ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A7Y1ZRW9 | MDTTIKQVSSVEYELEISATADELAPDLNSALKTQRARTKMKGFRTGKVPLSIVKKMYGEALAYGIAEKSIQEKFETEVVEAETHDVVGKPKLTRFEYKLDGDLSATIRFGVKPTFELEDISTLTVNKMVHGTNEEDVDAEIERLQKAEADLTPFDAPAGDNDYVVMSMQALDDESGTPIIGEKQDDMTVHIGDDRLKSELRTALIGMSAGETRRVDIAHDEPHDHGDEHHGDSHTHSYEIEVKEVKKQELPDLDDEFVKSVSKGEVETVDAFKEEIRKQLASGWEQRSRELLESSLMLKILDLHDIEIPDSIIDIYLDS... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A3P1WUA3 | MIGYAKLPWYVSGPLFVTAGVLLGLGQAPIGWWPATIVGIGLFSWLLQGRTKRTAVAYGYVAGLALNGLTLWWISVLGAPVALALIGYAAIWYGLAGLIISRLIKLPGWQAWVACAWVAIEHVSGRWPFGGFSWIRLAHATLDQPLGGYLPFLGAAGASLLMALVGQLLFTRRFQICLPLMAALFLVGALLPAQKLPTTGRTVEVANVQPNVNRHEYGGPYYARAVTNNALSATVFALAEARSRNKIVDMVLWPESASDYDPLLDRKAGHQVELATKLAGTPLLVGAVTRPDTPENSRQTTGIFWEPEVGPAAVYHKRNL... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A8J7R8L4 | MPLKSAALRKATKAVMFALSQEPQARTADDLHRYLSQATCLTTNEIDAALKQLLYVRSLVGDDAGGWTVAQARACKTGVVMGARGGAYQFRPDDETEVFVLHGVDHLAVFPGDRVSAMPKQFMDGKFRVATLEALIERRDKTHVCRFGHYCRDGIVCVVPVDPFAQTPIYVEAQADELKNQIVVVELDDEPMYTPWGAMCAQGRVVERLGDQDDSEVELEVALRRFELPHVFSEETIREAEALPDDVPAREARHRVDLRDIAFVTIDGEDARDFDDAVWCTTHGNGWRLLVAIADVSHYVKPGSALDRDAQERATSVYFP... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 783
Sequence Mass (Da): 885... |
A0A1H3JNX5 | MAYFPLFVEISKKKCLVVGGGQRAFEKVAALFDFGAQITVIAPKIVEDIKEVSGVTCIERKFQESDVEGQFIVVAASEDSGENTMISEICKQLGIHVNVLDNKEESTFLFSEYIKQRDVVAAFSSSGKCPVVDKYMKLQNTEVVDSFLGEVNEFFASIKRQVDKCVPDPQRRVMVYEDLLEATLILKRKPTMDQVGSVIEHINEKEL | 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: 207
Sequence Mass (Da): 23225
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A0A847QNB4 | MPTEIPSKYRNSLESFQNTARRLFDIDISEAQLKQFAIFTDLLLEWNERINLTAITELDEIMVKHFLDSLIFCKWLDRSSFKENIVLADLGTGAGFPGIPLKIIFPQMKIVLIDSLNKRINFLNIVKKELCLENLETHHARAEDIGRDINFRQTFDIVVARAVAELAVLLEYCSPLLKVGGHLLAAKGQNPEAEVTSSQRALAELNCKLEMIEKYSLAENADKRSLIIISKTGNTPQKYPRQAGKPKKKPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 251
Sequence Mass (Da): 28451
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A0A1H3FCE6 | MKVYFKRTLLVLVLLFAGILIICLYYNKIESNRIPKKINDSLKTEKVNNDDKQSIEVYAMDTYMTLYAYGSNAKAALMESKKKILQLDSLFNTTNSESEIYQLNCDKKIIASKDVIEILKEAKKISDLTDGKLDLSVYPIVEEWGFINKKFCIPTDNRLEELKKNVSYKKIFINEKTSEVRLDNKSMKIDLGAVAKGYTSKMIMKIFKKHHIKSGLVSLGGNVQIYGKKPDNSLFKIGIANPEKKATNYLGVYQGKDKAVITSGSYERYFEKNNKIYHHIIDPATAKPAESGIVSMTIIADDGTLADGLSTSCFILGKDK... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 363
Sequence Mass (Da): 41353
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A0A0D9Y104 | MTSSPPPIRLLLLPATRFCCLGSAWGGGFGGGARSVRVERRGRQRAVVMAAAGGGDFEARVARIASTIRVIPDFPKPGIMFQDITTMLLNPEAFRDTIELFVERYKDKGITVIVGVEARGFIFGPPIALALGAKFVPLRKPKKLPGEVISEEYSLEYGTDKIEMHVGAVEPNDRAVVVDDLIATGGTLCAAVNLLERAGAEVVECACVIELPELKGRDKLGSKPVFVLVKAD | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4.2.7
Subcellular Location: Cytoplasm
Sequence Length: 232
Sequence Mass (Da): 24877
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A0A388S908 | MRVEHQISLSPFTTFGVEARAKRLVRLESREDLEALRTVREKDEPLLIIGAGSNILFTKDFDGLVALNRITGVEELPRGDAGEYRFRAGSGENWSPLVSRMTESGHPGLENLVLIPGSVGGAAVQNIGAYGIEAAERIDAVEIFDLESGEFRTLSTEECDFGYRSSVFKSEEGKNWVIVSVTFRLPNEKDWTPVTGYKGLSAALEGKEVTPRSVLVAVEALRRSKLPDPKEFGNAGSFFKNPVVPELQARALLEDYPQLVAYPLGGRRTKLAAGWLIDAAGFRGRVLGNAAVWDRQALVLVNRGGATGKEVKALCDEVIH... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 337
Sequence Mass (Da): 36794
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A0A1J1E156 | MEFLTLPSFDPAFNLALEEHLFISLLPRHPGLFLLWQNAPSIIVGRHQCTAEEVNAGFVKRENLQVVRRITGGGAVYHDRGNLNFSFMENARGRTRTDFRRYLLPVQEALADVGVTAEISGRNDLEAEGRKISGSAQLLRQGKALHHGTLLVDVDFERMTEALTADSEKIRSKGISSVRARVGNISEYWAQETTMEKLKICLLRRCARSEARLNPGDRAVAEALAETKYRQWDWNYGASPLYTRKKRERFPWGSVEQRLAVRNGVIESCKIHGDFFATASIEDLEKIFVGRRHDPGALEHALNHLDWETWFSGCDHESMR... | 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: 331
Sequence ... |
A0A1I5VUS2 | MKRSWRTILAPMLLAFALFGLPVDDARSQSQDDAASEVVPGSPTLEAPPAPPAPPVATPPSSPAIVAPGAAPLAATPAAAAPPAAAPSVSTSEPKAAPTAAANPVRSRATPAAAATPTPTPSTTPATETAQALRVVLGLTVLAILPALLVCLTSFLRIIVVLSMLRHAIGMNETPPNTVLIGLALFLTLFTMSPVLQKVNHDAFEPFMAGKLSMEEGYGKGITPLREFMVRQTREADLALMVELSKAPSPKSMDDISNVQLIPSFMLSELRAAFQIGFVIFLPFLLIDLIVSSILMALGMMMMPPTTIALPLKVLMFILV... | Function: Plays a role in the flagellum-specific transport system.
Subcellular Location: Cell membrane
Sequence Length: 335
Sequence Mass (Da): 35124
Location Topology: Multi-pass membrane protein
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A0A2V2PY93 | MATAADITAMGRAIALAARGLGSTSPNPVVGCVITDASGAVAGEGFHQRAGGPHAEVHALRAAGGRARGGTAYVTLEPCNHTGRTGPCAQALQAAGISRVVYAVGDPNPQATGGADTLRAAGIRVEQGLLAEEAEAGNAAWLTSVRLGRPHVLWKYAATLDGRIAAADATSRWITSPEARADVHRLRAEAD | 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.
