ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A118JYM2 | ITCKHTTHKINNPPFLRGCIKRSSSDHPPDFHYFPSQHRSIMATKGNPGDNRTRRSFSVFIVFGLCCFFYLLGAWQRSGFGKGDSIAHEITKNADCSVISNLNIETHHGVGVKNPDDLRSESKVFQPCDDRFIDYTPCHDQSRAMSFPRENMEHRERHCPSDNEKQHCLIPAPKGYVTPFTWPKSRDYVPFANAPYKSLTVEKATQNWIQYEGNVFRFPGGGTQFPRGVDAYIEQMASVVPIGNGIVRTALDTGCGKNVITMSIAPRDSHEAQVQFALERGVPAIIDVLGTIKLPFPSRSFDMAHCSQCLIPWTQNDGKY... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 490
Sequence Mass (Da): 56427
Location Topology: Single-pass type II membrane protein
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A0A0C9VJR9 | MAYFQPAPSPPRAPARKNKFNPHHDIDEFLSSDLELSFASTMSLNSPPDRAPSPMAMDISPAFTMTSQSGHLAPPAPRLFGRDLVNESRSFGSTKSNDTKSKNKARQRSALPSQWISTAQSSPRDDSIEGISHVPITLTVPSSGDAMDVDVQMDCSSPHLPAPVNTMFPSSPSPLPVVSNTNYGNLFFDASSPAAPKSPLGHKKRRSTSPSPKHKQLLHFSPSSPSSPSDHKFTRAATVNIGGSLFKKPTVEKKPSFEYNAPSVKRVPGRRPTISAFIGPNGYSQQPQSAYPIIATSKEEPMSAAMPAPRRAFSAMIAHG... | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 708
Sequence Mass (Da): 76549
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A0A644SUE9 | MKTHILGFPSIGRQRELKQALESFWNGSRSAQSLIEVAANLKKRHWRIQRDAGLAYVTTGDFSLYDRMLDITCMLGTVPARFAAGKGDSPLERYFSLARGDALRNLAPMEMTKWFDTNYHYLVPEIEGDTPWQPGEHPVLADTALARDLGFAPKPALIGPFTWLTLAKSRHEAHKWSRLESIALVYADLLASLAPLCDSIQIEEPVLSTELLPPAAVRRFTEIYAGLNSASGNRLMLTAYFGPLEKNLALALDSGCAALHVDMVRGRDELGKILAAIPDNMALSLGAVNGRNIWKTDFARILPCIAQATAALGSERVLVG... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
EC: 2.1.1.14
Sequence Length: 577
Sequence Mass (D... |
A0A7C9EFL7 | HDWCEPFSTYPRTYDLLHANYLLSHYKDRVSYCLLEDIMLEMDRILRPQAFVIIRDEESIISRIKELAPKFLWDVNSYQLQNQENKTEFVLICRKKFWAIV | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 101
Sequence Mass (Da): 12315
Location Topology: Single-pass type II membrane protein
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A0A316UVN2 | GAGLFKTRCAQCHTLESGGPNKVGPNLHGLFGRKSGQVEGFSYTAANVNKGVTWDESTLFDYLENPKKYIPGTKMAFAGLKKEKDR | PTM: Binds 1 heme group per subunit.
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrie... |
A0A5J6Z890 | MVSRSEQNPNHRPAQQGRVVQPAVRHSQSQQRPPRTAGEQFSEAVKRRAEELVAQIHPDWELPHVHIVLAKALAEAEAGQRILPAQENILRAFRVPPSEVRVLIVGQDPYPTPGHAVGLSFSAELPQGVPYPKSLVNIFTEYEQDLGLSRPQSADLSPWLDQGVMLLNRVLTVRAGQAGSHRNGGWEQITEAAVRQISENPQFAAILWGRPAQQLAPIIGKERCVMSPHPSPLSAYRGFFGSKPFSRVNQILVDRGADPVDWDLSR | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular L... |
A0A2P4SN91 | MGGYFIINGLEKVIRMLIMPRRNFPLAMTRHKWKNRGPGFTEYGVVLHCVKDEHSAINMNLHYLENGCVMVNFIFQKELFFLPLGFALKALVNFTDYQIFEELVKDKKNDTFYVNSVTEMLRAVAEAGCYTQQNVLEYLGKSFRVKLNLPEWYSNEQAADFIFNKCICIHLTDRTEKFYLLCMMTRKLCAFAKGECMEDNPDSLMNQEVLTAGQLFLMFLKERLENWLQSVKFILEKRTEKADINVNADSLMKAFNMTTDVTKSFEYLLATGNLRSKTGLGMLQDSGLCVVGDKLNFVRYLSHFRCVHRGSAFAQMRTTT... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase... |
A0A7L0LUQ5 | SQMTQDMLPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGFGYGDYPKLPDKSHHERDPWYRWDQPDMRHNWGEPMHWDFDMYIRNRVDTSPTVVPWHIMRRHFFIFVGTMLVMFVIGGMYPSYMPVGPKQYPFNDLYLERGGDPNKEPPVVTHYEI | 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.
