ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A923UXU4 | MDTLLDALAKGDFDGLARCFEVAGLRVSLPGPGMLRIDAGAPASMRLLISVGVHGNETAPIEMMAQVLASLARTPGSLAVDLLIVVGNPVAIAQARRFIDADLNRLFGPERGSLGEAAEAARADLIMQASTDFFAVAAGQGGVTRWHLDLHTAIRPSHFERFAIIPDAAGDPAQAALGAWLGSAGIDALVFNDEAAPTYSAFTAHVLGAVSSTVELGRVGRLGDNALAPLARTRAAVERLLRGQAEPSGADLPLRFRVAQEIIKRSEAFAMAIGPDTHNFTEFAPGALIATDGPLRLQVGAVPEHVVFPNPDVLVGQRAG... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
EC: 3.5.1.96
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + su... |
T2STK3 | MQEIFLCSISNVRSGDCKEDCAYCTQSSHHQGAIKRYKFKDEKVVLQEARALRELGTLGFCLVTSGRELDDEKCEYIAKLAKAINKEELGLHLIACCGRADLEQLEFLRDAGIHSYNHNLETSQNFFPNICSTHTWEERFITCENTLRAGLGLCSGGIFGLNESWEDRIEMLRALASLSPHTTPINFFIKNPVLPIDAETLSA | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe... |
A0A0L0DKH7 | MSAVSPKREASEPADNQRPTKVAKPLDGAQSAGAPAAAYIRTKLPGFAPRLAIILGSGMGGVADAIEDKTEFPYSELPGFPVSTVQGHAGTFVCGTLEGVQVACLKGRVHLYEGTDPQLIRAPIYTFKELGCEIMFSTSAVGSLREDVGPGELFLLKDHINLQARNPLIGPNDPIGPRFPSLLNAYDPALRALIQAKAAENEINITEGVYLACLGPSFETPAEIKAFKILGADCVGMSVVPEVIVARHCDLRVATVSIVVNLAAGLTNEHITHDETLHFSGLAAGKVTQLVKSFIAANGEW | Pathway: Purine metabolism; purine nucleoside salvage.
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
EC: 2.4.2.1
Sequence Length... |
A0A0N0I796 | MHGFFFYLLAGNAFCLPAKAGSRGDRVCLCAENDSVCLMMLEWEGCAVGYPIVLHLRGRRAVVVGGGKVAARKVYGLLEAEADVVVIAPEAVPDIEALAAKGEIVWRKKTFAEDDLAGAFLVIAATNDRNVNEAVAQAATPGQLVNVVDDPERCDFHVPAVVRRGSLTIAVSTEGASPALARRIRRELEEQYGEEYGPYLQFLRKARDIILREMADDAARKQLFRALAADSFRQRGRWDEELAQLLANEKERNGERGRES | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 260
Sequence Mass (Da): 28618
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F4GIM8 | MEKAVSAKTMAAIDENSQEQYGIPGIVLMERAGLLAWKILREYINPDMSVVFLAGGGNNGGDALVMAREAFMEGFDKISVIACGSRISPSCATNRGIIHSLGLPFVDIGTEEPGASVEAILREADVIVDGLSGTGLSGPLRGNAATLVSLVASVRKTSREILKETRNVYVCSIDVPSGVGDDVPASAPVMRADRTITMGMMKYALLLPAFREACGELSIVNPGFPPIVLDAAQDVLHVADSEDFSLRPLDLSAYKKNRGHIAVFAGSEHYSGAAGLACMAAFHARCGLVTLYADKNVQPLIARENPSIITRTISSGEIAS... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q3JQU8 | MTTSMRERRRGIAFMRSCDDFLRTSELSIAAVNSLRRTIAPSHRVLDACGSGAACLLASRYGAKQVVALAAAEATLVGARAGANGPGERISFVDAEQAAALVARQGRFDVVLGLAGGGRDGLDPHYGARLDAFARRFGTANVAVVPNGVRYDAQLVEWREAERLEADVAARQRALEARYDLTLGPVLDQVAAGAAPRGRVRADALRALCARLPFLSCRPGDGGDAGTSGTSGTAAPEHVELTAAHGGRADGVLWTQELIHDGIVIERIQGCSWLDERVDLEAGDAIAVPVADMARAAPLDGGEAPPQLAPAPRASGAPAP... | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 503
Sequence Mass (Da): 53112
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A0A3T0EDL3 | MTASLPVMALATRTSPLAMAQALMVQARLAAAHGVSDAEAGFPILGLVTTGDQITDRALLDAGGKGLFTRELDRAQLDGEAAFAVHSMKDVPTHLPDGLELACVLEREDPSDILLTASGPGTLKSLPQGALIGTASLRRQAQALHARPDLQITLLRGNVGTRLQRLKDGPIAATFLAKAGLKRLGRPEGDWPGLDFAHSLPAPAQGAIGVTIRSDDDAARVALAPLNHAPTALAIAAERGVLEALDGSCRTPLAAHGVFEGDTLHLTAEVLKPDGSQRWRMNDTRTGIDTVEAARAFGLSLGEALRKDGGAAVEAILTGT... | Cofactor: Binds 1 dipyrromethane group covalently.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.... |
A0A3N5BLC6 | MKYLYNALQLAKFVEHQTSTNPAVGCVIVNNGKIVGMGAHLIKGEHHAEVHALKQAGLSASGATLFVTLEPCSHHGKTPPCTQAIIDGGVKEVIYAHRDPNSLVHGHHVLEEANIKTTHMPLAEIELFYHQFDITISKQRPYITIKTAMSIDGKMHLDNFDSSWITSESSRKDVHQLRHQYDAIAVGANTYHYDKPRLNARLDDYGQQPLPIIFTNQPRDILNDQHQHAILVGQYGLNPTTALSDLYNQDISSILIEGGPTLINQLLTQRLFDELIVYIAPKLLGSRHTIYENPHITSMEDIQHLTLFSTEQFESDIKLT... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A1V0RD78 | MKRLICFICLLPLSVVAAPSGGGDYDIVPRAVNFVIFVAILYYLLANPVKHFYKSRILKISSRLDEIQKKLLESKSKKLDMMKKLEEAKANAAEALVTAKKEAEILANKIKEETREELALLDRHFEEQKEFELRKMEKEVVSQILAELFGSKGSSLEQKEIVSIMMKKAS | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 170
Sequence Mass (Da): 19333
Location Topology: Single-pass membrane protein
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A0A847X9K3 | MAKPLTVSELSKYISNVMKRDPILSNFYLEGEVSNFKKSNGHVYFSLKDKEAMIRCIIFRNMDLSKECSIYDGLNIIIKGSIITYAGGSYYQVLVKKIELSGEGDIYKQYEILKNKLFEEGLFREEHKKPLPKFPQSIGVVTSSTGAAVRDIITTLKRRYPICNIVLYPAIVQGENAAADIIRGLEFLDRREDIDMIIFGRGGGSFEDLNAFNNENLLRIVYQMKTPTISAVGHEIDNMLSDYVADVRAATPTAAAEIASPNIKDILSKFEAASNRMNQRIKTLFKGEFRNLDYYAKEIEFYNPLMRVKDCERELAEKKA... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
E3GZ48 | MVAPATGGHGAPTKVAEVEIPPIRLIAFGTIGGLIGIYLSGIPVVGPVIAGLGGVCAIFWGADAVRRVASYGLGTGVPSIGAMLGAVGLLSTIMGVSVPLLSKAIPSLLAPIAALIIALIIGAVSGIVGRVFIKMEIPIFVQCTTELAGASVLSVLAFSSAIAGSYLMTGSGLLNPTLLTGYMPALYFMCAMAIQHPFNACLGPNEDQYRTLKCALAAGFAMMAIVGILSIIKNPYWWLISLVAAVGWAISMKMFVKDVFENTIVQRTGWWPEEEQ | Pathway: One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 2/2.
Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-cons... |
L0K853 | MGYNINYANRGQNLENMIETSNQQYSFQQRALIQKIPTPVKVLNINSRTGKITNGFYKKKSTVDYIGVYNGVSIAFDAKETSIKTRFDLSNVKQHQHKYLKQWNDNGGIGFLIIYFNKLDELYYLPFQLLDDYWQGMLQGGRKSIPYQEIAQKEFLIGSKGLVLVDYLSIVDKIIADKDNYNS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous ... |
L0K9K3 | MKVSYNWLQDYIDFDYSPEKLAKKLTMAGLEVEAIKYQGSAIEDIIVGEILEIKEHKNADKLSVCKVNVGDKNLQIVCGANNMKEGDKVPVAPVGTTMPEGMKIEEVKLRGVQSRGMMCSTNELDLPDDGVDGLFILEEDMSIGNKLTDELDLNDVIIEFDLTPNYSHCLSMIGVAREIAAITGNKLQYPKPKLEEIEEKIEDWINIRIEDEDLAPRYAGRIITDIKVKESPRWLKRKLEAVGIRPTNNVVDVTNFILMELGLPLHAFDYNQLAEQQIVIRRAKQDEKLVTLDDQERDLDPEMLVIADANKPVCIAGVMG... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 799
Sequence Mass (Da): 90199
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A0A2U1K962 | MDHGYNESEPRRSGSFSSSMRRNSFVLLRGGSHNEIDDENERRSVSEAGDIGCRELNSKRHSGNTSSRENVVVPIHGHSFDELPGSPASPGVILHDKDHNEEYRKELPMFLMTISSLIHLAAFGILGVLSRYLLEKLFGPQVAGVTNADSILYTDLFPNMVGSFLMGWFGPVFKGDISKFSPELAVGLTTGYLGSLTTFSGWNQNMLELSVNNHWVYSVFGFLLGLFLVAYSFIIGVTTATCFKQAIYKTNVCSKSGLSQVNNLGSQSILLLVMIALFGLLWGGSVALLKKDFNGDVSTSRLWFGCVVGPVGVWIRFYLA... | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 439
Sequence Mass (Da): 48309
Location Topology: Multi-pass membrane protein
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A0A2U9DPS0 | MLYFMFGLWAGMLGFSMSLIIRLELGMPGSLIGNDQIYNSIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLSAPDMAFPRMNNMSFWLLIPSLTMLITSSFINIGVGTGWTVYPPLSLTLGHTGMSVDLSIFALHLAGASSIMGAVNFISTIINMRMKMLMMDKISLFTWSTFITAFLLLLSLPVLAGAITMLLTDRNINTSFFDPSGGGDPILYQHLF | 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... |
A0A1F7K1Y9 | MISLIQRVTKGSVSIQDKEISLIRHGYVVLVGIFKDDTDSDVTQSVEKITNMRIMADENDKMNKSILKTGGEVLLVSQFTLCADHTYGRRPSFIKAMEPDAAKRLFDLYTEKLRETGISVQTGSFGEYMNVEICNDGPVTIIFDTKKS | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0A411WTE2 | MFRLVLSTVVLPLACLPSGAAAQAVQQSALRPAGVQAATIFSLWNFTLALCAAVFAAIVLALCVALWRAHKAGRAAGASPGLAPDLAPDLASLQQPERRVHRAVLWGTAIATVGLVMLLVADVWTGRMLARLPMNEAVKVELTGHQFWWEVRYPEEGVTTANELHVPVGRPVVVTLKSRDVIHTLWVPNLAGKRDMIPGRTTTIALRADQPGVYRAQCAEFCGLQHALMALPVTAVAPAQFARWTQARGKVAPEPATDSRRLGRDVFVRAACAACHTVAGTMANGTLGPDLTHLASRPTLAAGMLPNDRANLQAWIVDPH... | EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 349
Sequence Mass (Da): 37437
Location Topology: Multi-pass membrane protein
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A0A8S2A8J5 | MDALIAQLQRQFRDYTISLYQQGFLDDQFTELKKLQDDGSPDFVAEVLTLFFEDCVKLISNMARALDKTTGTVDFSQVGASVHQLKGSSSSVGAKRVKALCVSFKEYCEAKNYEGCVRCLQQVDIEYKALKTKLQDMFNVQSDESFHLCSQNVSESSCVWLLEDSFWCLLYLIRILRSCLVSMSIKEPSFMTEIVEDRENEMDEAATSLVMFSEQVYDFDLPPNDDDETKDLDQLTPIQEKILDCVEWILDLREMISHSGFEKSTTCSDVVAAQALPKLQSNSSRKCIICGKSFGCYQALGGHQRVHRPIRGKLVRQREY... | Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Location: Cytoplasm
Sequence Length: 660
Domain: Histidine-containing phosphotransfer domain (HP... |
A0A3N5BJJ2 | MKVYPSLLAANFLNLQRDIERLNQSAVDGLHYDVMDGQFVPNLSMGPFILKQIDAAFDLFLDVHLMIEHPDRYISDYANAGADRLTVHAEACTHLHRVIQQIKSHHMEVGIALNPATPINSILPVIKDIDCVLIMTVNPGFGGQSFIHSMLEKIDELNQFRAHHDLSFVIEVDGGINDETSRLCHQYGVDEVVSGSYLLASDDMTDTVKRLSND | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 214
Sequence Mass (Da): 23927
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A0A6L5WZL8 | MRVLYLDLGMGAAGDMLSAALFELLSRKEQEGYLSAMNHLRLDGVSVQAERSEKCGITGTHMTVLVDGSEEADVPDHAHTHVHAHHHHGLAEIHEMIGGLNLPDAVKTDAQQVYRLLAAAESHAHGVEVDQIHFHEVGEKDAVADIVSVCLLMRMIRPDKVIASPMATGSGTVRCAHGLLPVPAPATAFILKEMQIPCLSGTEGGELLTPTGAALAGFFVNAFGRMPEMTINGIGYGMGKKDFSRANCVRALLGQTTDDEDGQDGACDEVSELSCNLDDMTPEDLSFAMDRLFEAGALDVFTTPAGMKKTRPGVVLSALC... | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent e... |
A0A1G0YGC7 | MIAIPSVNPEDTHDASVSGELRLASFLSGYLSELGFSVRLHEKTPNRPNVIAEYGPEQPRRTILLESHMDTVGVATMKRAPFKAEIIDGRLYGRGACDTKGPMAAGLCAMTPEVLDALAEAGCRVVFVGAMGEEKGNVGAIQLVEAGIHADDIVILEPTNMQLVHAHKGTLWLNIHVSGVAAHGSNPERGKSAILGMQAVIEMLNRQIAADRERFCDPVLGRPTLNIGKIEGGAAVNIVPDRCRIEIDRRTLPGTDYEEALSNIGSGMRKLCSEGVIAGFDLEIIKNGVPFQTRADSSLVKSLSASLARKGQRVETVGAA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 377
Sequence M... |
A0A2P9FHK6 | MAGPTRRAPGREPGRGADAVPQRGDPYRPLGFAGVVTVDDRDGIVRTAVDRHSRFRMVTSACVADGRLVPGSLWGRGVAGCELPGPGDRAAVRPPRYAVDQPRSAGRRGGADASRRRTHMTVPHSGRAEAAEAAEAAEAPATPRTPARRPSPWHGQGPVVAVVAVGGGIGATARYGASLLWPTEATGFPWTTFWVNVVGCFVIGLFMVVITDVWAAHRLVRPFFGTGVLGGFTTFSTYAVDIRTLVGDGHPRTALAYLAATLLSALAAVWLAATTARLTLARRRR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 285
Sequence Mass (Da): 30090
Location Topology: Multi-pass membrane protein
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A0A6G1FA17 | MAVRSAAGTSRRLLPALLSPAGTCTRTHTAFLHSHATSFGYKQVPEEEKSKLVGNVFSSVASSYDLMNDLMSVGLHRLWKDRLISKLNPFPGMKHLDVAGGTGDVAFRVLERINSVSHVAMQGTLTDIEEDTQIYVCDINPNMLNVGKKRASEKGYKEGHCLSWIQGDAEALSFEDGSMDGYTIAFGIRNVTHIEKALSEAYRVLKRGGRFLCLELSHVDVPVFKQIYDVYSFSVIPAMGELVAGDRQSYQYLVESIRRFPNQEKFAQMIQEAGFERVKEGKSWKDVNTEWQMHSMAWRIYLGCSLARNLRSGCCFWSTG... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-methionine... |
A0A1G1X4V2 | MQTITTFDQLERIPLSERKFCYISEALTATVPIQDTGELLRKIENTSSYISLKSSNQSNIFYLRSGALDRLLHAARIINRRTKGEMKIALTDTFRPLDLQRKYFDEIKSEIQDREGLSGDALWERVTQFIADPDGCPPHSTGGAIDCTLVQASGEETDMGTSVDALSDAANTWYPHIPSDAQRNRILLFTAMTDAGFVNLATEWWHYSYGDQYWAAYKGAPCALYGSVASLPTD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 234
Sequence Mass (Da): 26191