EC: 1.1.1.193
Sequence Length: 191
Sequence Mass (Da): 1937... |
A0A2T2QWL3 | MAQADDIISVPDERLRQHARRVGVITDDVLDTIETMKAAALAWEQTRDNEVGVALAAPQIGVLERIIIVRHQPDNRDDHRFDAFINPEITKYEGEIGAEPEGCLSVPDTYGLVPRYGAIRVSAMDTGGETFRLKTTGFLARVLQHEIDHLRGLLFVDAVTDDAFYRLTDHGKLKALTKQEIDADRVFWNG | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A0G1IFZ6 | MPTDNNRSVIDLPKGVSGLSRHEAQQRLKLYGSNEIIQSKKLSVAANFFLKFKNPLIIILIIAALISGFLGNRIDSFIIIAMVILSVAIDFINTYKSQRAAEALRDRVKITATVLREGVLAEIPLSLIVPGDVAVLSPGDVIPADGTILQAKDFFVNESSLTGESFPVEKETSSSVFMGSSVVTGNGLMSVLATGRKTKFSSIAESLTRKEEPNDFDRGIKDFSVLIMKVILILVIFVFFVNAFKTSTSQHQLLESFLFAIALAVGLTPELLPMIIALNLSRGSLVMSKRGVIVKKLSAIQSFGSMDILCTDKTGTLTED... | Function: Mediates magnesium influx to the cytosol.
Catalytic Activity: ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate
EC: 7.2.2.14
Subcellular Location: Cell inner membrane
Sequence Length: 819
Sequence Mass (Da): 90367
Location Topology: Multi-pass membrane protein
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M0NW45 | MDEASVRDGSAGSHTVDGEPGTIGAVEDVLADLGTPDADVAVETDLPIGAGFGVSGAAALGAALAANDAFDRGRSENELIRIAHEAEVGRGTGLGDVVAQARGGVPIRLEPGAPGMGALDGIPADARVEYATFGELSTEEVLGGDTAALSAAGEQALDRLRADPRLPTMMDAARGFAREADLLVPEVSEAIAAVEESEGDSPDGSDDYGAAMAMLGRTVFALGTGLSDAGYDPEVCRVDAAGARLVGR | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
EC: 2.7.1.169
Catalytic Activity: (R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+)
Sequence Length: 248
Sequence Mass (Da): 24862
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A0A7X9BEE6 | ATANIIAKTAHGLADDLLSTVLNAATCPVLFCPAMNKDMYENRITQRNLSILRELGYHFVEPGRGMLACGVEGIGRLAEVEVIQVSIEALLAGEQDLKGLRVLVTAGPTVEPLDPVRYLTNRSSGKMGYAIAAAALRRGASVVLVSGPTSLKPPVGVEFIRIETAQEMFDAVLEQYAKVDVVIKAAAVADYRPQKVAEHKIKKNLEQMTIDLEKNPDILAELGRQKTHQILVGFAAETNELEKNALAKVAKKNLDLLIANDVTKPGAEFGSDTNIVKMVYPGQKVVPLPKMDKRILAHRILDEVLSLRANRK | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the se... |
A0A1H3HDT8 | MIIRKMKEQDTTAVAKIEEINFAQPWSANAFCESLANKDTLFLVAQEEKEILGYIGMYISLDEGEITNVSVSPQHQRKHVATKLIENIIELAQKKQVSRIILEVRKTNTPAIKAYEKQGFKIVGVRKNFYEKPIEDAYIMDVNI | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 144
Sequence Mass (Da): 16502
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A0A0T6YD25 | MPAKQGRMTAESTVEQGTAGLDSLAGHEMALIDDLNRRYRARHGFPFIVCVRHYTKAGIFAEFKHRIGRETDAELAEALRQIANISRYRLGALIKEAQEVITPAA | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
EC: 4.1.1.97
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2
Sequence Length: 105
Sequence Mass (Da): 11695
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A0A1V1PT13 | MLPSLGFNEILILGVLALVVIGPKDLPLMLRKLGRWTAKLRGMAQEFRTGFDELARQAELDELKKEVDALRRTTNLQSIASDLSKPLPTLEDYAGIAKPKPLTTPDGASASSSMEEAPRSGGGGARAGGGNEPLEATPSTMAATPPQSSLRDDSSPIEGELSDEPIARSAP | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
D8IS48 | MTTILTACPAPAKLNLFLHVTGRRPDGYHLLQSAFQLIDRCDTLDFAVRDDGRIIRTNEVLGVPAESDLVIRAAHLLRDAAGRPELGADITVHKVLPMGGGVGGGSSDAATTLLVLNHLWKCGYNRASLMEMGLKLGADVPFFLFGRNAFAEGVGEELSVLRTADCWYVVIEPGVSVPTSIIFSSKLLTRDTQPVRITDFPDATKQVASSFGKNDLEMVATAHFPEVAAAVEWLGKFGNARMTGSGACVFCAFEHEHQADEVLKTLPSRWIGWKAKAMQEHPLAHLVQS | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A3P3YJH0 | MPRTAPSAARLRSRRARADPGRPLHRFEYCDSDAPHHSCSPNPATCCRCNHVGAALAILAACVRPRAARCADAARAYKPALADWVQQTPGTAVCRRVCTTTGGFGSVRWLPARTWCAKLGTKGRPRRCASCRQSAAGCNPQFRSASKCACGRRAMIMFQRGAARRLAGRRCSTAPAAAQKPTKAPGPDPATLTDKFGRRHSYLRISLTERCNLRCHYCMPEQGVTLTPSEKLLTAKEIQRVASVFVKAGVNKIRLTGGEPLIRKDLPQIVESLGDLRADGLESISMTTNGIRLQASLVDLIYAGLNTVNVSLDTMDSLRF... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 524
Sequence Mass (Da): 57356
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A0A388SFB6 | MKEEESRFYALVPASGVGRRMGLAVPKQYLRLAGETVLSLTVRALHDSGIFSGILVVVSETDAWIDEETFPEGVSVVRRGGETRADTVVNGLETLSGGAVFPASGSDWVMVHDAARPFVDPADIRKLRDEVLSAGHGAILAMPMADTVKEASPDRRILATRDRKSLWRAATPQAFRLSELLSALRRGTEGVTDESSAMERTGHPVSVVPGSTLNFKITTPDDALIAEAIAESRLRKHP | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A8J7QV09 | MSFISSRIWALKQTFRGIFHAKTQFMLAVTLAGLTLTIPVFLGILIWTFSEPLISVPMHTEITVFADRSAGKESVQRLNERILAIEEIAQTQVVPKQEALAMMHDNLGLRPQQSKAQNPLPDIVIATVHPHLSDQEIAAVAKQIERLTNVDMVAYDDKWAGHVSALFSTASIILAILGSIIMALVGIVIAASVRLTTYAQRDEIAALYIFGASNAFICRPYTWRGCMTLALSAAISLGLSYAGLHLLHDPLISFTQLYGVTVHLSMLSLDWCLVYVGMAAILGGLIGAGTASSALGKIRRRTY | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell inner membrane
Sequence Length: 303
Sequence Mass (Da): 33007
Location Topology: Multi-pass membrane protein
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Q5WBZ1 | MSLRPKIILLFLSIVLVPLNLLGMITYAYFSKTLEDQTYHYTVQVIGQVNQNVNAYIDEMHRLSLLPLYDRDILAILKNRSDVHHSYYPQTEEFERMSSFLSTLSYNRQELSGIHIITRDGSLFSDLGSPRTVHRLAEGTSDWQEAIEAGNGASLLLPTHSPSYVLGAEKSVFSVGRLLRDPDGFRPLGMIKVDIELSFIESLLEDVDLSEDASITMIDRNGEPIYETGKAIYPLLKGKGEDVWQLAERESIAVDGVDYLPVIRNDSSGDVQTIVFLPEHHIVGASQSLRLFTIGLMLAVSAVVIMLALVAERSLTKPIF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 577
Sequence Mass (Da): 65208
Location Topology: Multi-pass membrane protein
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A0A258L6F3 | MASEEDLIRTYLAPLARAHAGASDLADDCAIFTPAPGTELIVTTDAVAAGVHFFPDDAPEDIAWKALAVNVSDLAAKAAVPRVYQMALSFPDAPTHEFMQRFTSGLAEAQSAFAIVLSGGDTDRRPGPMTITITAIGEIPTGLHLTRDRARPGDAIFVTGILGDAACGLKLRREDADVRDWRLSASERSGLVARYLRPEPRLAAAGILRQHATAAMDLSDGLAKDIGRLAAAARAGAVVDAARIPLSPAVARLAASHPDVMDLALSGGDDYELLFTAPTIAETAIAEAASSIGLKVTRIGTMSDQRGLRLSTPDGERPMQ... | 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... |