... |
A0A7L1V6U6 | PQWAVVGDTFPVGCKVQKSVVYGDSTFHDNPDTKDPRYSTECGMYQPGCGLDNVLMSWGHDEYMYQVMKFNNFALPKEAFYMVRFHSFYPWHAHGDYAHLCSEEDRRMLPWLRELNKFDLYTKQEELPDVQQLRAYYQSLIDKYCPGVLCW | Cofactor: Binds 2 iron ions per subunit.
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
EC: 1.13.99.1
Subcellular Location: Cytoplasm
Sequence Length: 151
Sequence Mass (Da): 17873
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A0A118K1F5 | MQAINLGIKGSVIQSNIGRVDPGLGQFGNRAITVCMSRSERRSCFGLRSGSGPTGLELGRVGLGSGSMFRSSAKSRSVKSPDSDGDIEEDAPLKSPSRSSGSVLPYVGVASLGAILFGYHLGILVLRKMLFFKDGLLAHFLLVPLLVRLQGDHWQIILEGKKLLYWMQSRLQLEHFFAKNVETMILGRLFCGIGIGISSAIVPLYISELFICIGILAALVAGLPLAGNHIWWRVMFGIAVIPSVLLALGMAFSPESPRWLVQQRKISQAEQAIKKLYGKDRVTELIEDLNSSSQGSEEQEAGWFDLFSSLVSVGASLFLF... | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 470
Sequence Mass (Da): 50414
Location Topology: Multi-pass membrane protein
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A0A124SBI0 | MVVGDVSLENFGVTDFDQLNKMRRQVDVVVNSAATTKFDERYDVALAINTLGSKHVSNFVNECFNIKLLLQVSTAFVSGEKPGIILEKPFKMGETLNGRNDLNIREEENATQERLGQLDAEKADEEVVSSAMKDFGTQRIIDGYIAAYSRGRITCFLADPVKVLDIIPADMVVNAMFVAMVAHINQPYSKIIYHVGSSKSNPITASSYNDTNLRKLLNMVNLSEMDSFFFDSKLLNWEDYFVNIHVPGLLVLASEAPTTLRYLIGDGDLSFLLSVIPICVLVDELQLSSCILLVSNASADLETNASEASQRPGRVMQSHV... | 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: 549
Sequence Mass (Da): 60745
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A0A124SCI2 | MPTITTTFRKPLMILDCKKKGLELVSDIGVGSLVKDGHELKGFVKLYHWELEHLFQISYRGDVIQIDTWISAFGKNGMSTNWMLCDCKTGDILMRASSTFVMINKETRRLSKIPLEVRAELEKYFVDTAPIIEEITSNFPKLDKNNVYVRNELTPRWSDLDANQHVNNLKYVGWILQDVPERILENYELASMTLKYCRECTMGSVVHAYTSILGNNNGGIAYYSHVDCQHQLQLDVAGGDGEIILEGRTRWRPKNTTTSFFHKGSKDDDDVDEES | Function: Plays an essential role in chain termination during de novo fatty acid synthesis.