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F4GIR1 | MSSMEKSQTSKTDNTGIAERQTERNVGEASVPVLDRIRSFFSSRSWNPREGIVVAFSGGADSSALLYLLSRLVPASSLVAVYVNHRLRPAEELAGEIAHNTCFCAKLGIEIKIVDSGEDVISNRAAQEGDGIEAAARAVRYEILEAERARLGFPWIATGHTSDDQMETILHRLLRGCSVAALRGIEPVNGSVIRPLLDVSGTVLRSLLKDKGLSWSEDSTNAMDDYTRNRIRHDLVPVIMDIFPSARETLYGFSKRAGAAARFMEVSLPRFADFFTYDEGNVSAPLDFLRSLERHVMGEAVFGLWNLLHQKEGRNPRKLG... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A133UXV1 | MAKIGELNKGSYVVYNGEPDHPRAESLKIRKKLAEGFKKGLVTPEGLSAHGRGEAFDYILGEKTTEQAKKAIKAGAAEILLADEPVFSVNGNVAALVPEEIAKINEKGGIQVEVNLFHESEDRKRKIGKYLKEKGVEKVLGTEIEYLTDISEIQSQRRKVDERGIKRADTVIIPLEDGDRAKALKKLGKRTITIDLNPLSRTAKAADVTIVDNIIRALPLLTEKIDKLCQTPSKKLEKILADFDNKRNLNLTIQSMLNRLEKLSEN | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the condensation of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
EC: 6.3.2.36
Catalytic Activity: (R)-4-phosphopantoate + ATP + beta-alanine = (R)-4'-phosphopantothenate + AMP + diphosphate ... |
A0A6L5GQB1 | MKGTRQSEILHIIETHKIETQEELARYLEQEGYRVTQATVSRDIKELGLIKVADKNGGQRYSVMQDMKGIYDERVKNVFRQSVMRVDTAGFIIVLHTLPGMAQAAAMAVDNLNWPEIVGTIAGDDTIFVALRNEKDKESIAEQFRKLMKGLL | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 152
Sequence Mass (Da): 17224
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A0A142Y0V8 | MVLPLDEIEFPQDGSEQDPSLPLAPSNTDPLPPRRDVLLEVCEEHSGKRIDLFMTLKLDGYSRVFLRRLITEEQVSVDGRPVKPAFKVFAGQKVAIDLLPPPPTDGPIAEDIPLDILYEDEGMVIINKPAGMVVHPAKGHWSGTLTAALAHHFQQLSDAGGATRPGIVHRLDRDTSGVIAIAKTNEVHFKLSAQFEARDVTKTYMAIVSGSLDRDRDWIHQPIGHHPYHREKMAIRSGHPSSRDASTFFEVKERFRGYALLEVQPKTGRTHQIRLHLAHIGCPVLCDRLYGGHAQVTRGQLLRRVAQGLPARPGDDTIEM... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 362
Sequence Mass (Da): 40413
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A0A212PWP8 | MKPRHIGMAFGLLGLLAMVGCSSSDTSTQPDPAKLAEAQASQKRLPSGFKLGKPYQIKGKWYYPEYDPNYQKIGIASWYGDQFQGLATANGEIFDKNQITAAHPTLPIPSNVRVTDLDTGRSIVVRVNDRGPYHGDREIDLSQAAARELGYEREGVARVKVEFLGLADGIQPPPGLVYASAKSPGAQPGRSVLTATALPARSTPKPPLNPSVPAYQEASYPEAATALDIQPRSERNFARAAVNPAKGDLTRSTPGMVAAVDDGRQRRMCVSGPQFVQIGAFADTERVRMAQDALEGLGDVRTDPVFVNQRAAMRVRVGPL... | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 355
Sequence Mass (Da): 38109
Location Topology: Lipid-anchor
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A0A8S2A8R3 | MALRMWASSTANALKLSSSVSKSHLSPFSISRCFSTVLEGLKYANSHEWVKHEGSVATIGITAHAQDHLGEVVFVELPEENTSVSKEKSFGAVESVKATSEILSPISGEIIEVNKKLTESPGLINSSPYEDGWMIKVKPSSPAELESLMGPLLKGFYKESCPLAEEIVKHNVEVAVLKDPRMAASLLRLQFHDCFVLGCDASVLLDTHGDMLSEKQATPNVNSLRGFEVIDYIKYLLEDACPLTVSCSDILAMAARDSVFLRGGPWWEVLLGRRDSLKASFAGANQFIPAPNSSLDSLIINFKQQGLSIQDLIALSGAHT... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
A0A6N2SDQ8 | MTIFIVPNLLKEHAADCTCQVANILRDCGCTALLPQELEPEFPGVSAIFGPSAELMHQCDMVLAIGGDGSIIHAAMLTLPASKPVLGINVGRFGFLAQLESSELHRLPEILSGSYQVEQRMLLKAEVTGPNRPAEQYYALNDVVISRPTLAKIVDIDISCNGKTVISYRADGVIFSTPTGSTAYALSAGGAIIDPVLDSISMTPICPHSLFDRSILFAPDKRITAQSRQVNNEAEIHVAVDGENVAVLKTEDRLVITGGDVYVPFVSLPDKDFYEILNQKLMFRG | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A212QSZ9 | MIAHLRGYVARQGETWAVIDVAGVGYLIHASARTLRQLPSHGEAVEILTTMQVSEEQIRLYGFIDEAEQRTFALLQTVQGVGTRVALGVLGVIGPDGLAAAVMAGDKAALTRAPGVGARLAARILAELKERLVDVASISAPTGTVAAPPGGESGDDALAALVNLGFGRSEAFLALGRVRSKVGGDAAIDLLIRESLKELTH | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A847X490 | MRLKDEELIEFTRQLVQRPSLSGKEQDVAEYIKTKLEELGFEEVRTDDMGSVTGCIKGNKPGKTILLDGHMDTVSPLDTTKWAHHPYSGEIEDGKIFGRGTTDMKGSLASMIFSIARFMEKKKADFSGEIHIACTVYEEVFEGVACKQIVKEIKPDMVIIGEATTSTIKIGQRGRAEIQVETFGKTGHSSHPENGINAVLNMNKFINELKKLKLTNHEILGEGILEITDIMSNPYPGDSMIPETCQITLDRRTLVGEKKKNVLKQVQDIVERLRESDTQFDGKAYLVQGEGYCYTGKRFKSERFYPAWIIDKEEKLVQAA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 392
Sequence M... |
A0A2R6AEW1 | MLIGRASKLAEEQVVLFLEDGSVFCGSLFGSPNGVPAIGEVVFNTGMVGYPQALTDPSYKGQILCFSYPLLGNYGVPKKEFDEFGVLKHFESERIQVSGVVARWVCESPSHYDSQKSVSRWMEEQGVAGIKGVDTRALVTRLREKGVMFGAIAQDVEQAKNALKERTLTPEFYKSVASRKITKFVGGRKGKIALIDCGYKLNILRSVLKRGYEVEVYPYDTQTKTILEDRPQGVILSNGPGDPRIWRETIELAQSVIDENIPLLGICLGLQIIALSQGAKTYKLKYGHRGQNKPVIDLKTGGCFVTSQNHGYAVSRDSLK... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 375
Sequence Mass (Da): 41473
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A0A9D1ULX2 | MSAPTVNAEKLARLAELVTELSVVHGKVTLSSGKEADYYVDLRRATLHRESSKLIGELLRELTADWDFVAVGGLTLGADPVATAVMHAGDDINAFVVRKETKKHGMQRRIEGPDITGKSVLVVEDTTTTGNSPLTAVAAVREAGAVVAGVATVVDRATGAKDVIEAEGVEYRSLLGLADLGLA | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidi... |
A0A0N0Z5J4 | MLDRPSVPDAEYDRLMQELIAIEEQYPELKTSDSPTQRIGGPPLEAFRKVTHRVPMMSLANAFGEGDLRDFDRRVRQEVGEAAYVCELKIDGLAVSVRYEDGYFVQGATRGDGTTGEDITENLKTIHSLPLRLKEPVSLEARGEAFMPKASFLRLNEERKARGEELFANPRNAAAGSLRQLDPKVAASRQLDLFVYGLANAEELGIASHSEALDYLQELGFKVNPERRRCANIDEVIAFISEWHEKRPQLPYEIDGIVIKVDSFAQQRELGATAKSPRWAIAYKFPAEEVVTTLIGIEVNVGRTGVVTPTAILEPVRVAG... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
A0A1V8M134 | MLGKLVKFVVGSRNDRLIKKKRKLVSSVNKLAEEFAKLTDAELQAKTKEFRVRLRDGEKLDSLIPEAFATVREASSRVFDMRHFDVQLIGGMVLNDGKIAEMKTGEGKTLMATLAAYLNALPGKGVHVVTVNDYLAARDSAWMGQLYSFLGLTTGVIISDLDHAQRKAAYAADITYGTNNEFGFDYLRDNMAFSLDQKVQRDLYFGIVDEVDSILIDEARTPLIISGPVEDSTENYEKTNAIVPFLKKVERLEGEKEGEEQGSGDFTVDEKSRQLHLTEAGHMHIEELLVEHGLLAEGASLYEPANIRLMHYLNASLRAH... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular mo... |
A0A2U1P3K4 | MGSNDDRVLIDISSDEDDHHADQTYDDPYDSDDIIHDDCSIGDDDDDDDAENDDVPIDDKKASNEKSYVVLKEDKLIEGQKDEIKKVTSVLSISKDEACMLLLKYNWCVTNVHEAWFGDEIKVRELIGMLDVDHDVKFPKNDETEVDCGICFDSVMVKDTANCGCGHVFCKVCWKSFVNTAINDGPGCLNLKCPEPSCEAAVGPDMVNVLAEGEEKKKYDRFWLRSYVESSQKMIKWCPGPGCDYAIEFDDNFEDDSYDVTCNCKYVFCFKCMEDAHSPLDCETVGKWVLKNTAEAENTTWILAYTKPCPKCKKSIEKNE... | Pathway: Protein modification; protein ubiquitination.
