4 | NVKNGTILSVGKNGLIIACGNNSSISILEIQPESKRKMSIKDFLNGNGKDIFITNEIIGE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A971B8M6 | MTKANYHTHTYLCGHAEGLPIDYVQKAIELGLEHIGISDHGYLKDKWVDRMNLEEYHNIYLPNIQEAKEKYGDKIEIFTGLELEYLDGYDSLYQKYYRENDYLILGQHIVEVDGIEYDLYKPMNDSLIIAYKEAVIKGMESGYFKILAHPDLYMLRYREWNDLTEKIAIEIIESAIKNDVYLEINGNGTRRAATFTKDLELTWLYPRVEFWRIVSRYQEAKVIVGDDAHYFAHLHDLAVTNAILFAKKMGITIYDKIL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 258
Sequence Mass (Da): 30297
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A0A5C0B577 | MTGSAPVIDSIGIESGTPDIDTQSHTKAAGRTTADPWQDLRRHTAARLALGRAGASMPTDEILRFGYAHAQARDAVHVALQVDELTKALQDAGIPSLRVHSAATDRAQYLLRPDLGRRLDTNSVTQLQTSAAELPACDLLIVVADGLSSLAIHRNALPLIHEIRAQAPAGWTLGPVVIAEQGRVALGDEVGELLGARMVAVLIGERPGLSSPDSLGIYLTSAPRVGRHDAERNCISNVRPEGLDIPLAARKLWWLITAAKALGTTGVALKDRSDETALPADAMTALPDPT | Cofactor: Binds between the large and small subunits.
Pathway: Amine and polyamine degradation; ethanolamine degradation.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of exte... |
A0A1I7XPN4 | MLIGSIIHEMFQASVRCSNPLDVTRDWLLHLWRSSIVNGVMQSLCALRFSPSQFEVELEPYADVIVNWIRSHMPSATAQSLPTTSFVTEVHDIEENIWLPQLGIKGRIDVTLKVLLYCLMLAARNNQTISDGLLLYMKDGVSRPVIPRSVELKGLLSQRNRLAYYYHKHNLEKLPGKCYCSLLYNSSNVTVDQRKAIVASLSANDYILIEGLPGAGKTTTITVLIRCLVALGRSVLLTSNTHSSVDNVLTKLMKFMDKSKLLRLGRESSMKVETLELSLKAKTNTEHEDNYEKTRQILKETVE | Function: Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA... |
A0A452XWX0 | MATAAATAAKPAARTTVNVAGAVYRVQLALLDGAAASNEPLLHAAAAILSRADYDDVVTERSIAEACGHPACTSSLPDPANPKAAPRFHISLREHRVYDLEEARKFCSERCLVASAAFAASLPPDRPFGIPPNRLDALVALFEGSGDGPGLGFRSDGGKKEDEGRKVEIVEKETPGPGEVTLQEWIGPSGAIEGYVPRHHPIHEGDCFILNSVIYFDNFVVWIFILAFDYVAIG | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 234
Sequence Mass (Da): 24951
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A0A453KUJ9 | SSEFAGAFQPPTTMNLLSGLEEPNAADVELRLEKSSVGQFLKATTDNQDAGEDAHQLTIFYGGKVVVVDNFPSTKVKDLLQMADGAGDKTGSSSLAQQSPPQPAQNALPDLPIARRNSLHRFLEKRKGRYLI | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 132
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 14269
