ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A1B1ATE2 | MAKILAVLYPDPVGGYPPDYARDAIPSITGYPGGQTTPTPRAIDFTPGRLLGCVSGELGLRRFLEDRGDTYVVTSDKEGPGSTLDHELPDADVVISQPFWPAYLTPERIAAAPRLKLAITAGIGSDHVDLPSAIGHGMTVAEVTYSNSISVSEHAVMQILTLVHDYMPAHEWVTAKKGWNIADSVSRSYDIEGMDIGVLGSGRIGKAVLRRLKPFDVRLHYHDVHRLPEEVEEELGLTWHPDARSLASAVDVLSIHTPLHPQTMNLFDDDMIGAMKRGSYIVNTARALIVDRDAVVRALDSGQLAGYAGDVWYPQPPPSD... | Function: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Catalytic Activity: formate + NAD(+) = CO2 + NAD... |
A0A1F4YA57 | MSDKIYTISELTRSIKELLESNFVRIWVEGEISNYLRHSSGHRYFTLKDQAAQIKCVIWKWAGNSLIFEPQDGMKVRAFGQVTVYEKSGQYQLNITSLQPAGIGELEIAFQELKRRLSDEGLFDPAHKVPIPRFPMRIGVVTSPTGAAIRDILNITRRRAPNVEIIIWPVQVQGEGAAGQIAKAIRGFNRLELVDLLIVGRGGGSLEDLWAFNEETVARAIYESELPVISAVGHEIDFSISDFVADLRAPTPSAAAEMAAPDINQLAMRVDELVGRLGDDITDILSQLKLRLVELGSRYGLKRPLDIIIQRTHRCEELRK... | 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... |
A0A651HI23 | MPLAVVGVSHRTAPVEVRERMAFGPSEASRALLTLREEAGVEEAVLLSTCNRTEVYLYPSRDASHLGVVERLLQGRAGDLERPARDYLFEQRGEGVVRHLFQVSSGLDSMVTGEAEIQGQVRDAYELAISLAVDPPMAGPVLNRLFQMALSVGGRVRAETSINEGAASVASVSVELARKIFGSLREKRVMILGAGATAELVVEALSREGVRGIMVANRTYDRAVELAQKLHGHAVHFDELSTALPSADIVLASTAAPHHVLSRETFRRAFPGRRGHPLLIIDMAIPRDVDPTVGDEPEVFLYNVDDLRKIVDEHVQVRSE... | 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... |
G2SY54 | MIIDRGLDQKGTDANIGTSRVNLTQRYVESVKYNGLGDFTEELREEADYRKRIEKIFSEIHMTGETYADLQPEALMEAYWQGEEMISRYYWAKRRDTDDIIWVRVDVRIVPQLDTGDLFAFYNNWDVTHEKNRDRMMQLIIEFDYDYVEYICLQNGHFEIMAQEKSSMCPSARGTDYDADIRDYLTRVAVTDQLEAHIRAMQTEEIRRNLEAEPLYIQEIDVRESDGSVRRKMIRYTYMDKQMGTVFKSCVDIEDIVTEEKKKQERLERAIEETERANCAKSEFLAHMSHDIRTPMNAIIGMTSVARQECQDETICGYLD... | 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... |
A0A7J4SLF7 | MTPLLVKAARREQLDRPPIWFMRQAGRVLPEYREIRKKFDLLSITRNSDLAAEVTLQPVNKFDLDAAIIFADIVTPLHGIGVELDIVEGVGPVIANPVNSCADLNMLREIEPNEDVPYILDSLSRVRKSLPSDKALIGFAGAPFTLATYLIEGGPSRNYSKTKALMYSDPKLWHELMIRLSRIIASYLRSQVTAGADIVQIFDSWVGWLSPSDYSKYVQPYIEKIIQDISDIDTPVIYFGTGTSTLLRLIKDTGVDVVGIDWRIPLDEAWANLGYDVAVQGNLDPAALLGPFSVIESKTKSIIECTNGRPGHIFNLGHGF... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
EC: 4.1.1.37
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Length: 349
Sequence Mass (Da): 38785
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A0A919QQ55 | MPRTTRFALAAGVALGLAAAVVPAAPIALITPAAPAAPAATVAPAAPGTPATATLAAAATRTRAGESATAVVKNAAGRALGTVRIERYDAKKSRVSVSMRGLTPGFHGFHVHAVGVCDARSVDRATGSAFSSAGSHLGPGAHGDGAGDMPPLLAAEDGTAFASFVTDRFTLERLGDANGSAFVVHAGPDNFAHIPDRYFHRPDSTGATGPDATTRKTGDAGARIGCGVVKLHA | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in favoring mycobacterial survival in phagocytes.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 233
Sequence... |
A0A1H6BEQ2 | MATVSFRGLTSRSARFGAAAGIVALVFGLQFLLVRLVGPLPPYLLFYPAVMLAALFAGVWPGILATGLSAVAVDIWLLPPVGRLSIVNRADAVSMVCFGGMGLLMSVVAERYRRGQRKLAESAEARLQLFVEYAPAALAMFDREMRYVCASERWMSGVGLDVANPRGKSHYEVYPGLPEAWKEEHRRGLTGETIEREAERFDSPDGRVRWLHREIRPWIDTNGEVGGIIVFSEDVTERRRTQEQLERLGRTYAVLCDINQTIVREKDRGAMLSAACRIAVERGNFGMAWIGVIDLATGRISVLTSSGDDDGYLERVGVGK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 931
Sequence Mass (Da): 103089
Location Topology: Multi-pass membrane protein
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A0A7J4SL37 | MEGHLSGGVVVVGEDAKQRFHDSRGYGIPKKGNEIELDPVEAAHLLLRGDLDNIDGMDFIQFVSAQKPDFSAQFSTYLDLRFRGFHLTPVGASNNLSSSNIDFTVYERGTKPPDGVVKYELRVIGERSTIPADQLGEHTLAIVDEEGELTYFNTTEIEPNGKKQFLPPPSQGILLTDKVLLNNPDSTFHKEGFFGQHIPNTPHIQLSLVEAAYLCNCGSLSTNGNVLHQGRKIEGDLFDHRLSVYTVLRKRGLIPKTGFKFGFDFRVYQDFNTTENVLHSEYLVKVIKSKHVFSTKELSLNVRLAVGVRKRTLFAIVDGS... | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a st... |
C5RCL8 | MMKRLKIGSAVATERRPLVAVPMVDKTIAEIKSTAQTLRQTPADVVEWRIDFLLDLSELTVTNIRQVHEILNKPMIFTWRTVDEGGKLTYHHDRYQSVYHDAIQAGVEAVDIEVTLLADQQELLKLIPKDVKVIGSKHNFSTTPARLDACLAQMTKLPIDIAKLAVMPKDATDVERLLQATATAANESDVPLITMSMGELGMVSRELGYRFGSQLTFAVVNEASAPGQMPLATLLHKWGESYV | 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... |
D7CPV3 | MLSADGQKLFEARYAIRDEKGTVAETFDQAVGRLARTVATAEKEPSQWEERFARIIGELFFVPSTPIWANVGKPDRPWQPAACFVLPLEDSLESVFETLKDTALVFKSGGGVGYNFSAIRPRGFPVRSSQGQAFGVVELLRLYDHAAGIIVQGGVRRGACMGILNADHPEILEFIRAKLAGGLANFNLSVGVGDAFMEAVRENGTWRLVFNGQAIAELPAAEVWEAIVEASHACGEPGLVFLDALQRSNPIRGTVIAATNPCGEVPLLAGESCILGSINLAPMVDAAGNLKEVQLAETVGIAVRFLDNLIDVGQYPLTFI... | Pathway: Genetic information processing; DNA replication.
Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
EC: 1.17.4.1
Catalytic... |
A0A644VEL5 | MDAQTAGSLKLLKNLSLFTETYGCTYNAGDTEKLMEIARSQGCVPALSAEQADAVLINTCVVIDKTEQHMYERLDLYADKLLFVTGCLPPVAKEVLESRYPHIHVIDQAFIHSCYMEVATAHPGTNAVLQIARGCNGHCTYCITRLARGKLLSFPAEDILRQAGSIIKAGATEIQLTAQDTSSWGMDRNDGQRLPDLLKALCKLPGHFMIRIGMANPDTLLPILDDFLEALKDPKIFLFLHIPVQSGSDPVLRLMGRRYTSAQYEEICQRAREAFPDIRISTDYIAGFSGETDEDAAASAAQIRRTRPGKVNITRFSVRP... | Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
EC: 2.8.4.5
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladen... |
D7CKW1 | MHPILFRIGKVSVYSYGFMMALGIAVAVVGMRRMFKQNGYPEEKLYDLALVAVISGLIGSRLFYVVFYAWDAFLENPLMFFNLQGGGLVFYGSFLGGLVGGIVYLWRQKMPFWEVADMAAPYLALAYAIGRVGCFLNGCCYGKPTSLPWGVVFPGIGGVARHPTQIYSSLAALGLFVFLSWLYSRRHFSGQVFLCYVAGYALIRFIIEFWRENLVLWAGLTVGQVMGLAAILLTLPFYMVLKRGIRHG | 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,... |
G2SXR4 | MRFIGITGGVGAGKSEILGYLAKKPDTRVMLADEIAHELMSPGTECYDRICETFGAEDIFLPQGGLNRGKLAAVIFSDEAKRRQMNAIVHPAVRVYVEKEAAREKQGGKRKLLVLEAALLIEEHYDEICDELWYIYTREDIRRERLMASRGYSTEKVDRIFASQLTEEVYREHCRVVIDNNGSVAEAFAQIDRALSEKK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A4V2ZQA0 | MSKSIIVNLTTTIIITIIITIMVNSNLKNKRRLIYPSYAKINLFLEILGHLPDNFHQIETLLCSVSLFDTIKYTLTKKKDLKKWIYLNDNISENNLIYKVADYLYNQYKPDWGIEIQLIKRIPIAAGLGGGSSNAATTLLALNYLWELGLSIDDLTSIASIFGSDIPYFLYGGTAFATNRGEVIQPLEDFNLDNILLVNPNIMISSSEAYQIASIPTENERRHCRISQDVKWFFNRLEAQVRIDYPLVNEILNDLIKLGASTALMSGSGPTCFGVFEDKFKMHKCEAYFKEKGYWTKLVRTITREEYQNVFQA | 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... |
D3H589 | MENVILIDHNDCETGIAEKLYTHKKGILHRAVSVYICNSDGKLLLQQRALGKYHSPGLWSNTSCTHPFPGESNLSAANRRLREEMGIECPLSKLLKIYYNVYVGGDLTEHEIAHIFYGISDDEPVLNSLEAMSYKYVSLTELSSEIKFNNDAFSRWFVYCFPYIKNAFLNESNYTNLLI | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isope... |
D7N597 | MKDQYFREISYFRISLTPVCNFRCIYCMPYNQSFDKVNLIPMEQIEQIIKVSAQNGIKKIRFTGGEPLLREGLLPLCHKISNKIGIDEICLTTNGSFLKDMAKDLKKVNVKRINLSLDTLDSKKFSDITRGGKLKSTLEGLDEALKLGFKVKINTVLMGGINVDEISNLVELTKELPVELRFIELMRMGVTKNWQEDVFVKNDIVLDKIKGLKQIGNFGVASVYKIPGYCGEIGLISPISSCFCENCNRIRMTSDGKLKPCLHSKEEFDICNLSKEQVEEKFKEAVFAKPFQHKLLRGESETNRTMNLIGG | 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: 311
Sequence Mass (Da): 35278
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A0A2S9FJ89 | AADLTARIGAPLVVRGIGVRRVDADRGVSAELLTDNIEALVSRDDVDIVVEVMGPVDPARKAILSALEQGKSVVTANKALMAVSAGELAQAAESAHVDLYFEAAVAGAIPVIRPLTQSLAGDTVLRVAGIVNGTTNYILSEMGSTGADYTSALADASALGYAEADPTADVEGYDAAAKAAILASIAFHTRVTAD | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 194
Sequence Mass (Da): 19733
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A0A1F4YDG2 | MDNRPVEPHIFVIFGATGDLMQRSLLPALLNLAGRGHIRRESIILGTARSAQYNDVSFRKLAYESFAKAGISLDPGMTKWCDECLFYQSIGDEKLEDFSALSERIKALERELNSTGNRVFYLALPPIAFPSTIERLGEVGLSRSPGWTRLVVEKPFGRDLESARALNQLIHRNFDESQIYRIDHYLGKETVQNLLVFRFANPIFESLWNRDRIHSVQITVAEELGIGKRAGYYDRAGALRDMVQNHLTQLLTLVAMEVPVAFDSDSIRFEKIKVLRAIAPIMDDQVVLGQYGRGSANGKEIPGYLEEPGVPDDSRTETFV... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lac... |
A0A651DLV5 | MTPSSGEVDADILVVGAGAAGLSAALAAAGGVAALSGTPEPSASSVRSRGRPDSSVLLLTRGHLGRDGASPLAQGGVAAALDSGDSAELHALDTVLAGAGLSREDRVAILTTEGPGRVRELIGLGARFDRDASGSLELAMEGAHSRRRVIHARGDRTGAEVTQVLSRAIRRLPSITILEEIEAEELLTEGGRVCGLRVRRSDGSAGALRADAVVLATGGLCHLYLRTTTPRSTTGDGIAMAMRAGAAVADMEFVQFHPTAMAVDSDPLPLVTEALRGEGARLVDASGRGIDFPDESGELSPRDVVARVLWDLTRAGGEVF... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
Function: Catalyzes the oxidation of L-aspartate to iminoaspartate.
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
EC: 1.4.3.16
Subcellular Location: Cytoplasm
Sequence Length: 552
Sequence Mass... |
F8F1Y1 | MFLEFLYPLVKYFTPLNVFRYLTFRAAYGALTALFISFLFGPRIIEALRTLKVGQAIRDDGPQSHLKKGGTPTMGGVLIILSVIVAVLLWQDLHNFYVWLTLTGFVGFGAVGFIDDYLKVTQKNSKGLPAWAKLVGQFGVAFAIVLTLYYTEDEHITQLYLPFFKNPIVNLGWVWIPFAVLLLVWESNAVNLTDGLDGLAIGLVILVFIALSVLTYLSGRADYAAYLGIPYIQGAGELTIFCLALVGASVGFLWFNAHPAEVFMGDVGSLSLGGVMAVLSLIIKKEILLLIVGGVFLLEAVSVVLQVVSYKLRKKRIFKM... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yield... |
A0A5B8H9Z7 | MYCLKHIFKEKLNHMIKNINIITGVQSIFLVFNENVFSLEYFSTFNSQKNYVFSSLLIEEYFGIFIFFILATVIALVIAIASYSLTNQVPELEKLSPYECGFETYEAPRVKFEIKFCVIAILLIIFDVEMMYLFPWCVSVSKISMLGIWSMIDFIIELTFGYVYVIEKNALEW | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A524HNT4 | METGMLTLLLLAEEAGAPASPFEVNFGIFFWTWAVFITLFFLLKRYAWPSIVRATEERERSIQAYLAKAEEANLKAQQLAEENQRLLAEARGSAQQMIADAKQAADQERSLAVARTKKEQDALLERARREISAERDKAIVQLRREAVDVSLAAASKLIEERMSADTDRQLVEKYLASMATMRTPGSRT | 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: 188
Sequence Mass (Da): 21180
Location Topology: Single-pass membrane protein
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A0A2N5YZ66 | MKITKAIPSTITSLNLLSGTLSVVFAFRGDIEIAALFVIIASFFDFFDGLSARLLKAVSEFCKQLDSLADLISFGMAPASILYNLFILQNHNHKLLAYSVFLIVVFSALRLAKFNIDPDQTTEFKGLPTPASALVVISIAYYCFNNNTELATLFSNPYMLVGISIILSGLMVSNLKLISLKIKTFEFSKIFLHVILLIGGIILLIIFKSLGIGLTIILYLAISFLKQILTKKH | 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: 233
Sequence Mass (Da): 25706
Location Topology: Multi-pass membrane protein
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A0A6C1NJA5 | MADSSNGSGEAGAPEGRAAKRPADQLRPVQIEPGWASRAEGSALVHFGRTRVLCAASVLDRVPDWRRGSGAGWVTAEYGMLPRSTHTRRSRERDGASGRTREIERLIGRALRSVTHLESLGERTVQLDCDVLEADGGTRTAAITGSWVALVLATRGLLEGGVLDSMPVRGQVAAVSAGLVGDTPMLDLDYREDFAAGMDLNLVAAPRQRIVEIQATAEGDPLPRSVVDELVHLALDGISTLHQIQMDSLRGVDSGQQTHGGDS | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. ... |
A0A067XNA6 | GSVSLIIATICFLMQIAILATTVTLHFKQNDCRTPSNNQVVPCEPIIVERNITEIVYLNNTTIEKELCPKVVEYRDWSKPQCQIAGFAPFSKDNSIRLSAGGDIWVTREPYVSCSPDKCYQFALGQGTTLNNKHSNGTIHDRIPHRTL | PTM: N-glycosylated.