A0A1I5H6B4 | MNKPTNSRTNTSQIHKKKNNKKSKRTNQKSKKNKRQAANTGKDSIGKKIGLFFLILLLILSLCVLIAGLFIYFKYGNTIIRFQKEAQEAVSMSDRDTFRQAETSLVYDIKGKPISVLKGEKDVYYLEYKEIPETAVKAMISIEDKKYMSHEGVDLLAIIRAMTALIKNEGDITQGASTITQQLARNIFLSNEVTYERKLKEIFIAIELEKKYSKEDILEFYLNNIYFANGYYGIEAASKGYFNKSAKDLSLSEVAFLCAIPNNPTIYNPLHHMDNTKARRNRILDHMYQDGRIGLEEYNKASNQEITLSLSKVKKNNYVD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A165JNL6 | MAVAGLSRRPPSHPMKNCWTFPLINVRRLLSGSLMVFLIPATAYMLWKAISLITDSSHPIVVVISESMEPAFKRGDILILWNRQSLVKVGDIPVCWLPGRSLPMVHRAISVINTSISYAPVKVIQQILTKGDNNEVDDIALYPPGQNWIYRHQIVGLVWGYIPLLGWVTIALNEYPWLKAIVMLTLVLGILLD | Function: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-hel... |
A0A133XHB9 | MAQYVMSMLRVSKIVPPKRQIIKDISLSFFPGAKIGLLGLNGSGKSTVLKIMAGVDKEYDGEVQHLAGVSIGYLPQEPQLDPAKTVKEEVESALGEVMQAQAKLDEVYAAYADPEADFDKLAEEQARLEAIISTAGSDTEAQMELAADALRLPPWEAVIGNLSGGEKRRVALCKLLLAKPDMLLLDEPTNHLDAESVEWLEQFLVRFPGTVVAVTHDRYFLDNAAEWILELDRGHGIPYKGNYSSWLEQKEARLETENKQIDAHMKAMKQELEWVRSNPKARQAKSKSRLARFEEMSSQEYQKRNETQEIFIPVGERLGG... | Function: A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome... |
Q5E148 | MKKHYLSMKLKLTLMFFSTSVFVFIGLGFAIQYLVQSHFYEEDLRLINANRTSIFVLLENEGITSSEIFASLKSRGINIWIANDNGTLTQNTNVIPNDSAFKQSKKINEWTYAGSTFRTLYYPLENENNYTGLLIGINIDHHIEFNKRLKGILIWSISIASLLSFICSFIIVNMGFKPLQYLQDRIKQVQPNKLSIRLSDEHLPNELVELAKIQNQMLDRLELGFERLSDFSSDIAHELKTPLSNIMTQTHVTLSQPRTPHEYQEILSSNLEELERINKTINDTLYLAKSENDLLLKDNMQLDLEQLFAPIIEYYSIVSE... | Function: Member of a two-component regulatory system.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 446
Sequence Mass (Da): 50790
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A0A3P1WH87 | MGWVMLAGGLGAVARSIVDARLGGRVVPLGILTVNLLGSVLLGVVLALGEAGVWGDFVVRLAGVGFCGGFTTFSTAAVDAVQLAARRRWWVGLGYWAGGLAACVLAGVAGGWLAEFVIAVFDRCSY | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 12885
Location Topology: Multi-pass membrane protein
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A0A3P3Y7D4 | MTKRCRQEGHASAYHTFTHDEVPVVRANLLSWFDTHRRCLPWRGDKPPYDNPSPGRSLPSDAYAVWVSEVMLQQTRVDTVIPYYERWMKRFPSIADLASASMEDVNEMWAGLGYYRRARFLLEGAQWAMKECGGLLPTSVPGLKKVPGIGEYTAGAIASIAFGQRVPLVDGNVVRVLSRVRAIAAAPNASNALKLHWALAGDIVDYERPGDFNQALMELGATVCTQHNPSCSACPIESICLARQEGFCCAEGDIPDPVGVVTRYPLKKLKQRVTEQSTRVCCVESDGRVLLVKRACKGLLAGQWAFPCWERFGDQLDRAL... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 410
Sequence Mass (Da): 45697
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A0A3D3W9Z7 | MESIILASASPRRRELLDRLGVFFEVIPSPIDEKSLQLSGSPGEQVQASALAKGKAVAQLYPGRWVLSADTVVCIGREILGKPEDAEDAFRMLRLLQGQCHQVLTGVCLLRQPTEADGSEAGQIVFAAKTAIQKFKVCEETKVWMAPLSDAAIAAYVATGEPMDKAGAYAIQGFGSSLIQRIHGCYFNVVGLPLYQTSLLLQRAGLPLWQGDCR | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A158SNX4 | MKDPKLTMERSPLGSRFFSSSNTLVVAVSTGVDSMVLLDLLQNLPKLRRPRLIVAHVNHHLRTQSTAEEAFLRTYCRQRNLPLEVAQWEVAEHPAKGIEAAARRFRYAFFATVMDKYQAQAVATAHHQDDLAETVLMKLIRGGRIEQLGALRWQRPFASGELIRPLLALNKQDLRRYAKDHHLTWFEDETNRDLTPFRNRVRHHYLPSLSVENPRLVTALASDAEQINDLLSLANERLGELDATLRTERGFSLAAFRRLSESTQRSYLRYYLTKRGVATIKEEQLHQLVTGLGDQTRPPQSFQLPNQWCLVKGYREAFLK... | 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)... |
A0A069DL24 | MIWLVIVILILFYFLQTVLLFVLEYERPAKAGVWILISICLPVIGIALYFLAGRPYKRMRKHVKTEVWEHIHQHLASQTTVITKAEDMQSEVFTSHTRLFNLLSPIPNSAITGCNQTKYFTEGEPLFASLLHDIEKAQHHIHIQFYIFRDDIIGTMFQDLLIEKAKLGVKVSIICDGFGSKTLPKPFIQRMKNAGIEIHFFLPPGLAMKLRKLNYRNHRKIVVVDGTIGYTGGMNIGDEYRGQSQKMGFWRDTHMRISGDAVYFLQTTFLKDWEMVSGQTVDEELIPSLFPPHDCQVNEQVQIVESGPDETRHLIQEVCF... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membra... |
A0A1X1CYD0 | MTPAFSSWSDFFAMGGYAFYVWLAVILTLIPLIGLVLHTVLFRRRLLAEIRQRQSRERRIRDAKSKKAASEAAGESV | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 77
Sequence Mass (Da): 8771
Location Topology: Single-pass membrane protein
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A0A7Y2CSC0 | MKEFISVDEAESIIAAHVRTMSAEFVSLDSSYGRTLSSSILSERDIPPFDNSAMDGFAVRASEVDTVPVELSVSQEIRAGGFPRDSLLGGTCARILTGAPIPSGADAVVPVEWTEGDDPVRFLRSPSVGHAIRIAGEDVAAGHMIFSGGEIVTPPVVGMLAAVGCSDVPVSVRPACSIIATGDELVRHDRQPERGQIRNSNGPALVAQVVSAGGRVARELTARDNPSSLNECLTASLEDDLVILSGGVSVGAYDHVKDVLDNLGVRLLFWKVKQRPGKPLVFGVRGETLVFGLPGNPVSSSICFDRYVRTTIARMLGRST... | 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: 401
Sequence Mass (Da):... |
D8IRC8 | MLRLGSTGLLPLQCSNPDNPDMTTRPDPDDLLERVMRDEERQARGRLKIFFGFSAGVGKTFAMLEAAQALAAQGGDVVAGVVETHGRAETEAQLAGLARLPMRMVAYRDRQLPEFDLDAALERKPGVILVDELAHSNVPGSRHAKRWQDIDELLRAGIDVYTTLNVQHIESLNDVVGQITGIRVFETVPDHVFDEADDVMLVDIPPDELLARLQQGKVYLPQQAEKAGRNFFRKGNLIALREIALRRTADRVDADMRQYRADRSIAQLWQARECIVVAIGSGSGEERLIREAARLAAKLQAQWLAVHVDLPGQRQAMEAR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 939
Sequence Mass (Da): 102489
Location Topology: Multi-pass membrane protein
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Q5E701 | MTFTTQDHLMMQKAILLAKQGIYTTAPNPNVGCVLVKNGKIIGEGAHLKAGEPHAEVHALRQAGKEAQGATAYVTLEPCSHYGRTPPCAEGLIKAGVKKVICAMVDPNPQVAGRGLAMLDEAGIETASGLLEADARALNPHFLTRMETGKPFVQLKMAASLDGKTALKNGVSQWITSKEARQDVQRYRAQSGAILSTAKTVIDDDASLNVRWSDLPPSIQESYQQASIRQPMRFILDRQHSLTSDLKLFQASDEVVTISSQNTHPIGTSENHMQCRVDDGQLDLKEVVNKISRDFNVNHIWVEAGATLAASMINDNLVDE... | 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... |
A0A0G4IY72 | MDVAIEGPAPGGARSEVAICGPGDSKCGYCHSGSRTGRSSFGIVAERLTPVDYQVRDSWTLQVLIDRGWRRSGTYVYKPDNRRSCCPNWTIRLPVEEFRPTKKHRKIRNRFREYIQHGPRTRQPSDDASMQVVNEPVDSDAIQFESYLRCAVQDAAARLFDARDVAFTFKKSATLQCNVAFAIASQLRRSTGSSTTPADVAEKVAMDLTSMQLRDVVSVAADANGFVLFTLPAERAAAVAASRRQRHAADRQKRAAQQAPAASPPYVRYTTTVVGSRFREEAFLVYQRYQVAVHGDPIARVTREQYKNFLCDTPLVETAS... | Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway.