Function: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
EC: 2.3.2.31
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquit... |
R6XJT4 | MSNTIFSVKYLSQILDEVIRGSLFHNIYLRGEIQSKNVKGKYTYLTLIDSEDDGNVQASMTVLVSEYSRVQSKEYDVGDTVLLKGSLAYYKQRGTVSFWADYLIIDGEGKELVRLKKLKEKLEKEGLFAHEHKKELPLYPKCVGVITSSSGAAIQDVKSTLKKRYPVKIKVFSAIVQGLEASKSLYKELNNAMNDEEVDVILITRGGGSKADLAPFNDEKVARLIYSSKIPVISAVGHQIDTSITDLVADKTAITPTDAANLISFSLTELAERRFNAKNELKTLLKYNYENKLQQFHNYVLQLENLSPSTRINNLKSKLQ... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A3N5BJR4 | MAKVIHSIEVLRESLNTHRLNQQRIGFVPTMGALHEGHKQLIKTAREQSDIVVVSIYVNPTQFGPNEDFEDYPRQLDQDAALIDGIADYIFAPTDDVMYPLEESTSIQLNVGHQNTVMDGPVRPGHFNGVVTVVNKLFNIVQPDVACFGKKDAQQLAIIQTMANDFHMNIEIIGVDIVRNAQGLAESSRNVYLSEDELKNAPILYNTLTGAKQLIKEGTTDVNRVKEYIEKRIQCESLGQLDALDILTYPTLKHIDTIESTDESIVIAIAVKYDKARLIDNIIM | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
L0K8U2 | MDKIAIIANNKKEEISQVLLRVCNLLDEHKQDYILEKASAKLIDKQVENVNYKQIINYATKIIVLGGDGTFLNVARTFANSDVSILGINLGRLGFLTDIEVNKLETGLEKLLAKDYNIEERMMLKGEVIRDGEVIHKTVAANDIVVTKGPFARIINLKTMIGDQYLATYPADGLIVACPTGSTAYSLSAGGPIVNPRLESLIITPICPHTLHSRSIVIGKDEKVKIEIEADHKDIMLTVDGQNTFELAPQDTVRVSKSELITKLIKLKGYSFYQVLRNRMNENKF | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A917CBT8 | MAAAESGILADVRTFAPGIMLDIRYATADNFTGRPVPGYAAAKCLLHRPVAEALARVEQGLRGQGMALAVYDCYRPTVSVAAFMAWAKDADQSTKAAYYPELDKSVLVPDYIAEKSGHSKAATVDVGLLDCRTGTCRPFDMGTAFDYFGPRANTGYPQLGPAQRANRTVLLAAMAAEGFENYPMEWWHFTWRAGELPDTAYAFPIE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 206
Sequence Mass (Da): 22429
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H0QIA7 | MHSHSQPHGDSAVRSAMPHAGAAGAAAPPSGDAGTHEHGTHEHGTHDHGAHRSVADHRRAVRELLEPLLSPERTERLPLVQALGRGLAEDITAPLSLPPFPNSQMDGFAIRSGDVPDGGADLRVAAPVPAGAKPAPLQPGTAVPIMTGAMVPDGADAVVPVERAVPSIFPAAGEEAEVRLPATAAGTFIRAAGSDIDAGQQALAAGTCLGPAQLGLLAALGLPEVLVRKQLSVLLVTTGDEVVEPGEPLGDGKIYDANGTLLESALRQAGLDVTRAGISADSPDALRTLLRTHTSAVDLIVTTGGVSKGAYEVVRQAMDG... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 450
Sequence Mass (Da):... |
A0A6L5GTK9 | MGRNCMQIKKVALIGAGAIGGYFIWGLAKSMGDNFMVVAEGERRERLLRDGMVINGAHFPLNVQTPQQAHGADLLLVATKYAGLPSALPEIQAVTDDHTIVMSLLNGVDSEEIIATAIPERQIVNAYMKISSMRTEAGVVFDPEVTTGLMYGEKHTPEKTERCAAVEAFFADKPVRTTFVPDIMTQQWTKYARNISMNLPQAILGVGIGAYEDSEYLLAYSKKLEDEVRTVAAAYGYPLEPLERPHMGYRKLNRYSTLQDLDAGRHTEIEMFCGVLMKKAAAKNIAVPYAEGAYDLIKTLEEKNDGKFDYAEDET | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 315
Sequen... |
K7S801 | MSKLKLLFYLLLLGGIIDIGRYFIYPNISDLKEIKPIPTAFMEYRQEEWAEQNRDMEITHKWVPMTKISPNVIKAVLIGEDDKFWNHDGFDVKGMEDAIERSLKKGSVAGGSTISQQLSKNLYLSPSKNPVRKVKEAIITWRIENTLSKRRILEIYLNVAEWGDGIFGIEAAARHYYHKSAKNLTGREAARLAAVLPNPIKYNPTGSQKYVKNRARIIYKIMKRRGIVIPQYQEVMSPPKTEETLEGSSENNDSITELFGENVAPSEESNPFEQTSNLPSDNEVGAEGNGSLTF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2... |
A0A3P1XVQ6 | MQIRSAIQDILPEQLVESNPDAEITGATHDSRRVQPGDLFFAVPGFKQDARHFIADAIDAGAVAVVCEELPEQLDPAVNFLRVKNVRAVIGPIARRIYGEPDSGQQIIGVTGTNGKTSVAYLLSNLLRAAGKNTTTIGTLGVDDGKNINYTGNTTPEATTLMRELKRVADHGSTHTVMEVSSHALDLHRVTGVRFSALVFTNLSEEHLDFHGTMESYYLSKKQLFSEHPETPAVIDIDTEYGARLAKELREENPERRVITTSAHASPAADTIATEITTDLNGSRFTVVNKLTGENAGAETSWLGVHNISNSLLALVVADL... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosyn... |
A0A3D0W959 | METVSTARAFGGTQGVYRHASAATGTDMTFSVFVPDHPAGARLPVVWYLSGLTCTHANVTEKGEYRRACAEHGLILVAPDTSPRGEGVPDDPDGAYDFGLGAGFYVDATKAPFDRHYRMWSYVTEELPALIGEQFPADMDRQSIMGHSMGGHGALTIGLRHPDRFRAVSAFAPIVAPSQVPWGQKALAGYLGDDRAAWRRHDAVALIEDGARVPELLVDQGEADNFLAEQLKPDLLAQACEAAGIDLIVSNAGVADPVIGPIEDASLADWRRWQDSHVTGAFLMVRGAVPRLRQRAGASIVLIASTRALQSEPFCEGYAA... | Function: Serine hydrolase involved in the detoxification of formaldehyde.