Function: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.
EC: 3.2.1.18
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, ... |
A0A7S4B0Q0 | RRGRRQMALRLPILLAAAAGAHALVATPYRCPGATRITTCTSLPSATATGRAPLTSLMMASMAVGTASAGFPAELMPVKTNALTRFLTATQFLAASVVTILFWYIPLVPLYLYSLVFDRSRRRACDWIVQIWARCTLSLLFSDIRVEGLENLPPRDEAVMYVPNHCSFLDIFALSGYLPRRFKYISKIEILRIPFIGWAMQFAKHIAIKRMDRASQVQTVRDAVDCLKAGSSLVTFPEGTRSKDGRLMEFKKGPFSMAAKAQVRVVPISIIGTHLFQPPGSAFPMARPRGVKLVVHPPLDAPGKKKEQETLEQARAAVLS... | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 334
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A644YTV6 | MDIKKIISKIDGAVEEYSMLAGCRGVLVGLSGGKDSVCLLHYLASQFSSGSCEINVYACHLNHMIRGAEADADENFCRDLCRSLGVDFISEKRDIPVIAEKTKKSIEEAARDARYDLFDRAAGISGCDRIATAHTASDNAETIIFRIARGTSVSGLCGIPPVRDNIIRPLIDLNSDEVIAYCNYFGLEFRTDSTNADISYPRNLIRAEIIPQLERINPSFANAARRLSRSASEQRKYIISQADKYNNECSKNRIPIELAQRLNAGTEKCILYELIVRAIAGETSVPVTTERFDALSALIAEPKPDKVIEITNGLSAYPDA... | Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 460
Sequence Mass (Da): 51016
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A0A923NFC8 | MQSVLVEGGGAVLRAFLATDLWQQLDIYQTTTVFGTGVAGNEQRAQVGAIIVGSETALTDTPSLTVRHTSMTHPQPLRVILDRRGRLQSESQFFDDRTLIYTMNEALLRDAGIAVDVLNQSVSEKLNPSFHHFFETGHPYVMLKVAQSADGYITKVVGQSTKITDASADVATLAEVDAMQQVPNSADLKDATMYVTLEPCAHIGKVGACADAIVAAGIGRVVVGQGDPNPLVHGQGISIHHHAGFLFPE | 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: 3.5.4.26
Sequence Length: 249
Sequence Mass (Da): 26648... |
C5R7T3 | MLRRPIVIANWKMNKLPSEVERYIAEVSPKLAAYPHVDAVLAGQDVLLNAMVTAAKGTSIEIGAENMYWQDKGAYTGETSPAALADLGISRVIIGHSERRNYFRETDEMVNLKTLAALRNGVSPIIAIDEAVQLESLNDHAHWIVNQVVESLKGVTREEMSRLMLAYEPTAAIGSGQAMGPEAAQKSLHVIRQTVADMFDQEVADHVRILYGGSVKPANAYELLKQPDIDGVLVGDAALDAATFIELISLAEQAKRNL | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 258
Sequence Mass (Da): 28146
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A0A261RZZ5 | MGRLKSEAKAPELVEYVMAPFLADMGQYFDAHLRIHKAHVVMLCEQRLVDAEEGGSILAALREMERAGPEGLALHHDTDLYMQMEAYVSRRAPKAGGKMHMGRSRNDLYACGARLLTRDRLAALIADLLDLQEAVLARAEEHAVTVMPGYTHLQHAEPITLGHFLLAFHDALARDLKRLAAAYDNANQNALGSSALAGSSFPLDRERTAALLGFDGLVENSYDAVAARDYVVEAMGALAVMASTVARVVDTLIIWCTSEFGMIDMPDSYGYTSSIMPQKRNPGYFLESVRCKSARITGDMSSALCTLKGTTFAQSRDTSF... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
EC: 4.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 497
Sequence Mass (Da): 54317
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A0A428MZI1 | MNIHVLNSYEKMSQYAAHMIEAQMQKKHDSVLGLATGGTPEGLYKELIRRFQEGRVDFKEAETFNLDEYIGLGQAHPQSYSYYMWSRFFSHVNIDRTRIYLPFSKSAEDTDALAEYDIQLQEVGGIDLQLLGIGQNGHIGFNEPGSFLRADTHYVDLSLETVEANARFFSTEEDVPKQAITMGMAPILQARSILLLASGKTKARAVKEMLQSAISPQHPASFLQLHSSVDLVLDAEAAMELPNRDFVHQ | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
EC: 3.5.99.6
Catalytic Activity: alpha-D-gl... |
A0A2N3KWK9 | MKAIIAGILAMASTVVASNILVEYPLPGVLADWLTFGAFTYPVAFLVTDLTNRARGAKAARMVVLSGFAIAVVLSLVFADTRIALASGTAFLVAQLMDVTVFDRLRQASWWKAPLVSSTVGSMLDTALFFSIAFAGTGLPWHTWALGDFSAKMIMAMTCLAPFRMLMSVIRPVGRNGGMAAQSANA | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell inner membrane
Sequence Length: 186
Sequence Mass (Da): 19740
Location Topology: Multi-pass membrane protein
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A0A7C1GVS3 | MILLADVGNSRQKWALGEGHALGALGQVVNDDPGALAALLAGCPRAGLRRTVIASVAGESVNSLIREALALARLPTAEFVATPARAAGILVGYDNPGQLGCDRFLAMVGARARYPGPLVVADCGTAVTLDAVDGDGRHLGGAILPGRRLMREALVHGTRGVRVEAIEVAEVFGHDTAAGVASGSLYGLAGAIDGITARMSAALAEAPALVITGGDATALEPLLKHRYHNHPDLVLEGLVKYADS | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A8H6XA20 | MPTPNSSPGTFSPATGSASQSSRDHTPGGQWAQERIYPGMQLNSIHGEFSFSCHEMGPPSNSPATGGGLKARDVSKYMQGFADTLLPGKIMFDSEIITVSRDKTDSTWAITTKNRDTGLLETRRFGKVVLRTGGTSQPMIPASLSSSAAKEADFESKVIHSAHFGANLPKILSAISPKEDAEERRPKSVVVIGGGKSAREQEPKYHNSPLRLEYSALWHMRTNDEGVSREDGFHALVNNGTIQVIAPAWMTGYAAGRSVLLSNGQTVEADMVILATGYASTWDGIFKKETAAELGLYRHRSAIQVDERTNYKTLVNPPAP... | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 472
Sequence Mass (Da): 52108
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A0A5Q4DFE3 | MDPTHLGGSSAPPTHPGRRGRTDVNPENRTRHPGFDREPPYSMEAEVSVLGGVLLDPDSILRIEDVVDETMFFREGHRVLYRSMRNLHEQRTAVDVVTLGDLLRTSGELDRVGGMEYLAELLDAVPTAANIQYHARIVRDKALLRRLVEASTRTIQDVYEPGERTVEEIVDEAEQRVFKVAESHDRGGFTWIKDLLWDTFENIEKLQKSDGTLTGVPTGFASLDRMTTGLQSGDLVIVAARPSMGKTSWVLNVAQSAAIEHKVPVAIFSLEMSKSQLVQRLLCAEARVDQQRLRGGRLTPSDYQRIATAGGKLNTAPIWI... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 497
Sequence Mass (Da): 54945
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A0A124S3J0 | MTRSQFFINISCLFWQYDAFDIGFITTDDFTNADILEATYPAVAKRLHGDWIKDPAIPIVTGFLGKGWRTCAVTTLGRGGSDLTATTIGKALGLREIQVWKDVDGVLTCDPNIYSGAEPVPYLTFDEAAELAYFGAQVLHPQSMRPAREGDIPVRVKNSYNPNAPGTLITKSRDMSKAVLTSIVLKRNVTMLDIVSTRMLGQFGFLAKVFSIFEDLGISVDVVATSEVSISLTLDPSKLWNRELIQQASELDHVVEELEKIAKVNLLQHRSIISLIGNVQRSSLVLEKAFRVLRMNSVNVQMISQGASKVNISLIVNDSE... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 345