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A0A8X6KE80 | MSQSKTEKGHILFEGDILEDSPDKDSHSSMKALPNKGALWLERIIPYEYHSSVNRSTGDTIRNAMNEWERKTCLKFVPRTTERQFLRFRTDNGGCFTFVGKKNIEGQDVNLGPGCEHMQIAMHEIGHALGFYHEHSRKDRGEVIKILWHNIERGMASQFRPGNDNNRGVPYDVTSIMHYNPMSFSGHLFEKNTMVTLDPRLQPLIGRNRGITFRDAKLANIIYSCDLECPNKANLHCQNDGYRSPYEGNSKPCTCICPPNTKGKKCESVTGDYYGSITCGGDVLTEGIIQSPGYPGRNPNESCTWQIKAPIRKRIQVTFE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Zinc metalloprotease. Provoques deadhesion of endothelial cells from cell cultures, and also degradation of fibronectin, fibrinogen and gelatin in vitro. Its role in the venom is not fully understood but it might act as a spreading factor that facilitates diffusion of o... |
A0A453PCH7 | MWQALISGCSAGGLTSILHCDRFHRLLPAAANVKCLSDAGFFINVKDIAGVNHAAAFFSDVVKTHGSVKNLPSLCTSKLPAGMCLFPQNEVKQIQTPLFILNAAYDSWQVRNILVPGGSDPRWRSCKHDIKQCSAKQLKILQGFRDHFLEAIEAQGDSPTRGLFINSCFAHCQSEIQEIWFAPGSPVLGDKRIASAVGDWFYGRSWFQKTDCPYPCDSTCHVFKNSSHT | Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
EC: 3.1.1.-
Subcellular Location: Sec... |
A0A453RC88 | AAGRTSSATATPSRTAASSPAPSAPSSPSRPRPRRRGTPQGTPGTRRPSQLVRETIKWILTDRSCRTKNVLCNGIHQGGQANLVSSSSWNILLHRIGDLLMCYILRHSAVFLPIKKSDYFQVTGVPLNIVLHKPIFASTMARKQQSRSTKVKCPMCHVLRNAKMKLNITGGNRGNSSDSAFYCSDNTQKCDALQSSGSCDAERVIKPNCSSDGCNCSNCFTRKPRKRKRLYSWQRCSKQKQFCNEDNLTELSKLNDSNYALCNLLSDGSAAGVNGQTHSLKRTADNISIGMNNGEFVSQTEEPCNVPVLSLKKPPSSVLD... | Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Catalytic Activity:... |
A0A1H5K2B1 | MTDPKSTLAGSQGEPAASNPTPELIPAPAEYQFPTRKARRHAELTGMIPIIVPKNAAAEPAAGQQETGKNDAETTPGTSQADAPVEQVEAAEQVDTEQDKPDSPAAPLGEASGVGHSMDTELPMDAETDSENAPRPVSAMQVTGLPVIPVPQGPVGAMPEAATTLKAARTPKAGRDLPAAISVGVGLLVLVVVSLLFFPVAFVFVATVFACVGVWEVNRAIGTRGIKAPTTPIMVGALAMPISAYFAGAEGLLFALVASAAATVLWRSLDSEPGAVKSILAGVFSLMWIPFLLSFVFLMLRGDQQPILGLTLDLGNISPG... | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 453
Sequence Mass (... |
A0A7X8ZID2 | NQIVKKVNVLGDYFLIGDLDLITKPLLNQPFKKAAFAATLKNVSLEECIYKLTLTDFLEIVFEA | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 64
Sequence M... |
A0A4P7JHD4 | MGLAPGWEAATGRLMEYMARRLAYGGGFVLSVLALMVCASILGRALDGVGLSPITGDYELVEAGCAIVVFAFLPWCQLKRGHVSVDIVMQHLPPRVTAFSGLVGDILLTVVAYVILWRLWLGFGEKFPYGSDTFRGVSGSGRGRFFPKPPMNWRFRPGFPMACR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 164
Sequence Mass (Da): 17931
Location Topology: Multi-pass membrane protein
|
A0A8J5I747 | MGDVAKDRDWFVEKDRIGVPTWKEVRSRISIARLTWPRIDVKRALLITHPKVWSKVSSASLHNGQIFHGTYGSLSFMRRVKRTGRRLPTLAGQNRTNLPEWLEPAVPNLLSFPEENNGSLKKIPKLDDPSQYSRLGLVEGHSIILAIPQEIIDTHELQTITFVHRRECQRNDIVDSLVSPEFSDDGSTNGAVDSDPHLNDQDLQEFLHLLRLSGSGLKIMEAGQWRKLAR | Function: Plays an essential role in chain termination during de novo fatty acid synthesis.