EC: 3.1.2.12
Catalytic Activity: H2O + S-formylglutathione = formate + glutathione + H(+)
Sequence Length: 419
Sequence Mass (Da): 44808
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A0A897NGX2 | MTVAVVQFGGSNCDRDTVQALEALEIDAERVWHEDSLPEDTDGIVLPGGFSYGDYLRAGAMAAHSPIMDEVKEAAEGGTPVLGICNGAQVGCEASLTPGAFTTNESARFQCEHVHVSVENADTPWTRQFEEGEVIELPIAHGEGRFEIEDDRLAALEDDGRVLFRYCEADGTVTPEANPNGSKHSVAGVTGEAGDNVAVLMPHPERATLPDIGVTDGQGVLEGFRTD | 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 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A2T4VYF1 | MRNTLKVYNTIERKIIKFQAIDPLNVKMYVCGPTVYDFAHIGNARPVIIFDVLYRLLRYIYGIKCVTYVRNITDIDDKIISRARQEYPSIPINDAIKTITQKNTKQFIHDTTKLGCLSPTYQPRATEHVPQMIYLIKEIITNGHAYESNGEILFDTNSINNYGSFFQRRIEEQKIGARIPQKKHKRNPADFVLWKMSSEEEPGWESPWGRGRPGWHIECSAMCSHYLGKVFDIHGGGIDLIFPHHENEIAQSCCAYRTEKLANVWIHNGFLNIEGHKMSKSTGNIVTIHELLETKKFGKQSWSAPVIRLAMLMTHYREPI... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 462
Sequence Mass (Da): 53000
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A0A7S4JEC7 | MEPENNPSIQRRESEDVFPENIVSHRVESARRSEAFSPAFLSPRMWNEEDMLLPPSSEVPKRPVIRDRDSQDKGCFGLYTFIMVLFLIQGIAAILGANYQLPHEFELCEARLAQEKVAVARDIPEAEVIQHALEGRHENFQTGGKRLARLKVVKKSHANWDPWSHRLRSVAGKQLAEEPGSFQVSHGHARKLLSSNMLPQSLKQLLKDIKLQASTGLPSHALRNGTSLAQSNSTSHGESNSTKKEKEQNSEEGDFQDDLSPEQVLENAYKRVRNASGIVALLAFSSIVFGAIWVLLLGRFTTAFVYITLSALPIALFCSA... | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 489
Sequence Mass (Da): 54697
Location Topology: Multi-pass membrane protein
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A0A101G8N5 | MKHTLAVLALNKPGVLARISGLLSRRVFNIESIAAGYTEDSDISRITIVVNGDDQELDQAMKQLSKLIDVIKVQELFKSGSIDRELVLIKVRADSARRSEIVDIVEIFRANIVDINRETVVIELSGGEEKINAACAVLKRSVKPQEGLQMPPVIGITCSWDDVSQRHFLGSLYCEAVRAAGGVPVLLANYEKEEEIAELLGIIDGLLLSGGKDVDPFYFGEETLPECGEITPLRDAFEIKLARMAIKGQIPVLGICRGAQVLNIAAGGNIYQDIKTQLTCCLKHYQQAPGWAATHRINIEKDSLLESILQVSEIMVNSYH... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 383
Sequence Mass (Da): 42039
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A0A0L0DA59 | MGLLGQPQAPAASAAAKAAVDLVLDGSPGAPPAARMVVPLSSGPVSFHLGAGDTVASLVDSLVANDPSLSVDDVVLRSPSGVALAGSTPWASVLRESSVAAGAPLQLELSGEVHSLVPSYDGTKARLGGSLDITQLLKKEDFAAVAKALRRDTRSAMPKQEFVELCEKYEIDELEAEFLARSLAGCGSILYFYDEPNLASTLFIKPRRVFKQLHRTLNVMTPNEIAAANPKTELLASMEAEIEPLTEIKSTIESKSAASASRMMFLGFAGVVAQLGIITRLTWWEFSWDIMEPVSYVVMIGQAVLLYGFYNVTSADPDSY... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
G0A0C1 | MAETEPKEAEKKSSKKLIIIIVAIVLLLGGGAGGYFFFMNKPADSEQSDKKSENKAAEEEKEDDDPAQAEQYYELSDPLLVNFPPGSSAKIIKVSVTVLVKGEENAATLKKHEPMIRNNLLMAISSIGADKAKTLEGKQELQATMLTEVGKVMELMTKKNPVKAVYFTEFVMQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 173
Sequence Mass (Da): 19013
Location Topology: Single-pass membrane protein
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A0A0D7AL67 | MLSSLSRQILLCLFSVAVLLVCYFCTVDVATKLSPQGCRMSRMTPSYVLYKKFNTSWTPLAERYSLWLYREVGWEDTKIGGGRPVLFIPGNAGSSRQVRSIASSATRQYYTSPGVVAPEFASQHRVTPLDFFAVEFNEDLSAFHGPTLESEIAYTTSAVEYILSLYPTGTEIVVLGHSMGGIVATALPANRIAAIITMSTPHRLPPARFDARIDVLYEAREIVVPLVSLCGGATDMMIPSEACVLPPAPPGMFYRTVFSSALEGAWTGVGHQVIVWCHQVRWRVARAVLEMATASSPVVALDRWLRDGHELPFALQQQGV... | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 960
Sequence Mass (Da): 105753
Location Topology: Multi-pass me... |
A0A1W9LRY8 | MVQKELATVQDKVASIIKGHLGLDISAEALKQIENFLEEFDLNSVDALELLLKIENEFDIEIDDEDLNAELLKSVKTLSNYIITKL | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
A0A2U1L361 | MTNKIQPQQFPTITENLLSFDSMFHQLHTLLILLATMGNSRLFQLIFLIITSILTSIDASAKYLHRNNHKNPPPPPLTLDYYAKTCPRFHEIVRTTVVPKQLSHPTTAAATLRLFFHDCMVGGCDASVLIASNAYNKAERDYDINESLAGDGFDVVTRVKMALEVECPGVVSCSDVLAITTRDLLIQVGGPHYEVKLGRKDGLESKASNVEGKLGRANMTLNEVIRVFESHKYTHREMVALMGGGHTIGFAHCKEFESRLFGPKPDPSVHPKLAERLKAMCVNRSKDPSVSAFLDPISAGNFDNMIFKNILNGLGVLGTD... | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 694
Sequence Mass (Da): 76879
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A0A2U1LQH4 | MNKPIETEVSEDPPKDTWMKHEQSQPATGEAKSEPEDGEMVSDSIIGQEDSVGFMAEEAAIDDIPTATTMTAIVVHPVAEKPSITSSMAETGAGNQDGSDVSIVYTSGPTEVKPEEPVAYTVSTNINLNERAKLRFWQRLAGNQPSPPFLGYAAPSLQVQYYTSNAYSPVQDVTDSCRTEAVTNVIFGLIIPIFAIVVSIFVSFTFATMYGVAVAGIGMLNAIATGLAIDAYGPISDNAGGIAEMAGMSHIIRERTDALDAAENTTTAIGKVVYYLE | EC: 7.1.3.1
Subcellular Location: Membrane
Sequence Length: 277
Sequence Mass (Da): 29484
Location Topology: Multi-pass membrane protein
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A0A0L0DQH2 | MDTCSAAAGWRAFYLVGLAALFGLLLLDLTKLASADVVVLFALHLLQRAIETWCVHVYSPRKLSLFHLAAGVGFYLAMPMAVASAAVAAAGSSRLSLPPAPPFSPPFSLARLFKSLPMLPLPVHGHLAPVRGEVIVYFAIAAAGRWHHALTTGVLFVVINLAVTASATAEWYVAKFGQDAIVGKARLIPGVW | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-gly... |
A0A317FDL7 | MSASPSPISAPGWCGRRAVASTALRSGRNGPRDASKRTRREQDRPSRLRLWLKRRRGLAKPAALGLLGFGALAAVGTGLYLADPAGRMQALVENAAQFGDAAGLEVREVIVEGRVNTPRELIRAAVGVERGDPMLGFSPAEARERLMTIAWVENADVERHLPGTILVRLTERTPFAIWQNQGRFAIIDREGRVVTSETLDAFGPLPLVVGAGAETRGAALYDLLLAHRPILERTQAMVRVGERRWNLKLHSGTDVLLPEGHEAPALNRLAEMHARNALLDRPLVAIDMRLPDRMVLRQHPPAEPPPQAQRRGGRSG | Function: Essential cell division protein.