Sequence Mass (Da): 38188
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A0A366IBX8 | MKDDKIEIVIDYHFKDQSILKNALTHSSFINDKSKLKNNERLEFLGDAVLELVVSHYLYENCNNRAEGEMTKLRAKIVCTDSLAMAASDFQLGNYIYMGKGEENTGGRTRKSILANTFEAIIGAIFIDGGLEEARKFILCKLKNNIDDSVKGKLVFDYKTKLQEHIQQKADNDIDYVVISEEGPEHDKIFNIQLLLNGKVIGSGAGSSKKEAEQHAAYNGLIFLGEVHEK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A3Q8WX14 | MMTFAYTIAGSESAGVAGLQVDLRTFHELGTYGLSTITCVVALHPDNDWNHSFTPMPADLIAEQIAAATAAFDLDTVKIGMLGTVPTIETVAEGLRSQPWKNIVVDPVLICKGQEPGQAFDTDAALRREVLSQATVTTPNHFEARTLAGMDSLETVDDLIEAAKRIADTGPKAVVVKGGIDLPGDEAIDVLWDGSEATIYRAPKVGEHRVNGAGCTLAAAITAELAKGTELKQAVQVAKDMVTAGIEHRIVAHPPYDTVWQGAYSH | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
A0A7D4BIZ8 | MIQIRRQLHQIPEAGFAERKTQQFILDFIAELPQEHLEVKTWRTGVLVKIRGLQPSRTIGWRTDMDGLPIEEETGYEFRSIHPGYMHACGHDFHMTIALGILVHFAYRPAKDHILIIFQPAEEGPGGALPMLHSEEFQAWKPDLLFGLHIGPDEPTGTIATRPGILFANTSELFINLTGVSGHASLPHRSRDMVIAASQLAMQLQTIISRNVDPLDSAIITLGKVTIGTKQNIIPGQARLEGTIRTLSMESMDNIKSRIRSLVAGIETGFECNAQIDWGANYCQVNNDTDLTEEFMEWARQDGTVDVVSCQEAMAGEDFG... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (acetylase route): step 3/3.
Function: Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
EC: 3.5.1.47
Catalytic Activity: H2O + N-acetyl-(2S,6S)-2,6-diaminoh... |
A0A4R5JPE9 | MNINNQVKYQQRGWVHYQNIKLEIETSGDYVQKVNFTSEVYYSTNPSPALEEVCQQLLEYLQGKRKEFSVKIALEGTPFQKKVWEAMQNIPYGRTCSYKDIAIAIGNPKAAIAVGQAAHKNPIAIIIPCHRVLATNGDLKGYAGSIEIKEWLLNLEKRNKDK | 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... |
A0A366IBW2 | MENASLVTANVKMIIFNMLNFLILFFIVKHFFYEKINGFIQKRSDDVSLEMKNAQALKAEAEGYKAEYSAKLAKAEERSKEIIEEAINTAKDRKSEIIEEANKEAMKIQERAKAEINLEKKKALEEVRGNIVDLTMYATEKVIKESLHKAKHEQLILDSIKKVGEVK | 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: 167
Sequence Mass (Da): 19179
Location Topology: Single-pass membrane protein
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A0A7D4BK87 | MAKQKMLAAEAIALLLERKGVEHVYGVPGAAILPFYDAVREKTKIKSFVVRHEQTGAFMADGYSRATGKVGVCAATSGPGGTNLLTGLYGAYMDSIPMLAFTGQVAVPLIGSMAFQEAPVTEMAKPVCKAVYLPTDPHKIPEIVHEAWETATTGRKGPVLIDLPVDVQKVEIEVDLDAFTSVPERLPEAKDEDIDEVLHLLKQAKKPVLLSGGGVNLANATQELKEMAEALQIPVVTALMGIDTFPNDHPLFAGRMGTMLNTPYGNKTILESDLIINLGGRFGDRSTGKTDVFKRDAKIVHVNLDKKEIGKSVKTEVGIV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
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: 576
Sequence Mass (Da): 63008
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A0A7C9A3W9 | SYWTALRVVFLLLKVVTFFVFFSRADENSENPAWEAIGYKVDSRESCKSPEGRPLEKGIVECKHASDSTLLQALKDKGLQVTEDLDPSVLKIKCDVVIVGSGCGGGVAAAMLAKYGHKVVVIEKGDYYFAEDYSSLEGPSVDQLYMSGGMLTTLDGKMLILAGSTVGGGSAVNWSASIKTPDDVLQEWSVVHKLPMFHSLDYKSAMDEVWKRIGVTEDCIEEGFQNQVLRRGCDNLGLKVQKVCRNSPEDHYCGSCGYGCRTGEKKGTDTTWLVDAVDNNAVILTGCKAEKFILKNEDNGMRRKRCMGVLAIPLGNNISK... | Function: Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
Catalytic Activity: a long-chain primary fatty alcohol + O2 = a long-chain fatty aldehyde + H2O2
EC: 1.1.3.20
Subcellular Location: Membrane
Sequence Length: 616
Sequence Mass (Da): 67216
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A0A118K2E5 | MNTEKLRRAVRESGEEDNMFYFDPRIIDWDEYFQHIHLPAIQPNIKKLFLLVRASDPNMALHRLQSEVINKDLFRVIKEKYGKNMHTFISQKIKVVAGDVSLENFGVMDFDLLNEMRRQVDVIVNSAATTKFDERYDLALAINTLGSKHVSDFVNECFNMKLLLHVSTGLNL | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 172
Sequence Mass (Da): 20004
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A0A0B9GGU1 | MLNFVRKLFDRVIGAGVSILTISLVMCVVWQVFSRFVLHSPSTSTDEIARFLLMWCGLTGSAYMVGQNQHLAIEMLGTRLTGIKKLVLNIIVQLFIAKFAMMVMIYGGIVQYNNISMTGQLTPSLGMPMSYIYIVVPISGLIILLYNMLNIADYVNEIAEEKRKQNLNLSEV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 172
Sequence Mass (Da): 19302
Location Topology: Multi-pass membrane protein
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A0A1E3QIJ6 | MSEFQRKLFKVETPGRGAESLASSTPDVAKEAYFQVNEVYEDPQTRIRFQTFYTPPSGNGPLYVFHHGAGSSAMSFALLARELRERWRDDSTPIECGVFAFDMRGHGLTHGGESLDYSLARLVADFSFVTKELFRRHFNDTAHPSTFLVGHSLGGAILTNAVSANRLAPLKVTGLVMLDIVEETAIRSLSVMPLYLKTRPKQFASLDMAIKWHLRTNLLHNFRSAQISVPAILSRDASEGYCWRTRLEDTEPYWSSWFQGLSSRFVAQTPSLAKLLILAGQDKLDKELMIGQMQGKYQLVVFQDSGHFIQEDCVSKTAIT... | Function: Demethylates proteins that have been reversibly carboxymethylated.
EC: 3.1.1.-
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine methyl ester + H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) + methanol
Sequence Length: 351
Sequence Mass (Da): 39437
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A0A411JM87 | DYALPAYFDRRENPLPDVQFVTELSAAQKSLKEKEKGSWATLSNEEKIALYRISFKQSFAEMNEGTKEWKSVIAGMFFFIGMTGLVVLWQSKFVYGPV | 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.