EC: 2.3.2.8
Catalytic Activity: an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-t... |
A0A101FZT0 | MVLTLIQNVALVVMLGTAQRYLSRVLDAHPRLSALASGILYGSVAIVGMLTPFRFAEGIIYDGRSIVMSLAGLFGGAPVALIAGTLAGAYRVFLGGAGVVPGVVTVVTSAAVGVALRRFSGGRLTSLRVIDLVSFGLAVHLLMLGVQYLLLPAEVALLVVREVGPLLLTLFPLANAIAARMMIDQMDRERARVELAEESRRLRLAMAAADEGAWQTDLESGVFTLSTEAAQLLGRGDGPVCLAPEEWLRGMHPDDRPVHAASLGALIQSQEGEAPRVFRWEYASGHYRWYQVLGAVSDRDATGTPLKISGVITDITEMRL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 1012
Sequence Mass (Da): 110487
Location Topology: Multi-pass membrane protein
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A0A1E3T8W3 | MYETVRPEDAPAALMRAYAAAVLPPAGPVFLSIPMDDCDRPCPRLPQIRTVSATLPADTDTLRPVIDALAGADSPALIIGGAVDRSGGWDHAVTLAEKLRCAVVGRPGGGRPGFPETHRLYRGTLPPAIGPLGEALAGHDVVVVIGAPVFRYYPYIPGEYLPVGTRLFQITDDPSEAARAPVGQAVLADPGRSCAVLASALPAAQRNSPTPRASQPPVRPAQITAEWLYRVVHTVRPPDSVIVQESLSTAQKLREQIPTARSRSFFSMSSGVLGFGLPAAVGVALAERDEGSNRTVICIVGDGAANYVIQALWTAVQQQL... | 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: 405
Sequence Mass (Da): 42737
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A0A940HZI4 | MKKVTLVCNHNITDGKLQQALNEIISLLRNHGLAVSLFDCAPANFDFDVCCQEELQGIDLVIALGGDGTILSSARLVAAKGIPILGIKFGRLGFLSELEFHEFPSTIPKLIDGNYMIDERGMLAAEVLRAGKKVFQAYCLNDAVLSRGTLLRPVGLKVDVDGNTWARFLGDGVVVSTPTGSTAYALSAGGPLVTPNVKAILLTPLCPHTMSLRPLLVDIDCRIHITFTGLRQGGILVLDGQKTYPLREGDEVVITSAPFHTKLVRFKHGNFFQLVQNKLSRNVYDG | 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... |
A0A1F2P4G1 | MVECLAVNQIVGGSSPPGGVEVYLMSIREVFEGCRGRGALIGYLTCGDPDLETSLRIIKEAAEEVDILELGIPFSDPIADGATIQAASDRALRSGIRVDDCFRIAAEVEGPPKVFMTYYNIVLQRGLDRFFSDSVDAGVSGLIVPDIPIEESQDLLRSSKEYGVDLIFLVAPTTDENRMNRIIEHTRGFLYVVSRLGVTGARDHLDPGTIEFIRRVKAIAGGRVPVAVGFGISTPQHVEEVIRAGADGAIVGSAIIDRISEGVEDEKGIRRLREFLRSLREAARRR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-s... |
A0A3M0BZD8 | MAANRRTKKTSAPAKAPKTGPAVPSRRRDKGVLARLMYGLAVVGVWGAFAGVVGLAYLAHDLPDLGNLAPPGTGERAILIKAADGSTLVRSGPIYGDWIDFEAMPDTLIRAFLAVEDRSFFEHGGVDGKGLARAAFTNIREGRVLSGGSTITQQLAKNLFLTSDRTIRRKAQELLLAFWLEQKFRKDQILTLYLNRVYFGGGAYGIDAAARKYFGHSARRLTIGEAALLAGLVKAPSRLAPHINPEGAWERARVVLSAMVDGGVLSLKAAAAISDKPPAIIPDRAGVHVRYFTDWIETESMRLLGKRAMGQSMIIYTTLD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
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)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A0A927MHM7 | MLSTNRVNDTRKSILNQSANILTILNLSSGFLALIFVTKGHVQLAIVLIFLAAIFDMYDGKVARSLNVTSDFGKQLDSLADLISFGVAPAILIYTNVLYEYSVVGLFFTVLYVLCGAIRLARFNVTTFTGSFQGLPIPAAGCTLAFAIFFMNYIPSVLFMFLMLGLALLMIGTFKVKKV | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 179
Sequence Mass (Da): 19587
Location Topology: Multi-pass membrane protein
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A0A7Y2GYP7 | MSRIPEHSIEDVRAAADIVDVVGDYVRLKKRGTNFIGLCPFHSEKTPSFNVNPQMGIFKCFGCGEGGDVFAFVSRIEGLSFPESVRLLAEQTGVTLPEDDGPDEDASEVDAIYHALRFAARTFHAQLTDGKEGGMAREYLRDRGFTKETVRSFGVGYALNSWDGMIEHAAEAHISVDILEKAGLVLPRKSGDGPYDRFRHRLIFPILSHVGKVLGFGGRILDPEDEPKYINSPETRVYNKSRVLYGLYHGKNAIRAKEEAVLVEGYTDVMALHQAGVEHVVASSGTALTEQQIGMIGRYAQRIILLYDADQAGLRAALRG... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 644
Domain: Contains an N-termi... |
A0A934I604 | IYSTTNVISDKAAVDAHYYAGVVYDYFKNKFNRSGIDGNNMAMKSSVHYLKNWVNAQWTGTQMMYGDGDGVKATALSGSLDVVGHEMTHGVDQYEANLTYRDQSGALNESLSDSFGTFIEFYAQPSKADWLLGEDVWTPNTPGDALRSMANPTLYGQPDNMKNYVYTSDDNGGVHTNSGIPNKACYLTATNPSVGVQKAEQIYYRALCNYLTSSSTFHDARLALAQSAEDLYGANSSEYNAVISAWDSVGVN | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 252
Sequence Mass (Da): 27562
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A5ZAG3 | MIQKLLIANRGEIAVRIIRACREMGIETVAVYSKADKDALHTQLADEAICIGETKASESYLNMESIISATIATGADAIHPGFGFLSENSKFARLCEQCNIIFIGPKSDVMYNLGNKSVARKTMIEANVPVIPGSEEQIYDSKTGKKIADQVGYPVIIKAALGGGGKGMRVAYDPEEFEQAFNAAKKESEAAFDDGTMYIEHFVENPRHIEFQILADKFGNVIHLGERDCSIQRNHQKMIEESPSVILSDELRKKMGDTAVRAAKAAKYENAGTIEFLLDKDKFYFMEMNTRIQVEHPVTETVTGIDLIKEQIKIADGQPL... | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form ... |
A0A1F6EC89 | MKRPRAVIFDLDNTLARSFEAPALEMSQGLENILRRIPVAVMSAASFERIEKHLLPGFSVSADKNRLYLFPVNGAGCYTWENGAWRPQYHFEFTSEERARILAALKGSVEETGVGAESPKYGKQVVDYDGYIAFTALGLDAPREEKIAWDPDGSKRRTLRESLQKKIPDFDVYIGGTTSIDIMCKGVNKSYGVMWLAKHLGVEPSDMLFVGDALYPGGNDVVVIPTGVQTIQVAGPHETETVIEEILKACSG | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
EC: 5.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 252
Sequence Mass (Da): 27789
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A0A1G2G8J6 | MNYIACFGIVTSMHRFFTPQQLHEGSLMIDDAALAHQVRSVLRMKQGDEIMLFTDGESLGWDFRFRIERVTDRVLSGKVTERVKNEREPRVYVTLFQALLKKDKSEFIFEKCTEIGIHAFVPVVSERSIKKAINEERARKIIKEASEQSGRALVPNIQPIVSFADAIATVKKAGSLNIIAHEKEMRRSLDAAPPASRHISLFVGTEGGFSEKEITMARNAGFFITSLSRRVLRAETAAVVGSYAVLHRFGN | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A7C6PSV3 | MITPTVAVVLLVIALIIFGPGKLPELGKSLGRGIKEFKAATSEDEKPEPAKVEKEQSKDA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 60