Subcellular Location: Cell inner membrane
Sequence Length: 316
Sequence Mass (Da): 34537
Location Topology: Single-pass type II membrane protein
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A0A7S4PGA9 | MTQKRRALGETINHEIRFTKELFTSSGEDFPNQMRTKDGAPHFSKRLFEEMSKEINGMGEYPYRPGTHLEFGSPQLELLKHLCHVFSLDSDISSEVASMKRGLLKLLQVREFSVEAQFKNPARSVILPDLFCSSVLCSASR | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 141
Sequence Mass (Da): 16067
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A0A6N3S6X6 | MFHSSSNAWLELQWYMFGAMFLLTAGYTLLKNEHVRVDILSSRLPRHKQIWIEIFGVVFFLLPACTLIMVLSWPVFMDSYLSGEQSSNSGGLIRWPVKLLIPVGFALLVLAGLSHLIKCIGFLRGQCPDPTAREGSKSAEELLAEEIAREALEREASVQEQRNNHEGR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 168
Sequence Mass (Da): 18989
Location Topology: Multi-pass membrane protein
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A0A8S1ZG10 | MQYVKQTPYYDLQVTTPCKRCTPKVVGSTLYSSRGDMMITFTFFTGSEGESNYITITRSVHHPIPFYALCKSEEYKHLMKNEDRENMKWLKVFNKCDLYSKRKIRSKHTTTYGHTVAGLLTNKNVKSERQDVNP | Cofactor: Binds 2 iron ions per subunit.
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
EC: 1.13.99.1
Subcellular Location: Cytoplasm
Sequence Length: 134
Sequence Mass (Da): 15659
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A0A6G1BQH7 | MMLLSFSDVALTSAASTFEYVSHGLRPCVLMSPVRKKAPNPPCRLAATIEPCFHTPPHYDGQARTKGDSGRSVRHIRHGEDLKDGVQLVERVAWHSIVRLFICSVLCS | Function: May be involved in cell wall biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 108
Sequence Mass (Da): 11959
Location Topology: Single-pass type II membrane protein
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A0A0L0DPA2 | MDPKLASTVYRTLLKRTSTFAVLIAGGAIATEMVLGNVIDGFYWGKNKDRLFENIPAIRQQREEAAE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
A0A2U1MUN1 | MNLFPMAETPRATMQQPPAKQPMTIFYNGQVVVFNDLSPEKVEEIMKIAESGQKKPVVKIEECSKNVIVPNSDLPIARKASLARFLEKRKDRITARSPYQVQESPKQEDSKTWLGLGAQSHVQ | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 123
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 13895
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A0A7X0MQ24 | MEPPGKIEAAIGARPAKWLFGLVVGMGVATVALLIRMKIPFVIAGSQAIFSYPAIIIATLLYGARAGSVAGIICLPFLWYFVVAPRRSFAIESWPAAITLVMYVLVGAALVWGIARMRTSLRRHRALVVDLESEVGRRTAERNQLWERSRELLAVVTAAGSVRIVNPALAALAGIDTTPMGRSFESLLVAEDRHRFRSMSGQDGLFEARLTTPDDPAWISWSCTAGDGETYLVGRDFTAEHHCAEQLRQSQKMELVGQMAGGLAHDFGNLVPPISMTLHLLGKRHADDARTRELIGAAEESVERAATLIKRLLALSRPSS... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 467
Sequence Mass (Da): 50115
Location Topology: Multi-pass membrane protein
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A0A6N2RM15 | MSVFQDFIKPTLVLAVICLVISFALAKTYSITQPIIDRLAIETANAARAEVLPGASDFEQLTVANMPEGGLDAYRATDGSGYVITTAWKGYGGTIKVMFGMDANGVITGAKVLENSETAGLGTKACDPKHMVQYTGKTVDTLGEVNAVGGATVSSTAIMNAAKAAYRVYNEVGGEGAAAPQRAPAKEETLRAIYPDAQEFIPLDMEVEAYRVDGKEHIVVISEPSFHDDIVAAVGFAEDGTITGVALDYINENPDYGMKVARPEYLEQFIGKTSADEVASISGATSSSDVLKKAINKAVAAHPAAQQAPELQKGAE | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 316
Sequence Mass (Da): 33246
Location Topology: Single-pass membrane protein
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A0A8S2B223 | MILEKATDSRKGSEKGPAEWGKLNPQWKVCSTGKFQSPIDLTDERVSLIHDQALSKHYKPALAVIQSRGHDVMVSWKEDAGKITIHQTDYKLVQCHWHSPSEHTINGTSYDLELHMVHTSDSGKTAVVGVLYKLGEPDEFLTKVY | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
EC: 4.2.1.1
Subcellular Location: Plastid
Sequence Length: 145
Sequence Mass (Da): 16314
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A0A6N2T3F3 | MTNTVYSSRTRKTRKMVMTAMLAAVSSVLMFFSFNVPLMPGFIKMDFSELPALIASFALGPVSGVAVCLVKNLVNLFFTTTGGVGELSNFLLGSLFVAPAGIVYRKIKGRKGALVGSLIGAAAMAVCSVFSNYYVVYPIYTAFMPMEAILGMYRAINPHVENLWQALLWFNMPFTFLKGMCSVAITFCIYKKISPIIKGQ | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 200
Sequence Mass (Da): 21880
Location Topology: Multi-pass membrane protein
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A0A2P1LA17 | FLSLGMFIGDGAGTGWTVYPPLSNNIYQSSPSVDFSIFSLHLAGASSIMGAMNFIVTILMFCRCSYDKLSLFSWSVMITAVLLLLSLPVLAGAITMLLSDRNLNTSFFNPIGGGDP | 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... |
A0A8S1ZDK8 | MATYIFDPICDSSWVANTLTWLWGKIPWEDDRRKSTERFWKETWKLKDAKQLTEWEKSCNILFGMKPTSSEMNLSYMPNYKGSVDFMFEKQKPTQFFVPTGTFSVSIPMKVPGLHASYRFMHPKGKRDKLELQYEGLEHWLFKLKLPLSLTERPTIVFSVTPNYEAFSLPCEIKLEGNLDKRIRACRIANWSIGLTSDASIFSFAFKITKSTASCKAKIHGLSASADWDGEDLKCSFEQEIEKFSITSKCQINVKDAMKNVCSVGVGKMWDDDEKGFHRGIQVVFDTHDVATITYSRSLTKKLSLELSATVDHSISGVSG... | 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: Membrane
Sequence Length: 566
Sequence Mass (Da): 63909
Location Topology: Multi-... |
A0A142Y896 | MSNVPDSEGKFIKMAQIGVLQTQGKLRTLLGSCVGIALFDKKLKLIGLAHVVMPCSMGTSDSPGKYADTAIPEMIRRMNKLACGSKLFLTAKIAGGANMFSYTTASPSATIGEQNILAVEESLAKEQIPVLGRHLGGSFGRRMVVDAESGIAHIHVVGYATVQF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 164
Sequence Mass (Da): 17383
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A0A142Y7Q0 | MGGRMSRCFDRSQHPDGSTMEHSFIAWAKQRSSKLPQVKLGIGDDCALLAGSADDCVVTTDSLCDGTHFILSECGGRRAGRKLLGVSLSDLASMGATPVAAFLSLCLPRASAGDIAAEVFEGVLEMAREYAVAIAGGDTNVWDGPLALHLTAIGSVAPDRAWKRSGAKTGDAIVVTGTLGGSILGKHLDFEPRLRLANQLAQLDIVSAATDISDGLGIDLLNMTVASRCGAEVDLSRIPISDAARRLAESTGRSPLDHALGDGEDFELLLAIPKEKVDRLPAVIGGVPLTRIGEIVGRTGLWSKEKGGVKQLPPRGYVHG | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