EC: 3.1.2.-
Subcellular Location: Plastid
Sequence Length: 230
Sequence Mass (Da): 26158
|
A0A3A6NPZ8 | MPVRISTANVITLLRLPLLFLVVALLYLPGALPPFLALALLPALYLMDWLDGYVARFKNEVTSLGGVLDIALDRVVENVLWIVFVHLGKVPLWVGLVFITRSFLVDGLRGFALAKGHSAFGMMHSALGKFLVTGRFMRGFYGLAKGVTFGFLTLGLGLEALGPQAAGQMPLVFVAGPLLVYLSVFLCLARGIPVLLDIRRLVG | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 203
Sequence Mass (Da): 21978
Location Topology: Multi-pass membrane protein
|
A0A1I7X2E1 | MVLSTVFYLLTENLERSNMTLDPMLKWCGSAAAIENFNSEWEVIVLENNAVISQHGYWFVMGDMQNLLTHFSLAVSTVLHQSAFVHTYVNLLCRMQGMNMNWRIVRGEHRENDASEPVHRSFTLEFETYYLNKFYASKIFINSYLHMVSRAEYYAGMWVRNGNQLRVQAIIYAQAHINASFQTPDIDLIRYCAANVDADWFIEALIASFHLDDVFSLPEGGICCWGNILSPNVTDGTKVNCNDMDLTLGESMETGEINSLILVHSGDFMDDTLRGAGDTKGREHMELFMSLLAKIPSDNAKIINRQEWIDPLLSAALRFD... | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A8X6KQ20 | LSHFNSKMTCINEYYSPFRSPFNDVLGLVANSQHYVRCRELELNVLDCTDVYGRKGLTRQCALEYGDFLECLHNTKQNARVAAMQQERLRQYYAGERTKKNFYSEPPKLDSYYQTYTETIG | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
H6D863 | MLMSLLIRMELSHPSVNLMSEQFYNSLVTAHAMVMIFFMVMPTMIGGFGNWILPLMLGAPDMSYPRTNNLSYWLLPASFLFMYMTLNVESGVGTGWTVYPPLSSNLSHSSPSMDMSIFSLHLGGLSS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A0G0AR24 | MTNFWQKLSKPISVLSPMEGVTDTVFRERLCEIGRPDVFYTEFINVDGLVSIYGLSDLRLKFSKAEKPIVAQIWGNVPDHFFKSAQIIQNSGFNGIDLNFGCADKEVIKHGCGAGLIGDFSLVAKIIQSVKIGAPKLPISVKTRFAMNSNLTNDWIQFLLEQNLSAIVIHGRNSKQNYLTPANWQEFEKIVKLRNNLKSKTLIIGNGDVISYQDGLNKADKYKTDGFAIARGILQNPWCFLKTKIKDPRITQRLILLKKHVELYHQVWGDLKSFATFKKYIKVYIQNFPEAQALRMKLMEANNHQELIKLIEIN | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 314
Sequence Mass (Da): ... |
A0A1Q1AK53 | GMLGTSLSLLIRTELGNPGSLIGDDQIYNTIVTTHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLILLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRINSMSFDQMPLFVWAVGITALLLLLSLLVLS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A7X8WSM2 | MLILTGPSASGKTVIAKSLIKNHNMKKLVTYTTRPLREGEVNGVDYHFVSVQEFKQLIAKDFFFETVLYNHNYYGTAISDITPDKVVILEPTGLKQYLAKMRDKVKVCFLSCPKEIRFERMIKRGDSLEVIERRLANDDAIFNEEISSMADWVIPGEYGTADEQAQIIYNLYTNARKREQHENR | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Subcellular Location: Cytoplasm
Sequence Length: 184
Sequence Mass (Da): 21243
|
A0A1Q7AN34 | MRIGIIGAGAIGGAVIDRLLTVGVAKNNLIAWLAVPPLEMKKVLRAIRDALKHRPLIVSFAAAMPLTLIQTLLPAGTPAVRVNPNSPSLVGSGFNPVVYGKNATGSARALAESFVAALGTGYEVPDSKMNLYTALTAVGPTYFLPVFDALIAAGVAGGLSRADAVQAAVQTALGTAAMVSHRSEPPEQLKLYTGLRPLKDAEVRDLVSKAIAEAASRMNGLEPQIASQPDN | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A8J5KM43 | MTGAEVENLKREKDRDEEEKSSVKIRAKQRSRERSLAAMEIIDVGEANLLEQMDAIAVLRRSFPIVAIDTEFSGFLRFTPRRAAEECRYRDLKYNVDNLCIIQLGIALFDDAGNHPGMAWQINFSDFDPDVDPCSPASIDLLKNSGIDVQRNRCEGISSVRYAALIREKLFGHHGGAFVTFHGSYDVGYLIKLLAGGRPLPETSGEFITAASGIFNGRLYDVKYMARFCPGLLGGEVSLMKLASMLNVEADGVAHQAGFDSLVTGLTFQEMHKRWAVMDGRDSMILYGLENVCHEIKSASSLGPLRRPWTLPPGRFMIPP... | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Nucleus