Sequenc... |
A0A540N936 | MAGTNWLRSRGLLSGRDKIIRDIEKRIADFTFIPVEHGEGLQILHYEVGQKYDAHFDYFLDEFNTKNGGQRVATLLMYLSDVEEGGETVFPAAKGNISSVPWWNELSECGKQGLAVKPKMGDALLFWSMRPDATLDPSSGCPVIIGNKWSSTKWMHLEEYKV | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 162
Sequence Mass (Da): 18299
Location Topology: Single-pass type II membrane protein
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A0A4Q7JI97 | MKPSVDLLPKEQVVDHLPKRFRSLKFGIQSNQNVANQAVVEVSDRLLYDIENNRAPYPNGPLDPRLHVVSQSCGGVLLDESEKQMFLKELRRPSLDNLRRTQICKRINESCRKTKHCFSCGSTNGQIRKVGVLKLVHDKFSAYNKSTATKKVPPESKIKFDESFAEARSQVPDLEKHLRKAMEDLNPLRVLNLFKCISPVDCELLGLDPSEGRPEMFIWQYLPAPPVCIRPSVAQENASNEDDLTTKLADIVWVSGMIRAALQKGSSIHTIMEQWEYLQTQIAMYINSDVPGLQQAGFGKSIRGLCQRLKGKQGRFRGNL... | 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: Nucleus
Sequence Length: 723
Sequence Mass (Da): 80917
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A0A540LKD7 | MISLTDVYHVVAATVPLYIAMILAYLSVKWWKLFTPDQCSGINKFVAKFSIPLLSFQIISSNNPYKMNHKLILSDCLQKLTAFLALAAVTKFSSYGGLNSIITGLSLSTLPNTLILGIPLLKAMYGDEAAKLVTQIVVLQSLIWYNMLLFLFEFRAAKAASVTPSSEPTADEMEVPHEAQSKDETEDETRADNTRKIKSILLTVGRKLITNPNTHATMLGLIWASIHYKWGVKLPEIIAQSISILSNGGLGMAMFSLGLFMASRGSIIACGTRKAMLAMGLKFIAGPAIMALSSFAVGLRGKVLRVAVVQGYFWDAHCIA... | Function: May act as a component of the auxin efflux carrier.
Subcellular Location: Membrane
Sequence Length: 338
Sequence Mass (Da): 36659
Location Topology: Multi-pass membrane protein
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A0A8J7UC30 | MSPIDSSPFVRTEWISPLGPLLLGSIGDELLLCDWKYGRHREAIERRLERLVAAERQIGTSPVIRETQRQLQAYFEARLSAFSLPIRYVGTTFQQSVWEELLRVPFGRTASYGELAERIGNPNGVRAVGTAVGHNALSIIVPCHRIIGKNGALTGYAGGLEVKEALLRLEHII | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A8C5TD49 | MLPVIKALLLLIGGQRTRVTSECITNSSMNLNADTFMMLSSSCWKVCGMCITSKLKIKTNKSSILYESLLCRSWHGKVVFFLCVELVAALHPWQTFSYPYASCNVTEARLPLFLSSHCTDTYHHHWREGNLSSSARCEVCKKTCGSSEVLSGMRCEWCGILAHAACYVIVTPECTFGRLRNMILPPSCVQLFSRNFSKLHCFRISENLQTESGKNFKASKIPRNCCPLLVFVNPKSGGLKGRDLLYSFRKLLNPHQVFELTNGGPLKCTVIPVTKFHTFSKVPSFRVLVCGGDGTVGWVLGALEEIRHKLVCSEPSVAIL... | Pathway: Lipid metabolism; glycerolipid metabolism.
EC: 2.7.1.107
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 504
Sequence Mass (Da): 56115
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A0A8T2P282 | MSSIEKALKSHFGFNKFRSQQQEDVVKAVVKGDRDVFVCMPTGAGKSLCYQLPAVLARGITMVVSPLIALIQDQVDQLQARNIPACSINSKLPAGERRKIFEDLERESPCLKLLYVTPEMLASPSFQPCLSSLCSRGLLTRLAVDEAHCVSQWGHDFRPDYLKLGELRSRLAGVPCVALTATAPRRVQEDVARSLRLRQPLSFSTPVFRSNLCYDVIFRDVLPDPYKHLYAFAMLALGDGSAGKGCGIVYCRTRDSCEEVAHRLTGLGISARPYHAGLKAADRTEAQSNWMQGKVLVIVATISFGMGVDKANVRFVAHWN... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 557
Sequence Mass (Da): 62072
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A0A7X8KS73 | MEKMISKVLIDQDTLKKRVAELGEQITNDYKGQELLVIGIFKGAVPFLADLIREIKIPLRYDFMAVSSYGSGAVSSGAVRILKDLDTSVEDSHVLIVEDIVDTGLTLKYLKENLARRHPLSLKIVTLLDKPD | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 132
Sequence Mass (Da): 14712
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A0A9D2R685 | MIQINMNLVYTIINLVVLYLLLRHFLIRPVTQIMEKRKQMVEEGFKNAQDMQDQAARMKQEYEEALNGAKQESLRIVDSARRSAKAEYDRIVGEAGDKAGSIIESAKETVRVEREKTMKELQSQIAGLAVASAAKIMSGNGDGQTDSSLYDQFLKETSGETGEGSENED | 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: 169
Sequence Mass (Da): 18879
Location Topology: Single-pass membrane protein
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A0A069DG48 | MAGKLTTHVLDTSRGIPGRSMKVELYFIESTGEAKYLASAQTNDDGRLDAPFLEGELTTGTYELRFHAGEYFESFLNETGIRSIWDVIPLRFDVANDEEHYHVPLLVAPGGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 118
Sequence Mass (Da): 13180
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A0A0G1C2R7 | MFHLYGLMIGLGVLAGAWAASLAESRRAGKKDKHAWDAVFWAVGLGVIGARIYHVIDWWSYYSQHLLEIPAVWRGGMGIYGGILGGVIGLWIYVKKRKGRILPLLDAGAVGLPLGQAIARWGNYFNQELYGQPTDLPWGIYIRPENRLLSVWEYEKFHPLWLYESLWCLVIFLVLLKVVKKNQFIIYLGLYGLGRFFLEFLRIEAWTISGINVAQAISLGLILTAAGFIMGRK | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A1V1PL12 | MTTLGQALDTLASTIASRVGADPATSYTASLLAGGPAKCAKKLGEEAVEAAIAAVSGDKANLAHEAADVLFHLMATLQASGVSPAEVAAALEKRKGVSGHDEKAAR | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 106
Sequence ... |
A0A1J1DUR0 | MNATNAHDRHSNIPAGSSTPTDHLAAIRAAIDATDAALLKLFNRRSALSIKVGRIKASVPGIIFNPLREREVMDNLVLSNTGPLPEEHLRTIWREIFSSSRVLQRPQNVAYLGPEGTFSYFAGVEYLGHAVSFHPCGDISRVFEEITSGRCELGVVPLENSLQGTVGVSFDLFLKHDVFIQAELFSRISHCLLSNARSIAAIDVVYSHPQPLAQCGSWLRAHLPNAGLAPVESTAAAAHRAAAQNNAAAIGHGKLADITGLAVLARSIEDEQDNWTRFVIIGPKAAQQRQAVPRPSAGAGADKTSVLFTLPDKAGALSAV... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC... |