EC: 3.1.2.-
Subcellular Location: Plastid
Sequence Length: 275
Sequence Mass (Da): 31465
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A0A976MED5 | MICEVDKNYINKFVKNRPTITEDRLGRDARLTYYIYHLLLSNNIERFDELFDYVSGYERMFERMILSSSYVKRTIDLNTQSSDEFSQSIENDSDGFVDLDIVEDKYVDNVNVNVIDNLSVGNNYNVHHIVNDTVNLNEEEHVSSDTSVIDKMTFYYALVKDAPNIVLQIGYKIEVLVNILSSVKYNKCIIFTNQSHMRAQTYGILKYLGYTCYIISSRMSHAERVMMLYDLSSVNNVIILCTDVMSRGIGISNVDLVINMDIPGSKEIFLHRSGRSGRFGSKGVCVSICMESELETYKYFLFSLNFKSDSVGKLYDSEGC... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 453
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): 52347
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A0A7J4URS1 | MSESFYDILDIDRNATTPEIKQAYRKKAAQHHPDVSNDPNAEEKFKNIKRAKDVLTDPSLRKTYDQIGHSQFEQAQKQGGFSNTHFSGDPSDFFTNSNFSTSGFGNLFETFFGGTSRSTPRRGKTLTTSLEVDLEDAYSGVTKTIRFTRPESCTKCNGTGHPSDAKTTNCSTCNGAGTVTRTSSTLFGQIQQVTTCPTCNGDCVSYSKKCNSCSGSGTSINKTEIPFQVPPGVLDGTTFLYEGEGAALKNGTNGDLKVTISIKPHPEFKREGSHIYYSCEIPFQSAVFGTKVNVPTIGGSSELTIPPGTQSGDIFTLSGS... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
A0A421BGJ9 | MENNKVNIICYLSNGAPSVEKTFENAERYIEAGCDIIEVDLPTDNPYLDNQLIQDRMKYSFQQDESLDRHLQTIVELKNKHSKMKFIILAYEASILLLGIEKFIKAFQKINPEGLILVGEKDGDVRRELQGKGIKCAAYVPFDLPEKDVEIAKKSNSFIYLQAKSSGKIKDNLDTLDKVIHYMRQVIGLKQDIYCGVGVSTPEDIRMLKAAGADGAFIGSGVIKREDTPEEQIAYIKSLKIASK | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 244
Sequence Mass (Da): 27452
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A0A7S4ER02 | TMPSPFDSPATSRVPTEYPPEYPTVTSSLDLLRRTDLRALLVHAPFALVVCSAGLLLIDHVHFQYNGFLIGLLLYSIATLKSRPVLSAAIFAILLNLKHLFLFAAPFYFIYLLRHHVLASIALDAFS | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 127
Sequence Mass (Da): 14127
Location Topology: Multi-pass membrane protein
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A0A1F5VGE6 | MEKKLIFLIGFMGSGKSTIGPVLANAIGWHFIDLDLTIEQHVQLPIHEIFALKGESFFRAIEKEMLSHVSTMDNAVVATGGGMSCDQENRNLMHASGIQIWLQWHPDNLLKNAKNAGHLRPLLKDDDSFLELYYSRKQYYETADIIISCDNLTIQDIVNTILQSVTKYNIIDNDEVLDIV | 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... |
A0A7C9D574 | EQGLGFAKTLDESGSVIVLGNAVFLRHHQVAKAIQNIVSTSIADPNDPRIAELEKMEEKKAEIDRKADALVRRELWAGLGYMVVQTAAFMRLTFWELSWDVMEPICFYVTSFYFMLGYAFFLRTSKEPSFEGFFQSRF | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
A0A7C9AY77 | CNLNCVDEDDNSPNNDKRTISTIAGTPVSWHATLEQVPSGVPTIIIAYEFYDALPVHQFQRASVGWREKMIDVAEDSTLFGNTNLFTSSMSLDLSAYVDFASIRYSTQEASGVGTSILFLPHRLNQPVLYNRISTEINNQIT | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subce... |