A0A0L0DQ99 | MEMLNAAMSYPSTFEWIPGTTLLSTRPVMFGTLIVYLLVIFGLQEVMATKTTPSWVKPAIVVHNLILFLYSATSVITVLYLAISYSLEDEYGFVSVFCDQYRKYTSGPMYFLIYTFYLSKYYELLDTVFLALKKRPIIFLHVFHHVLTLYTSFSGMDSETTYQWTAVLTNTTIHSFMYYYYLRAAMGAKIWWKKYLTVAQMIQFGINVLILFGWAAIDLNLPEGQDCAGNYFCWWLMFGGMIAFFTLFKAFFNKSYKKPAAKSE | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 264
Sequence Mass (Da): 30633
Location Topology: Multi-pass membrane protein
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A0A1G1WC99 | MARTKIQIKPKVRKIAEGKTKIIYPFPRNKSLVRIVHKDDITAGDGVKRDILPGKGVWSSTTSSNCFKLLTAAGVPNHFVEDGKSQNEQIVRRSNMIPFEVVARRIATGSYLKRNPQVSEGHRFEDLVTEIFYKDDSKHDPLVEYDTQTGEWVFFNAKFPKRAGFMETVKQIKLQTGKVIKPETVDEMFTILRDVFIILEHAWASHNITLVDLKIEFGFDVKGSLMVADVIDNDSWRLWPGGEKEAMLDKQVYRNLVSTTKDDLDAIARKYQLVSELTDNFVKADAGAVVIIAGSGSDAEWVEKIEKHLSGFPRINVQKI... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
A0A0N7ANR4 | MGSSEIVDSGRVNSGPVKSSFSQTCNLFSQYLKENNNFPDLSLGRRVLTPSSTPTMNLFPMAETPRATMQQPTAKQPMTIFYNGQVVVFNDLSPEKVEEIMKVAESGQKKPVVKIEECSKNVIVPNSDLPIARKASLARFLEKRKDRITARSPYQVQESPKQEDSKTWLGLGAQSHVQ | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 178
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 19819
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A0A7S4H9L0 | SEAFGLGKRQTGGPCSGTRREERRVQERGDEHEEGNMICVECGQPVNDLHHQFRGAGIRLTRCEYCGCVADKYVEHELVIIFLDLVLHKPQAYRHVLFNRSEYCDAGISSRDAQLAFFAVILEAYSHTQSRDNHNSWAELAQSSAWRGYTPPPEAWKEYALLLLFCLAKLCIFCILSVTAAFVLFQRKYPIIKYNYLVKSIILSNFGRCFCVLMMIWDYDSPRFLLTMINLFVFSSNFVAIQVWTGSTRMAPFFILLAGWSARLLLETYVFTGLGETESICVHNSSHAFFRLQTNCWAAIASERHGYHVFLILLLQTWPC... | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 325
Sequence Mass (Da): 37319
Location Topology: Multi-pass membrane protein
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A0A2U1N203 | MDFSKLDSLMHQFKSSSTSIGAKKVKTECIHFRSHCKARNAEGCKRTYQQVKKEYSTLKKKLETFFQTHKSETDGGGVAAAREMNAPAAVFEQGVGVVEVMGEQRRWASGEGGGFAVVVLGGAVWGRRVGLTCGFDLVKNGGGGVILNGVKWFGYWAGICELGHGV | Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Location: Cytoplasm
Sequence Length: 166
Domain: Histidine-containing phosphotransfer domain (HP... |
A0A2U1Q524 | MDFRSWLIMTVILALFQTNFLRSDAAGNVNFDANYHVTWGNDHVLFLDQRREVQLSMDQASGAGFASNAFYASGFFQMRIKIPNKDTAGVVTAFYLFLNTTVHDELDFEFLGNRPGKPVALQTNVFTNHVGGREQKFNLWFDPSADFHYYKIVWNHHQIVFFIDDIPIRIFKNNGHKGVGYPNKAMQVIVSLWDGSSWATDGGREKVNWSSAPFQAHFQDFNIDGCVSTPDSPNKECYSQKHWWNTEQHWLLNPQQQKAYYDTRKKFMTYDYCADRNRYPHPPPECIG | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity.
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construc... |
A0A6G1BQX6 | MRRRGRRRSASMSSGREISPSRSPIGERSSCPSCFLTPETCFLQGKLADVVLGYDTVAEYVNASSYFGALVGRVANRIAKARFVLDGKVYHLYANDGDNTLHGGHRGFSKVIWTVKEHIGGGDTPYITLYYHSFDGEQGFPGALDVYVTYRLSSPYVLSVHMNATAVGKATPVNLAQHSYWNLGGAGSGDILGNTVQLFASRYTPADADLIPTGQVAAVAGTPYDLRAPTPVGARVHQVTGGSKKGTTIYGFDINYAVDGDDAAHDALRRVAVVRDGASGRAMELWANQPGVQFYTGNFLTAGDKGKGGKVYGQYGALCL... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 355
Sequence Mass (Da): 38240
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A0A6G1DKU6 | MGRAPANREPSPPPPPPGRCNFWLPNKRRHCANSPLPTSHYCGNHLPDSASDAGALSRRRVPCPVDPSHTVLEENLEAHVSKCPLKKQTAALAAQPFYSKGINSGGGEGGGGVTSAAKRAAVHKLTEDELHALIEKIKSVHATAAVAMRDSYLVADACDNWMRNQVDRCVFATFDGVKVGIF | Function: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
EC: 2.1.1.225
Catalytic Activity: adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 182
Sequence Mass (D... |
A0A7S4JIN1 | APAEGSHLLRESILSLLRMLSSAHENCRRVIESSRIFEAAAAESDEAEVARKREEVARRKEKIMEEMRKQQLAAAAQHNLMSDEESSENQGGGEMTGGCYSDPLAKIEGDECSLCQESMAALDATWSRKEPSTDTWIPYDETTSRELERADLEGMESVEIFVGGEIVVVDLKRRRQSAPLCMGRSSGGKVRELPIRREESMVVIIGYARPAAVLLEAFEGAARPVTISSCGHAVHSGCLERYASTLQGRRNVIVHGQTYENANSIDMAAGEFLCPICRRISNLTIPLPSPTDTAMLDYLASLEGSGSTGGAEGSGQEERR... | 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.
... |
A0A2U1PYS1 | MLELVTFEELKSKKFFVQHVETVSSSEVAVDIIQSFVASKPDSTDALETKTKHEDQRRSNKTDNTDAKEAHSLSCYLRNTDWACGVAVYTGNETKLGMCRGVVEPKLTAMDVMIDKLTGAIFIFQIVVHWYVLNAEEGPWYELLIIPLRFELLCSIMIPISIKVSLDLVNSLYAKFIDWDKQMVDVETGTSANATNTAISEDLGQVEYILTDKTGMLTENKMIFKRCCIAGTFFGNENGDALKDVELLNAINTGSPDATTVMAICNTVVPIKRKGFNIVMTTSLSSDVPVGYFSWVEYDIMAPFQPKTEKALAAAFISNC... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 420
Sequence Mass (Da): 46671
Location Topology: Single-pass type II membrane protein
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A0A1Y5T1R0 | MTKPTSVVQKFLCFPGKLVSWLVIPLALSIVLSVIAARQGWSVLIDWEGSVPLFGEALTVNSLVDLQWYIFSAIVLFGGIWAHLEDRHVTVDFVALGFSARTRTLISLFGNLFLLLPLCLLVMWFGSKFAMTAFATGEGSIQGGLTAHWLIKGALPVSFGLLGLAALLRAAQALRQLITKQYGDIHDATPTSGD | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 194
Sequence Mass (Da): 21031
Location Topology: Multi-pass membrane protein
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A0A0N0I8D8 | MFFCLFSALILRLGVVQIVYGEDYRREVERTQDEIVSTPVPRGKIYDRFGRVIVDNTPQKAITYTRSKTTQPEEILDVARKLAQYIDIPDAEKKVTERDMKDYWILTHPEEAKKKVSEQERKKLADQGLTQKEIDKKVYEWTLDRITKQDLAQISKSELEVIAIKHEMESGYALTPQTVKSKGVTDREYAVVSEHLGELPGVNTTVDWDRKYVYDNTFRSVLGSVTEEDEGVPRERLDYFLARDYSRNDRVGKSYLEMQYEEVLHGKKAKVKNIVDKSGNVISVEQLYPGERGKDLVLTIDTELQQKVEEIIQQEILATK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 3.4.16.4
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.