Subcellular Location: Membrane
Sequence Length: 98
Sequence Mass (Da): 11237
Location Topology: Single-pass membra... |
A0A1D1YZZ6 | MAESGGGGWADRGMSSDNIKGLVLALSSSFFIGASFIVKKKGLKKAGAAGVRAGVGGYSYLYEPLWWVGMITMIVGEIANFAAYAFAPAILVTPLGALSIIISAALAHIILRERLHVFGILGCVLCVVGSTTIV | 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: 134
Sequence Mass (Da): 13861
Location Topology: Multi-pass membrane protein
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A0A645GWS4 | MRGKDIEGYINPIGSGPARAVAKNDIFSQCWTYQDTHHEVVFGAQTQELPNEQDAQEIADACRVSPENVYILAARTGSLTGSIQICSRTVEASIWRMERKGFNISKVISGTGTCPIAPPIFDECRAMDRVNTALLYGVTVRYLVNSTDKEIEDIIDLLPFSASRRFGESFYDLFEEGKHDFYIVDKDVHTVARYEITNLASGKTFRAGVLREDLMKDSFFK | Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
EC: 3.5.4.27
Subcellular Location: Cytoplasm
Sequence Length: 221
Sequence Mass (Da): 24837
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A0A645HX29 | MTNIKPFVDEAYQNLTTEQFRDLMLLSIFDVETREEVKEYHLTDEDWKRVYEIREEYFGNWDWNYGKSPKFEIQKHHRFPIGSIEVRLNVEEGHIQQLKIFGDFFGLGEIKDVEDAFIGVKYAKEDILAKLKELDIKKYFGNVTAEELLEELY | 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: 153
Sequence ... |
A0A0C9U3D3 | MSPHPPSWQRAWDAAQPHLESIRKLLPGFPHISLRNLRVSQLDAELLDQELLQILSEPISKALGLVQSSYKSRYEPELNLILGILLYKFSVWNTGATYGAMLQNLRYKTPSKAAFVARTPSGLPRKTLLLNAAITIAIPYLHARLRLYALSRSWPDAPSSDYRRKAWTWLTGTETVHNSLGLISFVAFLWDGRYRSWTDRVLGLRLVPSTHISTRQVSYEFMNRQMVWHAFTEFLIFLLPLINTRKLTRRVTRAISGVSLTSIVPSFAKNALGIQRTLDSKEVTERRGKYWSLPADQCAICAENASTILSEPGYDVYSLP... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 418
Sequence Mass (Da): 47324
Location Topology: Multi-pass membrane protein
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A0A316V190 | MNETTVGSSGHNPLTSTSSAVPLPRILIIDHFDSYTLNLLTLLAALCNDSSSVSDRVVVLPHTHHLLASQDAFCQHLLPHFDALILSPGPGSPDRKADFGFGLEYLRNAAKYRLPTLGVCLGHQGMATAFGGVVRRAKSIQHGTQSSLQYSKGDVPQAGIFANVPPGTRVTRYNSLTVDPSTLPECLEMTAYADDPRNDCVEAPPQVSELMRSRATSPTTTMESERCVLGLQHKTLPLWGVQFHPESIESREGVRMMHNFIEMARKWQKEGNETACGSSLKIPPSILAEGARYVAAARPSPTCGATLPKKLWKVVEVDFG... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
EC: 2.6.1.85
Catalytic Activity: chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
Sequence Length: 907
Sequence Mass (Da): 98869
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A0A2S9FDY7 | MNATPFGHYQLRKLIGRGGMGEVYEAYDTKTDRVVALKVLPHHMAQDETFQARFRRESQAAAGINDPHVVPIHGYGEIDGRLYLDMRLIEGRNLGTMLEETEKPLGAAFAVMVVTQVANGLDGAHRLGLIHRDIKPSNILITGRDFVYLIDFGLARTAGEKGLTTAGSTLGTLAYMAPERFEGSEVDARSDIYALTCVLYECLTGRRPYPADSLEQQIAGHMVSPVPRPS | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 230
Sequence Mass (Da): 25273
Location Topology: Single-pass membrane protein
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A0A2J6IGT8 | MKKTDFLMTKIIATLGPATDSLEKILELIKAGVRVFRINFSHGSFNDYDKLIDNIRNAEEKSGQFVGILGDLSGPKIRVGKVIPEGVTLKNGQELKFVKKEIIGGSFGFEHSFSTTYPQFIDEVKEGERILLDDGNIQLKCIAKKGLGGDALLLCEVVEGNLLTTAKGINLPDSELSLPSLTEKDYECLEYAIKKSVDYLALSFVRRGEDIRHLKEKMKQANARPKGLGITSGDMGFSTSFEDNYIPIISKIEKPQAIDNLEEILEESDGIMVARGDLGVEMDLAEVALLQKKIINMCRHNMKPVIVATQMLQSMIDNPV... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 329
Sequence Mass (Da): 36380
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A0A0C9V1C4 | MNLLKKSTKDDDLELNATFFDKHVEIFVQLARLPFFLRVLAECLVIMAVAFPTSLVAQQAPLTRMAFVGFGGGLRIVCFRTLGKFFTFKITIRPEYKIMDIGPYGVVRHPAYTGSLFLLSVQ | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 122
Sequence Mass (Da): 13778
Location To... |
A0A103T1W2 | MEKCVTPTNSKAEDVEYKLFPESLNAKAEDPFPESLNAIPPRIASGSIPGVSADMYMKDNRQWKKRVNAYKRIHRIIASGRYPNIMDMNAGFGGFAAALDSPKLWTSSTTFPVPHLVSHTTAMAILILEILEPSRSESVGSSIESPAKIDVTSPRVPCTSCRTSTWLKVKKTEAESMLATTSKTTGCGVRRQLAGE | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 196
Sequence Mass (Da): 21406
Location Topology: Single-pass type II membrane protein
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A0A8H6X3U4 | MMILDQFYAENFGKVYRSCGNCGTQFKRIVQINDLWAVNGDVVAGINTNFGDTATIRTTQVDGVDDICVKYTGNSNGAEPVEIGSGPDTKNCLYSTSDIKQL | Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors ... |
A0A0F3IV64 | MFELSKQFYFEAAHTLERSIETESSRRIHGHTYHAEITVRGAPDPATGMILDLGLFTRALDSVRAELDHRFLDDVPGLGPATLENLCVYLWKNLAPSLPGLNRVSVWRQASGDKCTYFGPEEA | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H... |
A0A316V0A4 | MADAPPAAPIADAAPQAAAAQPAAAAATNTTNTTANRGQRPEGPPSGAANIMCKWWAQGFCARGEECWFKHGVVADPPPQEPVALTAPRARRLTASARVFQPAAASAASAASAATADTTDAPTNDTIPSPPISPDAILEPTKEQPQCHICLHDTPATYGLLEGCSHAYCLSCIRQWRDTRVPPSEDDDDFSEGNNRKTCPLCRKQSLYIIPSSVFHSAGPAKDVATARFKDVVAKKPCKHFEATKGTARGPWCRYGDECFYAHVLKEGEGRYEFGGGFKYMLKRGEKDRKAREQRQWRAHVGDMVRRNRLERAMRARRGA... | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 704
Sequence Mass (Da): 77143
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A0A644Y1R6 | MGYYDQHMHTHFSPDSAESFENYLEETDGILVTTEHLDFHDAYNGGVDTVLDYAAYSEKIDTLNAVHDGRIRRGIEVGYTPESHTQIESYLEGKAFDVILLSVHQNGLYDYLQPIIDEMDPKAVMKEYFELCTEAVRQVDGANVFAHFDYGIRRLPVTADDLREFEPELKELLKEILAKEMALELNTRSMYEYKNADLYRYMIGLYLEMGGTRFSLGSDAHSIKKYRYHFNDAIALLREFGVTGLTQFKDRIAYTEPI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 258
Sequence Mass (Da): 29807
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A0A7C8Z5E9 | NAEAGRCRRTDGKKWRCHHAVVPNEKYCERHMHRGSKRSRKLVEGSTQASMNPGALNLLPSNEHKIFTENLNQKPLLPDHESPMSNHSSVGASSEAKNCPARVMIRVPSLTSSAKFNEDNEQKNAGKRNSIMKDRIAAISLSSGLDFSPKSVLKSDQKCPQIENLENDPNAEAGRCRRTDGKKWRCYKSVLPDQKYCAHHINRGTKRPVALSAFGDAGSDVKFFGPEEAKMSRHANTSLNASLTISSGDSRYNTARHSMAHNCESSSTSETTITDDSADILDKIVLSP | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 288
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 31775
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A0A7C8Z5C3 | MDDDSTVARMIFSKIPLDEPYIQTRLCVLANQQAKSLREGKLPIDESFYLMGTADPTGALNEGEVCIIHENGQISGKVLVYRNPGIHFGDIRVLTAIHIEGLEDIIGCSKYGILFPTKGPRSSTDMMAGGDLDGDMYWVSRHPILLKYFKQSHPWTCMNHYSSKSSEKKPIELSDEELERELFSHFLTARFRRSKAMGTASNSWLAHMDQMLTNEHTKERNCLKEKLLELVDIYYEALDAPKTGGEVRVPRELIPDTYPHFMEMTKSPSYESKSVLGEIYDQAQEFNLNTPAIPVWKLPPLDVEVPYRNLKTWQRHYEAY... | Function: Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs).