Sequence Length: 373
Sequence Mass (Da): 41289... |
A0A3D2VYL1 | MRRMSPFAPGKSLAAALLEPTRIYARALKPIFGARLAKGAAHITGGGLVENTPRALPGHLVPDFDWNAWTRPAVFQWLQDVGGVPEEDMRRTFNLGIGMVLIVDAGAAGDVITTLEAGGERAFVVGALRNA | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + AD... |
S6CGK2 | MTTLRADGLPKPDMRRPLHFLAFGFGAGCSPKAPGTMGTLMALALYLPLSRLPEWAYLGVTLAVAASGVFICGWSARRLGVHDHPGIVWDEIAGYLVTMLWAPPGLIWALVGFVLFRFFDILKPWPIGWLDRRVGGGLGIMLDDLAAGLAALGLLQLLAHWLAP | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A452ZBW9 | SRPSRLSAPSPYLPHQQHSPTPVPTPGGSPDSQPNGPAAAAAKSDVKADASRPNAPAAVAGGSGTSTPSRTADDSSHPAAVDADATAIDAAGVNGGEAEDDGAVAEVRWETCKVRRGVSATDYIPCLDNIRAIKALRSRRHMEHRERHCPAPPPRCLVRMPAGYRLPVPWPRSRDMVRTFALAFVGKTRKRL | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 192
Sequence Mass (Da): 20307
Location Topology: Single-pass type II membrane protein
|
A0A453QV69 | PVCGEFIPGSDYCVNTHLDICLSRGAKRKLTQSSLLDFRFSKKTTAEPTPDILNNSDEAENKGLTDGDVSTDREFSSMNGVTGSPKDSGTTSLTGCLHGSPGISKTLNTCIPSNAGLPIIKNAENDDAVEKASSCLLSAGTTSVSIDACPDADSSTTVAVDTVIVGRRFRESFELQEGMGITVVRDPQNAKDPDAVKVLYAGSDCGQMLGYLPRELAKVLAPLLDTHFMECEGFVAGLPEQQLDNVPIQLTCQKCENDNQNYEDLRYQQSLWENFLGVVRNGNFQQPSGARYQANFNTMLLDVMTNHTHLFSDTETSFLG... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A352CCR6 | MDFYSIARFGHLIFVIAWMAGLMYLPRLFAYHALSAVGSDIDRQFQVMEARLLRIIMNPAMLASWGFGLWLFALRGFVDGPPLWALGKVGLAVAMTIVHMVFANWRKQFAQGNNPHSNVFYRVVNETPFLIAIAAIFLVVFEPG | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A8J5FFJ1 | MARSRTANCLSLAPSLLLWRPTAQSKSPPPCRRLPDPVSFPAASLSGQSSHFPTQASLSPWTPSVGHRTLSRRSLSTIRCPLFTTTRLVSTHDDQPHNEVLVEGKASTRAAILNRPSNLNALTTNMAIQLKKLYESWEDNPDIGFVIMKGSGRAFCAGGDVVALYQLLNEGKVEVCKDFFRNLYMFIYTLGTYLKPHVAILDGVTMGGGAGVSIPGTFRVATDKTV | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H... |
U1N145 | MGSRSKTDNKSDQSLLDILTDWYHLPVLLLIVGAMFAIRMQTYSNFIRDGEVFFSGNDAWYHFREVMYITEHWPSPIPFDAWTGFPYGKWVGQFGTLYDQVIATVALILGVGSPTQTLIGETLLIAPAVAGALAVIPVFFIIKSLSGRIAGIFGAVVLMLLSGTFLNRTLVGVADHNAVEPLMLAIAVFGLVVAFQKSEATMPVWEVVREEVFDNHEIDSIKMPLKWGLIGGALTGLYLWTWPPGIFLVGIVGIFTVLKISSDIVNERTPEPTAFA | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A1F3V441 | MKDEIFYTIVVSKMAADITAAKKMAKLTELAMQKFGCNGVEEFSLDEVSIDNIIGADAYAKDVLPANVVERIVESEKYNSSAVKFFFYGTDCEHNVEKFRKYLLQKNFFFQEISTLSSDWNAEWKKHYSPIKISDTLFIIPEWEKSNYPSSGHIFINPGQGFGTGNHETTHLCLQLLDELFLPKNPMVLDFGCGSGILGIAAIKLKAALVDFCDIDRQALDNCKENIALNFELSTLSGSSIVIRPRLNLGKKYTLVFANLLYPIIREEQKILASFVAGGGYLMLSGILNEQVDDTLALFSTSDFKLITHRKRQDWSALLL... | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 328