Sequence Length: 373
Sequence Mass (Da): 43389
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A0A0D8CAX0 | MRNKDRPIPTPDRPNFYGRRGSRPLKDSRKALVDAMLPKIGITYPDEAGIDPNSYFDGTPDQLWLEIGFGGGEHLAGQAEANPGIGIIGAEPFMDGVGSLLRHLDERNLSNVRVVADDSRPLLYKLVDACFDRAFLLFPDPWPKKRHSERRFIGPKNLALLARLLKDGAEFRVASDDMQYISWTLQHMHNHPDFEWLAEGPDDWRTPPSDWVKTRYEQKALRQGKKCNYLRFRRKKRAA | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 239
S... |
A0A0L0D3I4 | MGWVAQTVAWGVCSRVVVAVVMAAAAACLPPFDASGSRAALGHAANWDGIYYTAIADRGYVYEHEMAFFPGWPLLLRAVVAASAGWLSPPLAGALIASVAGIAAALAVAWSAGLVYEASKGSKWLHGSGVTRETFMATAGRLHALSPASVFGSVAYTEAPFAAVAFAAVAAYLWLATPARRNDSTASRVLASVSLVVAGVGAGSLRSNGMLLSGLAVALCVRAATAPAGSTLGRLAVCAAWLGASAIMVVPYLAFQVWGASEVCGSGVVAHDVRPHCGASIVAPLKLYSYIQATYWGNGFLAYYEWKQVPNFALAAPILV... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 427
Sequence Mass (Da): 44778
Location Topology: Multi-pass me... |
A0A1E8FGD5 | MKIAMIAAMAHDRVIGKDNQMPWHMPADLAHFKRTTLGKPVIMGRKTYESIGRALPGRLNIVITTDQSYTLADAEVVNSIDAALEMAQNTTTDEVMIIGGGTIYANLLPRAHRLYLTLIDLHTSGDTYFPDYNAQGNWQVTDEQRFASDDKNPHAYRFLTLERQ | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A2U1MA26 | MGEGILVYDIIKYLKPSLDDKKATLYTVVLALYPLHWFFTFLYYTDVASLTVVLAMYLMCLKKNYLSSALFGAFAVLVRQTNIIWVLFVACTGVLDLIQAKQKHDENRLSDPKDGQVTSSSGVYISSNLKRRKSDNTNDTASHSVRGTSLLSNPDRSSGLFSEIWSILLTSWHLKWELLVSFSPFFALFVAFVAFIVWNGSIVLGAKEAHTVSPHFAQLLYYALVSCCFMAPMHFSTNQASNLARSFRKNRLLGCFLWFLAMIGSFLSVHYFSIAHPYLLADNRHYPFYLWRKIINAHWSTKYLLVPLYVYSWTSILTML... | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodoli... |
A0A8S2ALD8 | MEIKIRRRRGYKAETTVEKEVEEEEQPLSPAARLFHAPEFNCYIISVVGLKNKIQPDVIIEGIKQTLIRHPRFSSKLVNNWNNNRQEQKWVRTNVVVEDHVIIPKIETQNIKNANANADAFLESYVSDLTTIPLDTSKPLWEVHLLDLKTSDAENVVVLRVHHSLGDGMSMMSLVLACTRKTSNPNELPSLPYQNRPSSGSSSLKTSSRCYARFFWLVMVLWSATMLVLNTVCDALEFIATTLFLKDTETPIKGDFRLSKRKRMCLVHRTVSLDDIKLIKNAMKMDLADMMAKGSKCRWGNWIGYIVFPFSIALCDDPLE... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Subcellular Location: Cell membrane
Sequence Length: 919
Sequence Mass (Da): 104778
Location Topology: Single-pass membrane protein
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A0A1G0YC11 | MKKVCMGQVEIGMKPRIIGCVTSVRTAQRIQKRKDLPFDVAEFRADLMGMDKLGDGTLCCEVEKSGRPVLLTVRSKREGGAWAGTGRELIDFYRRLLPQVSAIDAEIRSKTFSDVVQAARGLGKTAVASFHDFERTPSLSRLKEMVKEGRKGGAHIVKVAAMIRKPSDAITLYELLREASAGPLCVIGMGPAGLATRIGLPCAGSCLAYGFIDAIAAPGQLSCRDLKAFFRRFYV | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DH... |
A0A6G1E2I8 | MCARVCFWWFVGGSAVLAHFTLNEKLQRVGVLGCVLCIVGSTVIILHAPQERTPSSVDEIWHLAIQPDFLCYAAIAVAVSLFLMIYCAPRYGQMNIMVYVGICSVIGSLTVMSIKAVGIAIKLTIEGINQAGYFQTWLFAVISVTCIVIQLIYLNKALDTFNTAVVSPIYYAMFTTLTILASAIMFKDWSGQSASKIASEICGFLTVLAGTVVLHSTREPDQTISADLYAPLPPKIYWHIQGNGDIGKQKEDDSLPCDIITVVRQDYFV | Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 29535
Location Topology: Multi-pass membrane protein
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D5J254 | GSLIGDXQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINXITTIINMRLNGMSFDQMPLFVWAVGITAFLLLLSLPVLAGAI | 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... |
A0A7S4KGX9 | MAMYGDRADEGLLEKIARVGRAIPGFLCNLPVRVVLRRALGALYALGRSVKSILTMEALSDVLLEHKLPHTVWLLGVRYTLAPPPMGQRGEGRETEQTVVDESQNFKLDMWSRLWFSYRYNFHPISGTELTTDTGWGCMIRSGQMLIGQALVH | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoeth... |
A0A2U1PTQ7 | MQDFVAQAGDPTGTGQGGDSIHRLLDAAASRYFEREVRPKLSNSKKGTLSMAGSEYGHASQVFGKVVDGFDTLDSINDSFVDCYNRPFTNIRWNDGWNWIWSRRGITSTQLSTLNTLLDPIILTEGRDESVWLLDPNNGFTVNKTRIHLDNASLPDAYISTRWCRFIPKKVNIFVWRALRDRLPTRWNLSNKGVEIESILCPSCSSSPETIHHSLWTCSLATCVWLKVFSWLDLPYPTPSSLEDVFAYVDQLHVHNDRKLMLHAIFGVVLWTLWSFRNHLIFNSHPMARNEIFDKVEIIRLEYERTKLSEEELSEQIRAT... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Nucleus
Sequence Length: 519
Sequence Mass (D... |
A0A2R5EU21 | MTFAGYAVILSNLGSSSDRFVPTGYGDRYTIEQLFERAAQIPQVGAVELVGTWHVTEGNVRQLKDCLDRTGLKLASIIPDHFGQPKWKKGSFASKEASIRAEAISHTKEMADVAVELGCDLLSLWPGQDGYDYLFQSDYVQERQWFVEGIREASQHRSDVRYSLEYKIKEPRTHGLLSTAANALLIAQQAGGDNVGVTIDFGHSLNAYETPAEAAALLQQYGGKLFHVHMNDNYRHWDDDMIVGSVHTIETLEFFYWLRRLGYQGWLSIDQYPYREDGLAAVREGVLAMEAFNRLLDSIPSGELEGIIARGEATESTVYL... | Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose
EC: 5.3.1.5
Subcellular Location: Cytoplasm
Sequence Length: 329
Sequence Mass (Da): 36929
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A0A2M7H2L3 | MTTGSVSSFVFPRASDAIIKPVGSLLTFQKEVPMGNKTARVFYGVHWGDEAKGATCERYALRDDVNVIVRDGGANNCGHQTMRGGRLIKAHCIPVAGTLPGRTAVVAGMTLIMPTNIASVLQPGRFRPGLPQEYAALRELGCHDFKLVLDGRIGLILPPDLELEAMVEGGPHARGTTGSGVAMARARQALTCSVRLIDCFDQRVLTEALMRADWYREHLFATTNQTGGERRYADSRDDLLRLAEWVDRTADVTMLDADRFLRTAWQAGNSLAWEMPQSHGLCMLRGSVPFVTSSLPLQPTGTWFPSGTTSVPVFKMGYVT... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
F4GHW6 | MTSRPDDAFPVMLCGIDHDSADNEMRDMFFLDDPKSRRMAVTVRSRLAAQGVVVLSTCNRTEVWVHGGNGDPFPHMCRAAGISPSRYQDLFYHKRGDEVVPYLFELASGMRSALYGETTIIPQIIHSIDIARATGAADGVLEQLFRQAVTAAKEVHSSLRLAAADETVASAVQRMVEKYLAPVSLSGEPVLVIGSGEMARLTARSLLGRGCRVTMTIRDMEKASALVPEGCTAVPYESRLEHVSGKRIIISATSGLHHTLRKTDLASYLGGPVLLIDLAMPVDIDPRVREDERVKLVSLRELDVDQPRRRELERQAHAIL... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A7S4HAA7 | GIDTLRKRVKFEDEIDSRLSHNARGILSMANAGPNTNGSQFFITFKACPHLDKKHSIFGSVVGGIDTLRKLERIETDAKDCPTEDIIVKEVVVFVNPFETDLKAYFEEKKSNEIKEVEDKKKKKKIEAEDNEGFTQWYSNPSAAAASKVTLYKEGVGKYIAPKKEEEGKKEAAEQQDNGDDMWVNVPLSKQKNKAAPRAGFGDFSSW | 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: 207
Sequence Mass (Da): 23235
|
A0A2U1KB11 | MEQYSQEIMHVNNIVKDQKPSSSKWESLLELVDESEISSLGGFDCNICLDTVQDPVVTLCGHLYCWPCVYKWIYHQNTSSEIENQNKHNPQCPVCKHHISQKTLVPLYGRGQTTKPKSDKKSLGSGMVIPRRPHGPIMNQHSCQFRSLINQWPPIVQHQDLPNDKMAQM | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase.
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
Subcellul... |
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