K6W694 | MTVADSPMDMTPHPPGSEEIVLVAMVSANRVIGDGHDQPWHLREDQQRFRRMTMGHPLLMGRRTWEAIGRPLPGRPAVVLTRDTGWSAEGVTVAHDPVAGLNAARALPGADRIMVIGGGQVYEALLPFATHAEITEVDAESPGETLFPELTGPDWVETGRDDRFAFAFVTYQHTARTRR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A081BPX0 | MKRWSRIAVTFIKFSIAVAFAVFILYIGLILSLLYFWDGALFIETLCSDRTLFSIKISMLTATTVTFLSLLFAVPSAYALSRLDFVGKHLIDTLLELPMVVSPAALGAMLLIFFNNPIGVWIQNSYMQFVFTISGIILAQFVTTVGIATRLVKAAMDEIPYRYEDVARSLGASPLEAFFTITLPLSKNGILAAGALTWAKAIGEFGATITIGGSMAMKTETLPVAIFMRLSSADIEGTVALIFVLTGIGLSMLSGVRLLTKLGHRYD | Function: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 267
Sequence Mass (Da): 29076
Location Topology: Multi-pass membrane protein
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A0A2S9FHZ7 | MTMEDIALSADPTAGVHHYPLDPLSGAEIEAAAAIIMASEYGTPTLKFVMIQLAEPAKTASLTFDDPAGTPRCAFVTMYDAAAKMIYEAVVDLTASLIESWKPVPGRFPSYLVEHMTGVEEKVREDPRWQEGMRKRGVTDFSLAMIDPWPAGYYGAQDHYDNSALICRP | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
EC: 1.4.3.-
Sequence Length: 169
Sequence Mass (Da): 18560
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A0A6P7FCU5 | MKRIFLLWFLIQITSGARILAVIGNPSFSHQLFYRPIWLELAKRGHDIVLLTTDPMPEVPANIKQIDWHFAYEIRHNKYDLAKRMKDCNFNIFTIMNSFQEVFHDIVDEELSSPEVQVLIRNETEYFDLVITEYLPATLTAFSERFKCSFVTVFSTEVGNSYHQVLGNMLNPVLYPEHMASYEINLNFEQRLSSTLYWLYNSFYKQSSWDKMNDALLKKHFGQLPPLRDIVRNVSVVLVNSHHVFSSKPMGPGFIRIGGGLHVSQKNELPQDIKSFLDSAAEGVIYFSLGTNVRSSNIQQDILNKFLNVFKRLPYKILWK... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 512
Sequence Mass (Da): 59743
Location Topology: Single-pass membrane protein
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A0A6P7GXQ0 | MVKLFATGFKALETNLYLHASYTFMPKIFNPLRHQNPDVFKKLIPIKGDVSELNLGINKEDRELLVNTVNIIYHSAASVRFDDFLKDAIILNVRGTREVAKLALDLKNISIFVHISTAYSNCDKLVVEEKLYPAHANWRDAITIAEECDPKTLQVFSQKYIFPLPNTYTFAKSLGEHVVNELCQGKIPVVITRPSVVMQTLSEPIQGYIENYNGPTGLMTALGIGVIRIIYGNRDAVVDYIPADYVIKGIILATESQRTKKTTSDNIEIYNMSYNPILRITLEEIMRFGDKLYKENPYSQMLRHPKVALTENFYKFYSEV... | 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: 478
Sequence Mass (Da): 55100
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A0A7C8ZPU3 | GGPTSATMNLFPRKMEEEKNVSKGEENIKSLDLFPLTSSSATASTTDESTKNMTHWSESPISTEQTQTPGTKMTIFYGGQVIVFDDLPEDKAEEIMSLASQLGSLDSHSETRTQIQA | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 117
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 12761
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W3XN45 | MSFSQVSLALTILVSTVGTYIACSPPNPNPQGGPESESSPSHDLLSTLNLTKRHTNKFTIGPMCILAVHALLLAFYYPDLPPALLGHGDANGLNRDLITWSPATAIPLALILCVGIPLRLVSYASLGRNFTFALARPDRLTTTGIHAHLQHPSYTGVIVLVVCNLALLARADGVACCWFPPAWHAALRSPGAGEPTAVVLGLSLLAGVVWTRVRQEEQMLKAQFGAEWERWHAQTSRFIPGVF | 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: 243
Sequence Mass (Da): 26163
Location To... |
A0A103XS42 | MVGQFAKPRSNSFEEKDGVKLPSYRGDNVNGDAFDLKSRTLDPQRLIRAYCQSAATLNLLRDFATGGYAAMQRVTQWNLDFTEQSEQGDSRVDEALGFMSAVGLTVDHPIMTTTDFWTSHECLHLPYEQSLTRLDSTSSLYYDCSAHFLWAGERTRQLDGAHVEFLRGIANPLGIKQ | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
EC: 2.5.1.54
Subcellular Location: Plast... |