EC: 2.7.7.48
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 448
Sequence Mass (Da): 51169
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A0A1D1YEM6 | KYKQVLSRNAPRLREAPQPTGPMSERPGATGAGLLGAVPRWNAGGMAGALLGYAACRQLSQLLAAVVFFHGSEYALAVAFHGRSNVPMSSLLISKHYILAMASALLEYIIEIMMFPELKEQWWVSNTGLVMVLIGEVIRKAAVLTAGHAFTHNIKIYHEEQHQLVTHGIYRFIRHPGYCGFFIWATGTQVMLCNPICIVTFTVVTWRFFSTRIPYPPKKT | Cofactor: Divalent metal cations. Probably Zn(2+).
Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequenc... |
A0A1Q5XR25 | MPFRDEDRMQELKQATPARIGTGRAGTRPTTRELLKLRYDHAAAVDSVYGSVSTNLLAELGLFMVDSGAVDQELYLRRPDLGRLLPDHSIQQLTQRCIPSPQVQLVVSDGLSAGAIEHNAGDLIPALLDSLQVQGLKAGTPFFVRNGRVGIMNAIGDILHPETIVLLIGERPGLITSHSMSAYLCYRPHAGMTDSDRMVISNIHQGGTPPVEAGAHIGSLIASMLKQKKSGVGLVQ | Cofactor: Binds between the large and small subunits.
Pathway: Amine and polyamine degradation; ethanolamine degradation.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of exte... |
A0A2J6I9L5 | MNRIYLIGFMGVGKSTIGKKLANKLNYNFVDIDELFENKYKVSINAFFEKYGEKLFRELENKLLYDTFSYEKTIISTGGGTPCYRDAIDDINSYGTSIYLRMPTEALINRLENAIRPRPLIKGKSHDEIKSDVEKLLAEREQYYNKANIIFDAISPDVDKLLLTVESHMDKI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A7C9FAP6 | MTSRDLEKDRGMNSNYSNYATSSGGGYPIETSDRQWTSWLVPMIVVANVVMFILTMFVNDCPKNNFSGESCVAKFLGRLAFQPLRENPLLGPSSDALVKMGALKWDNVVHEHQAWRLITCIWLHAGVIHLLANMLSLVF | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 139
Sequence Mass (Da): 15604
Location Topology: Multi-pass membrane protein
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A0A482PXI3 | MTREELMPIRDRMMAAIMQEPFVQGIRNGKISQTSRDYYVAQDHYYVDVFMRLLDQTNAQLPLELRRKEMTASNESDAHLGLEPSEQYQQIAVGEHNTSYLNHLRATVAQGDPLASMLALLPCTESYGLIAQGLQQQGVASNGFNVWVDYYTNQAYQSAIDWSWRTVDQLFAQKQSAPADYASIYETSYQHELAFWQAANQ | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.99.2
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Length: 201
Sequence Mass (Da): 22987
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A0A6P7GSY2 | SLLLFQVRQKVQSKDYSVNKTKKVAWFVSNCGARNGRLAYARELGKYIPVDIYGTCGPLKCPRSDRKCFEILERDYKFYLAFENSNCRDYITEKFYVNGLGQNVLPIVMGARPEDYQRSAPEGSYIHVDEFAGPQELAAYLHRLDNDNNLYNSYFKWKGTGEFINTYFWCRLCAMMHAPQSTQRHYEDVNDWWRGPGVCTTKSWRNAEFV | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 210
Sequence Mass (Da): 24558
Location Topology: Single-pass type II membrane protein
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A0A7C9A9G9 | MSGGIVNYEGRFEIISLSGSFLFSENNGQVRSGGLSVSLAGSDGRVLGGGVAGMLTAATSVQIIVGSFIADGKKPKYMPSVPQSHMLGFSAPPLQASGSPPLEEESSEASEENGNNNHMDRGMGSYGNSNHPIHNMQMYHPMGWPNSTSKMLQN | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 154
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 16191
|
A0A7C9E197 | LPISAPGATTSTSLTWGGGDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKM | Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectro... |
A0A6P0JVK2 | IPLTRVGEPMSLSDLENQGAELARFLQVPLEGL | Function: Seems to be required for the assembly of the photosystem I complex.
Subcellular Location: Membrane
Sequence Length: 33
Sequence Mass (Da): 3594
Location Topology: Multi-pass membrane protein
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A0A6P7F5I5 | MSLYLRDFDINYIYDLLKFTELLAVTPPLNRKKQELTNYKYYHIIVILLIIIFAVYSSYGIIVYFIPKFNGTSTTLRLICIIVITIMNVLSVLIAACNVDTWNMFLNVFKHLDQKLKYQSRSENNILKLELSTFYLVLLSIFGYDAYVWYCNYHWDLFKFTLFKYVNFIHGNVMMLVILHFAAALSNRYKRINNLLIKSNDFYNIFNCLIVKGSEEKLNNLKSIKEVTDYYLLLSDLVEMFNKLFGWQILIVTEYVLLFFLEFFNGLMLSLDPAQKSGVYHDLKTVISLVIFSFLAIGHQAMIILFCENVNKESRNTLTI... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 408
Sequence Mass (Da): 47939
Location Topology: Multi-pass membrane protein
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A0A1E3QPM9 | MTESSTAAFQPEIWTASSNTALKVSLADTEGHGAVTFAPQFTYPIFGDAETVFGYKNLAINLVFDSWTMKPFLNVKYDEKLADHEEKELYDKLLAFLPEEVMLRDEGAWVDACTRERATFEIPGTKIASFTSRDSAFSVYRASFRDLNTLELHRRLQIFVLLFIEAGSYIDETDDLWELFLVYEDCDKPRLAGFATAYSYFKYEGAARHDVRDVAALSVRKKISQFIVLPPYQSRRVGAKLYDTLMERWLADPLVAEVTVEDPSEAFDDLRDRCDLTRLARTLLADVRAADVDADWLRARQRAEKLDARQFHRLTEMALV... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subc... |
A0A1D1ZI78 | HLLFFSFHGGEGKSLGFLAPFLCSTQTGFLSVWRYSRRSWASDRFGRFGAPASPSLRRRNRRGPTMTGRSAPLMRGGGQSPPWSRGSRIAMAVGIGVLVGCVFAFLYPDGFFPAEPTPAQGRINLVSSKVSSSPCESPERINMLKSELAATSEKNAELKKQVRDLNMKLQLAEQGKDQAEKQVIVLGGNYKAGPFGTVKSLRTNPPVTPDESVNPRLGKLLEAVAVRKELIVALANSNVKALLEVWFQNIKRVGIRNYLVVALDDAIEQLCKMNDVPVYRRSPDEGIDSVARTGSNHAVSGLKFRILREFLQLGYSVLLS... | EC: 2.4.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 499
Sequence Mass (Da): 56084
Location Topology: Single-pass type II membrane protein
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A0A7Y4RJ00 | MSNDAGALVYIFAIAAVGALVLVLALAGVSVISQRKIVNMHRAHAQKLLQAQEDERAWVAREVHDDAVQRVAFITQQYDAIRVAIPELAASHGGELDAVAQDVKDLGVFLRSVAHRLHPSALDHGGLEVAVRSLAGEITRNSSVAVEVAASPIGNALAPASALALYRIAQEALRNVVNHSGAARAKIELSRSPTAVTLVVSDEGKGFESRTRRASDGIGLVGMQERATLAGGTVSVTSRPGQGTRVEATLPATPAPTQ | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A258X7M0 | MKKHLLILGASGQLGSALSNTSLWPKDYKITALTHAQLDIRDSTALQCLFKEKGPFQAVINASVFMPVDLCEKFPELGFQTNGFSLLPLATLCKMHETLLVHFSTDYVFDGLKKTPYTQLNSNYGFNW | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Seque... |