Sequence Mass (Da): 36769
|
A0A0V1MSG5 | MVLSNTLKDSVLLLIYSLKNVVPENNFSYGTVLTLLSRSDEPKKISTMSWRTRFGARNAGRDSKDRCCCRMCPLREGVVLIGAWKVIEFFFGSISLLSGYLHGGITPIWLAVGFLFETFLLACTLMLFVGLRRRIAVLLLPFLVLQILILISMFIIVMYSVWLLKGERSPLDEEMEVDNIFTNFTLHALLKGNKLDFHLSMNPSEAAQFYCTFVDKLRQNYREDLVKDVMSSKSNSLQEFMVICYPGIVKNVDKALESLGGMKEIEKHKAGSLELNFHRKSNVFSRPALSRPREGAFLIIRARRLIQASPSSSKQATYSV... | Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
EC: 3.1.1.96
Subcellular Location: Nucleus
Sequence Length: 672
Sequence Mass (Da): 77138
|
A0A0V1MKS1 | MIFFYHTVLKFLPINFIPCFVFGILTVIEMAVRSRSNSKYFFSSLQKGTSVLAVTTFNEWKKGVVYNNRYISVEKSKLLEYYIHFKDDDIRLDRWCRRCDIKPLEDCESDAVTDGQPKLKRSRRKDRSATPAPSDTGVVVKLISIIQFGCVALFPWYPSILQRNTRLSGQLWVCNRCFSYFISLKDYRIHLSSCPRRKTKGNKAYESDKIILYEFDGETDSVICSHLCLFASNFISSKVCAYLLAPFMFYVLYRKGVDGVIEACGYFSKEKSGDNGKALSCLCVFPHEQRNGYGMFLMEFCYELCKRNRLYGTPERPLSN... | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 429
Sequence Mass (Da): 49733
|
A0A453Q8P2 | FSTQSSSSSNSHLDAGRLAEAEKCESQLHAMIDQVSSQQDKIAALEEMKVRQDEERVQLKILIQDLEKRSLQTLINKNVVPVAAVVIMACNRPDYLQRTVESILKYQKAVASKFPLFISQDGTNGEVKKKALSYTQITFMQHVDLEPVRTERPGENVAYYKIASRCSSINECFLRS | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
A0A8J5F1T9 | MHLRQKHRCGHPITIVIAYDYPSAAHVDSAGIDALLAGDSAAMVVHDHDSTLPITLDDMLLHCRAAARGASRPLLVGDLPFGSYKSFASQAVDSTVRMLKGGMDTIKLEGGGPSRIGAAKAIVEAGIAVMGHVGLTPQAISILNGFMLQEKIVASAIKVTF | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
EC: 2.1.2.11
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Length: 161
Sequence Mass (Da): 1... |
A0A8J5FD65 | MVDFTLSELKSLGVKQRFSFGDQQYNESSQLSHLGGADAIALNANRIVGIYPEIKDPVFINLRCPSGHTLRFSCKNKVNKCPICRKEIGQIRCLALEKLAASFHLPSSYHHLGCIEMMPDYSKLQHKTHCVYQPYACPHPGSDCPFTGDIHELMSHLKQCHKLDLQAGSTFNHHYVKQDPHSVDNCSWTLTLFNCFDCYFCLHYEAFVIGCEPVYMAFICFMGEEFEARKFNFCLEIGGHGRKTK | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 245
Sequence Mass (Da): 27912
|
A0A8J5FTT3 | MERHSSWVRKTTGAMTITCLMLLPLLLLVTQSAFNTYLDRLLPHVIRERIGKKFTSITVKEISGTSFCCHQSYSFAGWKDGSLTPRDDDDDDKLLGGLLSGDFDESSCLSRYHAVSYWKNPSRPPSPHLAAKLRRYEALHKRCGPGTELFEKAIHHLNSSNHTAGKPTTDCNYVVWVPSDGLGNRIIALVSTFLYALLNDKILLLHLTDDFHDLLCEPFPGTSWSLPQDFPVGDLLNIYADPPWTLSNPQNAPYLYLHLTHDQRFSAHGFFCEDSQLLLRSFQWLLLRSNQYFVPALFRSSVYEKELKLMFSDADVFYHL... | Function: May be involved in cell wall biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 550
Sequence Mass (Da): 62385
Location Topology: Single-pass type II membrane protein
|
A0A8X6HIL2 | LEAATRLYKIEEPDHVCWDETHFGKMASWYINNIFFFDVHPPLAKMLIGLSGKLTGYNGTFPFNKPGDKYEDRKYLGMRLFLCTSWNFPHSFLLFNCLGVD | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Membrane
Sequence Length: 101
Sequence Mass (Da): 11788
Location Topology: Multi... |
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