A0A316GD65 | MGRSEPYYSVPSARTEPAMTGTQDLESLGARQALDALWRGKMLIAAIAAAGAILALAFALVMTPTYDGRVRIALETRNMAQDAGAGQNEETEISNATFLTEMQVLRSPVLLAKVAEELNLASVPEFGAADAPALPWFSDGEALAPVSPQQVVERLGKHVQVLRDGTSYVITIVTTSEDPELAAAIGNEVAEQYIAWQHGRRQTSLLRMTDWLETRIETIRAQLEEAEERVASTRSSNLAESGVTQGALETRLASTNDELTRLRTELAAHEVRFEEFERLKAAGSDAATAVPAESDTISSLKQRLAELGANKVDMIANAGS... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 751
Sequence Mass (Da): 81755
Location Topology: Multi-pass membrane protein
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A0A4U0YGN9 | MFTGWVTCDRRTRSCWSRSPARIAATRSRPAASSWITSRRTRRSGRRRSTRRATPAGWTPARATRSHVGAGSPISIEPGGPRVESVERVIERLAEWIGPLGETERVPVLESVGRVLAEPLTAPRDVPIAPLSLFDGYAAAGPLVSGTSLPVVGKQFAGDAPARLESGTAMRIFTGALLPEGADTVIAQESVTVEDGRARWDEDVSLGAGVRATGADTREGQTLLERGIQINAAMLGLIASTGVASIPVSRRVRVALLTTGDELLAPGEPFAPGKIYDANGPMLEVLLKAAGVEIVQRAVLPDDPTVIDARLREAAEADLI... | 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: 479
Sequence Mass (Da):... |
A0A4P8IFW3 | MKNGIFVTATGTDIGKTYISALLVKTLRRQGIDAGYFKPALSGAVWSEDRLVPGDADYVCRKSGLSGPPDQYVAYVYEPSVSPHLAAKMSGRPIEKDVVSQSFLEIQKRFDYVVAEGCGGIVCPLRADDDEMMMLTDVATLTGFQLLIVAPSGLGAIQAAVTTAEYAAMKGFEICGIVMNHFKRGDLIHEDNRYQIERLTGIKVTGVADDAEEIDVSCFL | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A0G4IQ64 | LQVAVAAPNSDAVEKLRLGAVTRAAVCCTVGTPRAPMVVRWRPAAGSHRGRRMHGIVSEIRRLAGEGFPVRAERIEILDSPADFYERLLSISNIAVVAVPRDGFIGKKPGTTNMDNPGPPAESLRKVISNHGDLSVNVVLDYHRGQRRDRQGECSMSVLSKLATCFPAQFKVHLFRVPQWRWIHDAVVRWPRWKELVGVQHAKLYVFDDTVIISGANLSNDYFVNRQDRYYVIRDAALADFSHDLVARFARWSHRLQHDGLSLSRPLEPPSTIDVQPDKRTSAKRDEGSMGPTDTFVFPTIQLDVAGVRLDHELLTQIVS... | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-... |
A0A316G3A0 | MTAFSETERRGQPSRARPEGLLLWMHASTPPEAGPAPALARALSRLRQEPVSCLVTTDAYGPLLPSLVAEAIHHAAPDESSAAIQRFLDHWRPDVAVEMGVTDRPKLFAAMARRDVPLYHVSPSREAVGARRRYPDYLGAFRACLAVSASEAQVLRRSLGGTGTRIEITGPLCDTILAQRCNQAECDTLAQLLGGRPVWLAAQVRAHETDVIEAAHRKAFRSAHRLLLIVTPADPSEALAIRARFEAGNWRTSLRSEGGEPDPEVQVYVADGEDEMGLWYRLAPATYIGGTLTDGPPLADPFDPAALGSAVLHGPAIGQA... | 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... |
A0A5C1D9F5 | MIKRRFNFMLFSEKLEHGCGLSKSMYSSALGGTNNSSDSSIYNLICMESVSGSESGSSSTSIRTNGNDSNFDIDINHKYKHLWVQCEDCYGLNYKQFFKSKMNICEHCGYHLKMSSSDRIELSIDPGTWDSMDEDMVSLDPIEFDSEEEPSIEQEQPIEEEEEELYKEELYIVEPPIEEEEEEEQPIEEEEEEEEELYKEELYKEEQPIVEPPLEPPVEQPIEQPSIEEKCFRKKPYINSVPSKEMEEYINKPFKDEDFFTYLNQQYYSKRKRFSIIKVPKEPPVEQPGSIEPPKEPPVEQPGSIEPPKEPPVEQPGSIE... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group... |
A0A1E4SSR3 | MASTTPTHSLPFLTPEDLVPPVNRGLKVLDKSLFTKKFNVWSVTFPQFQHISDFLKNCKDDVLKLPKISPVTKPMPENNNMKSVLLTERLVDLSKKDQVLSKETLKDIDSNNGKFQLQSIELDYSYWKAEQILKAILPVELHDDVPSSFTVTGHLAHLNLREEFKPYDRLIGQVILDKNTSIKTVVDKVGTIDTTFRTFEMKVIAGKPDMIVELKESDCIFNFDFSKVYWNSRLSTEHNRIVSGFQAAEAVCDVMAGVGPFAVPAGKKKCLVFANDLNPNSFKYLSRNITKNKVQDYVVPFNQDGRDFIKSSPTILQQYA... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
A0A8J5CII4 | MLGSFSVDSRKDIMFNNSMMPKLCSNYIPDGTGSLEMEPPLDLKSGWDRINGFTATTADTFNHFLQWIIKNQNQLKAKNSSDKLRVDILCTRGTLKSVMLAPCTRNQNCEMIILAQSFKGSIYMTYKYDDHEGEKKDNSACFENYGHKFQQYMTGGNPDDVLECDCQFRCVLNLHLNELSLLYPIAIHGVDESLLQGNLTDTSAFVSIKETREKVNSFKQDCYERYTLNKWWIENQLAGIPRLLMGTRNEQAEVQTVQIMHTDAMPSMAKGKWKPSVCINFLERFLSFVMEKVTSEPNQVHRFDRSASDSDYITHFHDTS... | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 341
Sequence Mass (Da): 39260
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A0A847QNK7 | MPGKSGYEICRLIREQYSLLQLPILMLTVRDSQEDILKAFEVGANDYLAKPFNKREMLARVRTLLTLKRTMTEVLSSEMRFLQAQIRPHFLYNTLNTIMGFCRKDPEKARELLDQLSCYLRGKFKFGEMDKFILLKEELELVKAYLHIEKARFGDRLQVVSSFPAGANYWIPPLILQPLVENAVRHGIYPRKEGGTIVIKAEDLADALVISIKDDGVGMSKTKIEEILNTQKEIDGIGLRNVNQRLKSHYGQGLSISSEEGRGTTVMVRIPKNRERGS | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A540LSQ4 | MWASKKGGLPEATLETTIGILTIEINSPFSQTFPSIFFHFLRQGGDPTGAGKGGESIYGGKFEDEIKQELKHIGAGILSMENAGPNTNGSQFFFMLAPCPSLDGMLTFTQ | 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: 110
Sequence Mass (Da): 11804
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A0A3B9M4P5 | MCIRDRDNSLVGAAAVIDKDRAASLLASLLQADLLIIPTAVSKVSLNYRKPNQIDLDHISLDKAKAYMEQGHFAAGSMGPKIEAAISFLESGGSEAIITLPELIDDAVLGNGGTRICS | 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: 118
Sequence Mass (Da): 12438
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A0A540N8M9 | MVKETEYYDVLSVTPSASEEEIRKAYYLKVLGEAYQVLSDPVQRDAYDRNGKHCISRETMLDPTAVFAFLFGSELFEDYIGHVAVASMASSQLAGEGDSTEKAVQKEREEKLANLLKGFLNQYVLGYKEGFLEHAESEAKRLSDAAFGVDMLHTIGYIYSRQAAQELGKKTIFLGVPFVAEWVRNKGHFWKSQMTAAKGAFQLLQLQEEIRRQFKMDGSGPENDAESHIRLNKDTLLNSLWKLNVVDIEVTLLHVCQMVLRENNVRKEELKARALALKHLGRIFQEEKQTRNGGTSRRKSSVDKDDDGSSSDSSSEEDSP... | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Interconversion of serine and glycine.