A0A524HLX2 | GEIDRYNIRVATALAMRRAIDRTLWRLGDPAPRHRVLLDGLPLPECGHTHDALVDGDALCYSIAAAGIVAKEVRDRLMRQLAPRYPDYGWESNAGYGTDWHRRAILVRGPTPHHRRSFSPVSQMDLNLA | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 129
Sequence Mass (Da): 14536
|
A0A1D1XKP3 | MDTAGVSRRQPPPPPSSSPSPSGIEGNQEYFTYGAPGGGGGGWGWSLKAWGAPSPLSAGTGESRAFKSVLVVFACLSFLLTLIFVSRDYRAPLTFVSGFYGGSTSQLQHPHQQLLADGPTMLQTSTTNTTTLVVQLSNTVAPSPSPTSSERLSHATPLHQVATVAPSPAPVGIISSYAKLHNASIDQVGTPPPTSQPDAHDVAPSPSPTSREKPSHAMPLHKVAAAAPSPAPAASISSDAKLHNAFVAVGTPAPTSHPDAHDDMLLGGLLPVSFDGASCQSRYQSFAYRKASPHKPSPYLLQRLREYEALHKRCGPLTRF... | Function: May be involved in cell wall biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 544
Sequence Mass (Da): 59442
Location Topology: Single-pass type II membrane protein
|
F8F2C4 | MRIMQAPFNCLTPDLITDSIEEAFGISLENLIYPYPSYINRVYGLQDTDDKEYVAKFYRPGRWSQQQIREEHQFLQDLYLGECPVVLPIPDQEGATLQTLNLETYNPNSDQIDELIFHFALFPKQTGRAFDPETDEDWIRLGSLAGRIHVSGRKSPKLSRYRLDAFRLKYYIDELLKAGLIPEESLSDFLFITTKAFELLKNHNESIQSMCLHGDFHRGNLIYNSETGLSIIDFDDMCEGPAVQDLWLLLPGHHRDSRRELELILEGYTEFMEFNQEELKLIEDLRFFRMIHFLHWQSQQRFDRAFYQHFPDWGNHAFWI... | Function: A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.... |
A0A1V1THF2 | MFKASIQRQVRLGNVARQFSTVSLMRNSRSEHLAILRQTPSQPALRRLAPRYAFSHLYSTQSASAQANREGEFAPVASAPVTRFSELSQLGVNSRLIQALTRGMGYDAMTEVQAMAINPALKGSDMVAQAKTGTGKTLAFLVPVFQRVLMDQPDLADVRNRRRSSSEDIRAIILSPTRELAEQIGVEARKLAKNTGIVVQTAVGGTRKREALQKMWREGCDVLVATPGRLNDLLTDPGARVAAPKLQAFVLDEADRMLDVGFSDEIREIQNSLPSKHEVERQTLLFSATIPRDVVHLAKSMVRPENFQFVQTIKEDDVAT... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 688
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 75970
|
F0WFY7 | MPYQTLPGIIIMIGAITTMGVGLGWVTRSQARSNGQSKLQLLTEWDRMMDARDRKLWEREEENRNS | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A316USP0 | MRSSRRNGINTNTTSKGPATSSTSTRHAPLSPSQPLLNHLIANVRSLPKCSLPTGSGHLTLSVLFSPPRMAKVLYPWAHLDDPRGIAAGSRPFPQQTVQTWEEMVFFHAEWRRADQHEDDVKMICAIEAYNYSLPEYGSQVFYLSKLDTTGWAPRLQSAKVQKHLLLDGGKGPSPSSGSAGPVTSLTTHLTVSFLSYFLSLRHKPSLPTPSRPLRHSSCHILARAQEAYIFPNSPENPAKKPLSDAKLVVWWRQTLSQVVEAVRVYHAGVKEGSKGEGKSNGGLPQQPRIDACYMIPGLEKLESHPLVPLPPSMLGKSES... | Catalytic Activity: acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 796
Sequence Mass (Da): 86990
|
A0A081BP79 | MNRRLRSLRRMMLHVTLIPATTVVVIWLCVIAFSIYLLRNTIIRQHNLLIEAVARQCEQYLTETGNMLSATASGIRELPSEYQSRFLTQIQANYPRFSTLYLLSSEGTVIAEADSRISLLGLNFARERFFEPTKQSRMLYFSTPFISLFTNNIAVTGVVPIMNLNRLQAMLVGELDLRVLQEVIETADIGEQGTAFIADPRGTLVAYPITAWVHEQRNIGNLLLFENANQGQAVFEFFRDPESNAWLVGSAKQIAWNWVVITTQPLAVVVRPLILLIVISAIAFGGSVSLFVWAQVTIVRQITRPISRLMQEADLLAQGQ... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 612
Sequence Mass (Da): 68909
Location Topology: Multi-pass membrane protein
|
A0A103SI29 | MGTGIDSELVIVRQLLLSYESGKINLQKCGKQEEIGHRSMLSTEWMIGIHRFFNSLGDLVPFTNKISVQGSYLTTEDAYLSVIGGTRIFAGAYGQVKLQQLVFPFKLFYTFYLQGLAADLPAELLVTLWLRHRRWRRRLPQGHREGGHLS | Catalytic Activity: (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (9S,13S,15Z)-12-oxophyto-10-15-dienoate
EC: 5.3.99.6
Subcellular Location: Plastid
Sequence Length: 150
Sequence Mass (Da): 17100
|
A0A7C9EMZ3 | HSSTCMPFTYEELAKATDDFSESNLLGQGGFGPVHKGLLLDGKLVAVKQLNSKSIQGGLEFESQIEIISHAHHKHVASLVGVCIDGDKRLLVYEYMDNKSLVFYLHGSEVPTMDWATRMRIAIGAANGLAYLHDDCEPRIIHGNIKPTNILLDSNFKRS | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 159
Sequence Mass (Da): 17566
Location Topology: Single-pass membrane protein
|
A0A7S4B6K6 | PAQCLCCARPPVRTPPGGRNATRPIERSHPRAIPHRSVIKHRLQGCTYLAFLAVLAMAGLVVRKAKCSLVSAGCNNMCASRIGSEVSIGSASWGRTARRKLTHLSGQCTHTCPTTKPHSGTRALSSATQLKEENERLRAELDRLRATVRAAPPRHESAEQPQRSFFAGARSEFTCELKFWYPDEGIPPSIPCFRLIDDLGVPVAGSEAALPTIERDDAEQIQAVMVRLSEFDKVFNEAQRQGRISFYMTSRGEEACSVGSAAALSSADWLLPQYRELGAAMWRGFSFSDVANQLASNSLDPAQGRQLPLHIGSKEKRFMY... | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2... |
A0A7C9ADL2 | KLGELEAELTEMNSNNEKMQQAYNELVEYKLVLEKGGEFFHSAQRSAAAQQIESDSQHAEESLDTPLLLDQDKLADPSKPVQLGFLTGLVPRDKSMAFERILFRATRGNVFVRQASVENPVIDP | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 124
Sequence Mass (Da): 13906
Location Topology: Multi-pass memb... |
A0A7V8X9P9 | RLKKLSAEAQEARDQAAALLEDHRAMLASATGEASAIIAEARQAAERERAMGIEKTRAEQDEMLARARREIEAEKIRAVADVRREAVDIAIAAASKVVGQRLDAASDRQLVEDYIASIGKAS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A1H9W8J6 | MDVLHKIDTLILRIQATIMVVANLFVLFGVSAIAFQRYVFSGSLHGLDELIVIAAFWMYFIGAAYATRYRRNISADIISVYLRGRLLGDLVQLLSTAISLGLSCLFTYWGWELFSWSMAEQGATPVFSIPNVVLHTSIFIGFIFMTVYFAVELIGKIAEYWQTGHIEPAILKEQAPSSSRTIEEGR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 186
Sequence Mass (Da): 20910
Location Topology: Multi-pass membrane protein
|
A0A0B1RDG8 | MSLPDFQGKDSDIRALTVRTGAILRTLRDSLQQLGLDKTIAEVAGSIPDARDRLGYVVKLTRGAADGVLNSVEMAQPVQTQLAEDAEKLTLRWNAWAVSAQDDNSSRELAAATQTWLANIPDVTNDTRQQLHAIMMAQGFQDLTGQIVQRMVSVLNDVEQQLIQVLRDNSPGHASTGNSSSATSPTVTDKASSQNDVDDLLASLGL | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
EC: 3.1.3.-
Subcellular Location: Cytoplasm
Sequence Length: 206
Sequence Mass (Da): 22184
|
A0A7C8Z0E8 | PAGQMTIFYGGQVMVFNDLTADKAKEVMDLASSFESSLKKTKVEAPANPKPSPNTNTNPNPNPTRNLNPAVTQNLNVATSFGSPVSPSSTLPHPPVANASDLPIARKASLHRFLEKRKDRLVGKAPDVLNAGPSKPVEGKSWLGLASLPVYQA | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 153
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 16240
|
A0A4R1B7U8 | MQKLPEQFAAAVQLHRSGKIGAAIDLYLKILPRQKNNAQLLYLLGTAYLQAGRLSEGIAEVRRSLAIAPDNPDALNNLGNALKGLGRPDEALATYDRALALRPDYGDAHFNRANVLQDLGRHAEALAAYEQALALRPDHAEAHNNRANALKDLGRPDEALAGYDRALAARRNYAEAYNNRGVVLKDLKRHAEALADYERALALRPDYPEAHYNRGNALAELKRHEEALASYERALAGRPDYADAHHNRGNVLKDLKRYAEASASYERALALRPDYPFLRGKALQARMQQCVWRGLEADLQALAAGISAGRPVTPPFELLG... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.255
Catalytic Activity: L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP
Sequence Length: 734
Sequence Mass (Da): 80975
|
A0A260ZP50 | MEFTEVIEVLDRGSSIDVQSKHTFESLMIGQKTLERLKAAQFDRPSPVQAKAIPVGLLGRDMLVQAKSGTGKTLVFSVLAVENLDLRASYVQKIVITPTREIATQIKETMRKVAPPGARTSVYVGGCGHKLNMIDLKKTRPQIVIGTPGRIAQLLKLGAMDLSHVDFFVLDEADKLMDDVFRDDINIIINSLPPIRQVAVFSATYPRNLDXLLSTFLRDAALVRFNADDVQLIGIKQYVVTKCSPMLEKLTHVLKSIRYVQALVFCDQIAKCEPIASHLKSEGLDVTFVSSAMSQXDRQLAVDQLRAKRVKILVSSDLTA... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 700
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 78876
|
W3WQD3 | MKAAPIISCLASLANAAVVSLDKRAYSSSPLVVEIEHVGNSEVKASITNTGATSLKVLKAGSILDESPVEKSKVSQGDSKVAFTGLRLYVHTEDLSDSAFQTIAAGETVEVQWDAAQVHDLSTGGDFNITAAGSLRYAEADSNKIAGQVLYNSNVVQAAVDGVKAAKVHTAFRAATKNKRVTVQSDCSSSKQSTVDAAISVAKTYATNAAAAATAGTNMEEYFKSTSSSTESAVAEVFDTIASSVFNSDSSGVALYCTDIGNACSDGVVAYTQPGSDEYIVVCDYWFQFPATGSTCHVADQPYVLIHESTHLTEVKGTDD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine.
EC: 3.4.24.39
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-As... |
W3XB50 | MTALPHAVDAETPLKPSELQVLRNQYEKEGDMVGVQTKFNYAWGLVKSNSRNDQQTGVRLLSEIFRVSPERRRECLYYLALGNYKLGNYADARRYNDLLLDKEPMNMQAADLRRLIDDKVAKEGLMGVAIISGVAIAAGVVGGILFRGRRR | Function: Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation.
Subcellular Location: Membrane
Sequence Length: 151
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Sequence Mass (Da): 16987
Loc... |
A0A261AGW1 | MEIEVDVYNEDVDDFYIEVVQQPSGLKLPKADSHCDRKSRKMERIAGSISSEKVDAIEVGTSVILATSDRTLTHPTVDKAVKNGIAEATFLGDISIEALVEGMLVPSAADGRFAMLGTSVMWNALKSNIRDLKSSISEQTTQSFLEPRFDGIDLQLANVPNYERSYRIQAVGVFSNADLGYVYSLLKFRTSAKLLNKTKQFLKAYFIVACRPRCMIWRYTLRRSGNSHKKAILNLPQEIIQTVLTFLIDLTGIGDGSKPLESLNRSTPFYHSLGEDEAVRQQRYYEACKLKDLLMSFFRETITDCLNEIREMPFCLNTGT... | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Sub... |
A0A6P7GAE2 | MFDARESTEGKIVTLDRGDYTTCTVNLQGGTVVSWRINNEEQLFLGRRSSFSKFANIRGGVRLVWPHYHLWSFGRRHGFGRDMLWRVMKGPELLLNGDIFLDVCVTSNQYTKSMWNFDFEMHNRITLHSSQLTMAYTVINKSPYFDFDFHINLQTYVKVSDISTMRIVGLENFPYDDQVITDGTSMFIEKEKEIRVQGEFDRIYQEVPKLVNIYMDKNKQLSISLQNLPDLGFFNPGPEKAKKMDDLDDDEWKYFLVVQPAHVVSTIKLERGTSWNMSVTLEVRRTDEKEIQYKNFYDYFDKYC | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.15
Catalytic Activity: alpha-D-galactose = beta-D-galactose
Sequence Length: 304
Sequence Mass (Da): 35824
|
C5RC35 | MKSLNEEQSQAVMDFVAWGVAMHAYSEAETVYRTNLVLAKLGATSLVQGLTGHTDTNLSDLADQLIAVQDTDFEMGWQAAIDRTELLNIVTPTPDVLAAEFERLYKVDPEQAVKYYYFISESVENVKVNDIARNIAFTHNSKYGDIEITINLSKPEKTTAEIKAAASAPKSTYPPTALDYTNEGYLGTVTAAPRLTHRFIRENFSNETWGWHYSPYAYFEEHAIFVNFKRQPMQMGLRTFTRLMQIVTRYPMYMVGSNADLPIVGGSILSQEHYQAGRHAFPMMKADVKQKVALSEYENVEVAVLNWPMTAFRVSSTDAA... | Pathway: Carbohydrate metabolism; galactose metabolism.
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
EC: 2.7.7.12
Subcellular Location: Cytoplasm
Sequence Length: 501
Sequence Mass (Da): 56447
|
A0A0S6VQ29 | MGSLTPQVMADSLKQVGGVVVAIIALTILLELVLYFIFEKTLKYKYALPIMLLSPAVIGLTLLFIYPILYEFRLAFSNMSLDNFKRSYNITDTVIAKFQEAGMSADAIMEMKGLTDQVFTSEDDMLQELTAALGADVVQQHKDAFLQNADRKDGVLRITKRTLFTLKKSLPEEIVTKLQENKGMLNSIYTSERQFLRDAEQALGNETFAKYKDVLLQQSLANAGPSFGWQQGLQNFREIFTSPVLKQIHFMPLFLRTILWTAIQVFFHTTLGLGLAMLMNNNIKFKGIYRTLIIIPWAVPQIIAVLAWRGEFHSQYGFIN... | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 484
Sequence Mass (Da): 54861
Location Topology: Multi-pass membrane protein
|
A0A103XXB0 | MDIRFPYSPAEVAKVRLVQFGILSPDEIRQMSVVHIEHGETTERGKPKVAGLSDPRLGTIDRKMKCETCMANMAECPGHFGHLELAKPMFHIGFMKTVLSIMRCVCFNCSKILADEEDHKFKQAQKIRNPKNRLKKILDACKSKSKCEGGDEIDSQNQDTDEPVKKSRGGCGAQQPKITIEGMKMVAEYKLQKKKSDDSEQLPEPAERKQQLSAERVLSVLKRISDEDCMLLGLNPKYARPDWMILQVLPIPPPPVRPSECLSTMFNKQKAKPCKRLVNPNSLPNTLLDFISLVIFYSFLKQDDLTHQLAMIIRHNENLR... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 649
Sequence Mass (Da): 73768
|
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