EC: 2.1.2.1
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Length: 848
Sequence Mass (Da): 93786
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A0A8T2PK30 | MGQTYALPLRTASERAQWAARGTACQLRLQPCPLQLCRLAGRAPGGHTGLFVTRATHTIAMELLRHNNPFSSSCADRARMVADREEDEYQIPSSHPVTLTQPPICISVRIPSRGLESGPFVNGLSDHSTEGKKHKALEYGAHFDSGLFVSGAPRPALCPSLNRTPSDYDILLPPQAEDLFNSAPPSQPPPPPPARHSFAESSSSPSCSRAARPASGHDSFMLSSVATESIQAPARPPKPLPRKTPPDVHHRKAHGHDSAKENVDAKIAKLMGEGYSFEDVKRALMIAQNKVDVARNILREFALVAPRLNL | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conju... |
W2ZZ58 | MRLSHLVLLGAVAISLLTEASLAAEAPRLGSDISSMTVVSRGADQGVNIDKRMLRYHSNNKRDAEEDEEERGIPSGVDLSHLAGLAKTNKADSLGTKLTEFFNGMVKGRVNPSNIHKTELSGADYDILRQRFATWYRHYKDIE | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 143
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 15828
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A0A8J5D1Q4 | MRKITKICVKGLLGLAIVAVLVTLLSPYTPNLHPRLPQNPNPSPHNPHAPPTPLRLQQDPNPSPHASPTHPNSPEITSIPLKVQPNPNPSTHAPPTPLRLQQDPNSSPHAPPAHPNNPETTSIPLKVQPNPNPTTHAPHEPLRLQDHNPSTHTPLTPQQDPNPSPHATLTHPNNPETTQIAQTNPKSKEKNFKQTSENGYSKTQTAGRMDTKVDGPRDNQEVPQPPPLSYPTPEGYVEVAKDIKKPMKWSRIQGKELMRRRKERLKDVKEKFLKVLGYSPKELQERAKSFPDSSLEAEEGGGGGGGGEEEEAAEEEGEEA... | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 625
Sequence Mass (Da): 67896
Location Topology: Single-pass type II membrane protein
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A0A7X9GEK7 | GKVTGLSKLARVVEGYAKRPQLQERLTSQIADSLMNKLNAQGALVVLEAEHMCMTFRGVKKPGSKTVTSAVRGIFRRNKATRAEAFSLIKN | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 91
Sequence Mass (Da): 9974
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A0A0D9XIX3 | MEHALSSARDVLYNYGEVSRRLPVMLQSTELNIDSLKKQNSFLVQHAAKIVPMPLHCLHMQLTTDYYFRDGVIKEYFRGAALKEEEDKAKCENQSLYHYAMFSDNNEYRKLWKLGTLPPGLITFYNLTCTLNLNWHVLGLGYDPAVDLAEIENAAVVHYNGNYKPWLDLGISKNKPYWSKYVDLDNSHIQRCYMSEQ | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 197
Sequence Mass (Da): 22920
Location Topology: Single-pass type II membrane protein
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A0A8J4YJF3 | MVALLWSSVWPVVWACLSVTLETDARVAGRSSDPNVQHGDGGQIVSDPSNLPELPMGKPDTIETDIPGEPLSPSDFEKSVGMEHNTIDTSTQADPIELAGLFQGDIMLNSKDTLADLAHGDPKTGRKGRSAMVDIHRRWPNGIIPYVISQAYDYSATDKFARGTIAKAMLEFHEKTCIRFVPRTIEKDYIHILKGDGCSSSVGRVTGAQQVSLGPGCLYVGIVMHEFMHVAGFWHEQSRSDRDNHITININNVQEGRQHNFDKYGWDKILSLGISYDLESVMHYGPYAFAKGRSPTIIPRENGAEIGQRRGFSKRDIEKL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 484
Sequence Mass (Da): 54257
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A0A481QH33 | MKKVLALIVAATMGLSSVAFAAETTAAATAAPAATSTTAAPAVEKAAPAKATHHKKHKATTEQKAQAAKKHEKKAPAQKAQAAKKHEKKAPAQKAQAAKKQVKKAPVQKAQAAKKHHKAAKKSATAPAA | PTM: Proteolytic processing gives rise to the active protein.
Function: Required for growth and/or survival at acidic conditions.
Subcellular Location: Periplasm
Sequence Length: 129
Sequence Mass (Da): 13147
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A0A2Z6E7C2 | MNLPYLLALLIPVAFLAGWLAARRAAAYRSDVQVSALSSDYFRGLNYLLNEEQDKAIEVFLKLAEYNRDTVETHLALGNLFRRRGEVDRAIRVHQHLVSRPGLTEEMKTVALLELGEDYMRAGLLDRAETLFSDLVAMNAHAPSALRHLVAIYQHERDWHKAIEHARRLEAMTGESEAQTIAQFYCELAERARQHGAYAEARDYLRQAFACQVDCVRAYMLTGRLHAENGEHAEAVEAYEKAVAADVAFVPDILPPLLHSYARSQQMERAERFLRELLTRYHGISPVLALVRLYERRDGERAAIDFLTSQLRQRPSVRGL... | Function: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Subcellular Location: Cell inner mem... |
A0A552AHB0 | RYALNNIYLILFGLSGQLFFLLALQKNQKLNWLFLSGVCFGLAANIKWNGLGFLLGIFIFIGIAWLIKLLNQEQSKDNLWTKATNLRLEYIFIALIVFPLVTYSLLWIPHLLVNHQYNFWQVHQEIWSFHQGIKGNQSDVHPYCSPWYSWLVMGRPVAYYFKRVGDKIYDVHAMGNPFLWWFSTGAILVVFSRLFNRKERVISAYLICNYIANLLPWLKISRCTFLYHYMAAYSFTLIALAWLLADGLESSSPIYKNCSRSLIILIIFAFIHWLPIYLGIPLSVRDYYLRMIFSNWI | 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... |
A0A7Y2CAM2 | MSTGTLRILTAVVGAPLVLAATLYGGIAFAALVLVAAAACQIEFYQLTKATDNRLMVGLALLAGALIVAGFLEPLLWVVSALVLILIIVVFPFADKAGGGVHSISALLAGIVYPTTLLATLVGVRLSAHAAAAELTILAVVLVWSSDTFAYYVGKTVGRHQLTEISPKKTWEGSIGGLIGAGVVGAILKLWWFGALLGWLDVALLVVICGGLGQLGDIFESKLKRSAEVKDSGSLLPGHGGMLDRLDAVIVVAPLVYIVFVAGLRYVP | 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: 268
Sequence Mass (... |
R6EQZ8 | MRKESRLRHAKNQMKYLTGFMMAWGNFCSLPCPAKHWDNNYTSLMLGFLPLIGLVIGIIWSAIYFGLVYLGFPFFVVAFLITFLPFALCGFMHMDGFMDCCDAIMSRRPLEQRQLILKDSSTGAFAVVGMIFFVLGYFCFLSTAVTTGVDFANMVMIVVMSRSISGLHVLICKPMGQSQYAMLHDAEPPEETLPEETLPEEEPTEESTTEEDCTELVACDSVETASKKASAKSGVILLLVLLAVITALAFWCSSLWLATLIVSAATALGSLISIQYAKKNLGGMSGDIAGFGIIWGELMGVFALVLC | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A8J4XR85 | MVVTEGVTTKIMHRYHSKPPNLRLDAFPPHIMRRRTTSSMWDSKLTRQGTSMGQFAFSYQPHTDHDGSGLVEHEACLDLEITIQKGESISKGSTFQDFMDTPDPYVVLRIPGSSNSSKRTSHVDNCTNPIWDESFHFYLDPAKEYDLNMVLMDANYTVDETLGEQTFSISLLTLNVPQEVTFNYANDSKVHTILTLRKNKTPDLRFSLALCQDEKDFLQIRRRRVLDAMKNLLGPKAPENEKQVPIIGVLGSGGGFRAMTCLSAAIKALQENGILDCTTYISGLSGSSWYISTLYAHQQFPNVTHSQLQKELKDSVTKDW... | EC: 3.1.1.4
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Length: 999
Domain: The N-terminal C2 domain associates with lipid membranes upon calcium binding.
Sequence Mass (Da): 113561
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A0A7W6K618 | MHIDWWTLALQTVNVLVLLFLLRRFLLKPVLAMIDARQQAVARDMDAASRARAEAEAAKADTEKRLAAIEAERAARLGDAQKDAEALRAAALKAAGTQADALRLAAMADIERARAADEQAMADHAGALALSIAERLLQRLPETLRTEAFLEPFALAIAALPAESRALIAGADTVELKSAAPLAAAQADAFRDRIAGLVGAPLAVFSVTVDPDLVAGLDLVTPHLTVRNSFRADLETIQRELSGHAL | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell inner membrane
Sequence Length: 246
Sequence Mass (Da): 26205
Location Topology: Single-pass... |
A0A540MY74 | MLKTMGGGGGGGYGDEDCGDLLGNDVYNNRCPEAEAIIYAAAGGCDASALLDDNENIVALKDMVALFGAHTMGKARCTTFTARLQGSTTALEYIQLLRQLCSESDINTLANLDLATPATFDDQYYLNLLSGEGLLLSDQNITTRDDQTRELVETYAQDPSAFFGDFKDSMVKMGRVEAWE | 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: 180
Sequence Mass (Da): 19421
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A0A1I5FDE1 | MEALTIKEIAQGVGGTILTGDENMQITNVSTNSKRLEAGSLFVPIIGEKVDAHDFIPDAFENGATACFTSRHKELTKDMNQSMVYISVKDTLEALQALGTYYRSKFKIPVIGITGSVGKTTTKEMIAAALETRYKVLKTEGNMNSQVGLPLMMLRLDSSYDIAVIEMGMSEFGEMARLSKIARPEAAVVTNIGVSHIGQLKTRENIRKEKLNIINSFRSDSILFVNGNDDLLSEVYTASHTLQARKNGAGDGFEEMNKEYSQNPVIIDLSPETLEKFYQSKVIGFGTEGIYDYWAENIRTSQGKTYFTLRKTRKDNKESK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A8J7NYL4 | MQAYCASNPSGFYHMTSHQQDSLSLTFRRGRRPDAVLGRVEMEFEGLQVALSAASAPSMCFTVRPRRGCLVLCLGLSLLTLLLQSLWMPESSRETPPGKSPAVEDSSRHGVRRLALRLDALSSRIQRLTRDGDPPGLHDLPRVLQRAPSLSYEQFLQAGWHSDPCYAFYGVDGTDCSILAYLSEREDFCPTLPSRSLAIIPDWLQESTREKREALIRTDLTPLFEVIGSSRGPAVRFMLSRIKRLSRRWAKAGEKIRQKIGHRPQQQLRVLLYPGVLAGGAGQRFGEMVEKGGPLGELVQWADVSTALYVLGHHLIFASS... | 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-... |
A0A1E4T2S2 | MIKTSSLIFVLLWGVLFKLERMSLRLLSIVLIMSFGVVMMVWGQNEPNDTNQIDDSIIETDINEDIGDTSSDNNLLYGEIIPDNTNSNIIKLIKRSNLNSKNLILIGSILVLLSACMSGLRWALTQIMLKKNKRTKNPILTMMYLSPSMFIILILIGCLVEGFKQFLNSPIWLELGILKTIILIIIPGLLAFFMTLSEFVLLQYASLLTLSIAGIFKELLTILISWLLFDDVLNFINLIGLVITLSDIIWYNMYRFEQNQKEQIVQDIELSDIRK | Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 275
Sequence Mass (Da): 31384
Location Topology: Multi-pass membrane protein
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A0A8J5CTW9 | MLSYLCHCPCWGLKAEVTQQSPVMASTLVCRSVLILLVVWLELSVATPAVPPGKELLARHLFAFIPRHLKPSVSVTCLECRSALGALELWIATGATVEDVENFAINECITLNLFPEDVCFGMVKLCGSEVVYVLKTSKYSHDTMCGWMFGLDCQATELDPWSVEIPDGKPEPNHPEPQQPTPSVKKILHLSDLHVDLLYNEGSATVCEHPYCCRHAFGAPGPGVPAAGHWGSIAYCDLPLHTLEDLLAQAAAITTPDLVYMTGDLPPHDVWAQNRATNLLAIEVTMDLIKKYFPGIPVVNTLGNHASAPVNRFLQYFNVS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
EC: 3.1.4.12
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 631
Sequence Mass (Da): 69573
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A0A8J4YEU5 | MNSGRKQAGLLITQADNTSMPICMRTCKRTRNQVAATVVAIVMTTVIVMTMSEPSLRVHKYQLQRNDTFIPNYPNQTLVGRPAFIPHRFLIEEADACLRKGREVEVVVYVHSAISRVKQRQQTRLTWASSSALKMVVVFMVGRAKDDTEREIVRRESELYHDIVQGDYGDYYHLLSYKGLSSLYWITRNCAHVPWTLHADDDILIDTFLLKQFLQVQRDTSDESKLHCRTIRHAKVLRKGKWKVTQEEMDAKRYPTYCQGILWYINTRQLPNLLDASTSVNYLWVDDVYITGCLTREASIGLSDLVNTSVHVLSL | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 315
Sequence Mass (Da): 36288
Location Topology: Single-pass type II membrane protein
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A0A540KSF0 | MDTSAADDHSDEPLTPVGRLLLQPEMNQIIHCAMGFKNSIDIDAVKSHLKTSLLSHPRFSSLMLRDSRGLQHWHNAPYVDLDRHIIVIQNPVTTSPVNHETAVNEYLADLSTSSTRLSANKPLWELHLLMAHNCGVFRIHHALGDGVSVMSLFLESFRTRGSDGNEENILGRGRRKRVNGEKGWWGLLIGYVGTLWFSLVFLVEHAMRSLWLCDQKTAISGGEGVELWPRKLATARFRLQDMKLVKKAVPNATINDVLVGVVSSGLSRSSINGNHDNQVIAKLNCPDLHDGIRITGLAMVNLRKQPGLQVSNSLESNSES... | 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: 519
Sequence Mass (Da): 58327
Location Topology: Single-pass membrane protein
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A0A2D3UY38 | MNRYSSREAALEAGLHHKRVFCDLWLTDAIKFWMYRQTVAENNESPVAIRTSALGRQRKAVESAPGSGHEEPLNQQDGQMESVALPLLDLHHSADNHEPSADEITLSYPSGHRERFSFGKRSQKREHKYARTQDPAEDIIRTIEVICIQAGINKDNELKVKRAILELSLKNRKDLDAVKLPPLQTIIQNTCGWSTGMKLQRFDCGLQPELTEHFFDQLHDRSIADVASLLERTGEKARDSTYGELTPQFLTSIFLKTGLTASCTYLDLGSGVGQTCMQASLETQCTSFGVEREGKCHTVAITHLSQFKARSKLWGLNHGD... | Function: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared... |
A0A7W6K3F1 | MGASQGVKELEELVHSGDVPDINATGIGARVGNGVLLIATFCFLAGTGVTVMDVALRALLGRNLPGAIETTALTVGLGALLSIPACYLYRGHVTAKLLSEIAPGLFAKPLGLFGAFCSLMFAVLMFAILVVNLREKIGSPETTSDLQLTMWMLLGVITAVSGVGVVAALRALFSSGDTSKVLDN | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 184
Sequence Mass (Da): 18977
Location Topology: Multi-pass membrane protein
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A0A0D9WH03 | MEARVHYSATALLLVAPTPAPSTSAGALPAAEAAENGRGGGSLAVSFKANAIVLLSLLVCGLVAAVALHVVLQCALRVTRRACHGADDVAPHETRRAGAGEGRARRGGGGRKRTAAPPLSKTIPRVAYTEGLELAGSARSECAICLAEFASGEQVRVLPRCNHGFHERCIDRWLAARLTCPTCRQPPFPADAEPVAPDPAPATTTRDVPVVRVIVITSQ | 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: 219
Sequence Mass (Da): 22762
Location Topology: Single... |
A0A7Y2ETH0 | IHPRQDERHITRQDAIDLGRMVDDSGDIELNIEGYPSKGFIDLVEEVNPTQCTLVPDSPTQLTSDHGWDLTRHFDQVRETCSRLNSAGIRSAIFLDPDKSQIRIAPDTGTSRIELYTEEYAQTFGTKDNGMVFRKFEEAAMLARELGLGVNAGHDLDLANLADFLKIEGILEVSIGHALTVECIEYGMQAVIGKYLAICSQSIN | Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phos... |
W2Z0M2 | MRFFYALAAVAVFFIDSEVSPVEAEKSLIKLKPLKGAQVVATPNTNKRFLRQYAEFEDEDSEERIKTGTVVLDTTKKIDDFFWYRDYQQSSRSKADRRSTERKEAFWVVGYEDI | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 114
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 13360
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A0A8J7T8K5 | MTTSLAPVSSSKVTTTPVSTASPDTTVMPQIPVQEPTSAKPEATTQDITSPPIVDVATSAPSAADTPLGSTTAEMDFPHSEDLEPTTAAHSTSATLPSDDQSADPFVKGTSVVTVAVPSQPPTTAGAEDVTFREDSVLSSTIPVHTTQPSIELLPENNEIHPNPRMVNEAINSNVATVKPEKPIEKLLIELANPIYSYYSETSEQAASEGLLENKEVLAGVIAGGIIGLAFAVLLVALMVYRMKKKDEGSYALDEQKHSNGGYQKPQKQEEFLA | Function: Cell surface proteoglycan.
Subcellular Location: Membrane
Sequence Length: 274
Sequence Mass (Da): 28942
Location Topology: Single-pass type I membrane protein
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