A0A388SHK9 | MADGIDFDVFVIGAGPGGYECAIRAAQLGFKTAAADPWKDADGKAAPGGTCTNVGCIPSKAMLASSLAYESAGETFRELGINVGPASFDLDVIQARRAKVVRKSNDGILWLFKKNGVEFFPESAHFLPGGKPGAWKIGLSDGTEITAANVVVAAGSVPRLLPGVTPDEKTILTSTGGLEQTSVPKRLGIIGAGVIGLEIGAVWQRLGAEVTMLEALPGFLGIADEEISRAALQVYKKTGFTFHFGCRVESVEKRADGVVVRYRTGDEEKEAVFDRLMVSIGRVPALQSVNPEAVGLKADARGFVEVDEGCRTNLPGVYAI... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 475
Sequence Mass (Da): 49881
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A0A1N6NLZ7 | MLTRLSLRVRVLLVFAGLAAAILAALAAALWVAGASLSGRGVPMPAMLDALALAALVAGLGALGAIAWIWFLFDRNMARPIELLAGGLRTGQTPEIEEARYLADLGPAARDAAGARARSAEALAEAIAEHATELQREKETLEAILADIGAGAVMTDAAGRVVFYNASAAHLLPGIALDRQIGRHLPAAALEAGAARLAAGASATDLTCLTAQGQRLRGRMRRVDDGMLLILHDRAPLRPAPRALIETLRRRAATLVPMLGALDGPMPPALAQAIRAEGQGLAQALRELAAATGADDASQGRAGLNELGAGLDQAPDQPRL... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)... |
Q8RB20 | MKDKDLSNVMVIFGGTGDLTHKKLMPALYNLRYQNILPENFAVVAIGRRDKTEEEYRNEMLESVKTYSRFDIDEKIWQDLSSRIFYKRFDFNYDNGYMELSYFLDELDRKYNTQGNRVYYLAVAPEYFGIIVEKLYRHGMVSNETSWQRVVIEKPFGENLESARKLNKMITDVFTERNTYRIDHYLGKEMLQNIMVIRFANVFFEPVWNRRYIDNVQISSNETVGIENRGGYYEKAGALRDMVQNHMMQLLTLTAMEPPVNLDTESIRDEKVKVLKSLEIMTPELVEKNVVRGQYVGYRQEEKVSPTSNTETFVALKVHI... | 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... |
I7H717 | YTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQFIAYVAYPLDLFEEGSVTNXFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYEC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 168
Sequence Mass (Da): 18550
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A0A3D8YT82 | MNGMLLALQFFTSIPIRKELSMEKRHVMAMYGALPFVGILIGLAMTASILLSDWIGFGSIITAVLTLIVGIALTGGLHLDGVADTSDAYFSYRDQNRRHEILSDPRIGAFGTLGLIVCILLKFALLQELIATNQANIYVLIAVPFFARSAMVLYFVSTKPAKASGMAVFFLEKLNRGPLVSWTIVCIVAGLIAIGIVLETVVLPVVIEGVIVLSLLLYKSWTIRNFGGVTGDLSGAFIEGLEVVLWLAVLIVL | 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... |
A0A3M0C5C7 | MLQFSRIKIGFIVFVCLFGLAAAIPNFLSEDQRNALPGFLPSDTLSLGLDLRGGVHLLLEAKTEDVIAVRLENLAGQVQDLRRSVRALNFRNIQVDDRSVSFEVTREDMVERAREELLPLTQPTPGVNPLLSGGVQEVDLARDGTRFTLTLTDQGIQSQKRDAIQRSMQVIRDRVDPSGTREITLQPQGDDRIILQVPGADDPAALLRLIQTTAKLTFHDVDTSISPEDIARGRLRPSQLLLPLKDGGSVVIKKRVIVAGEDLIKANPSYDENGRPAVAFTFNNRGARRFGNHTRENVGRPFAIVLDDIVISAPRIISPI... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 533
Sequence Mass (Da): 57503
Location... |
A0A3M0D7R0 | MFEQFSPDMPLLLVGCGRMGQALAAGWLARGLTSDALWVLDPACDRSALPDVPGEHWAASPEGLAAMSVPRTAVIAVKPQIMGTVLPGLAALLGPETLVISVAAGTTLASLAAGLSAGTVSGTAPGLSDRPRLIRAMPNTPAAVGQGMTGLVGPGCDAGDKQLAGALMGAVGKTVWIADEALMDSVTAVSGSGPAYVFYFVECLAAAARDVGLDPESADLLARQTVIGAACLMDADPSKPAATLRDEVTSPGGTTAAALDVLMAADSLAPLVRQAVRAARDRGRALAGDD | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A3D3WBE6 | MTESKAGQPALTDHRIQTSQRSRPLPQEAAPYQDMPIGRVVAQYKDLYKVASQRAEVIAEISGKLRYASKGLSDFPAVGDYVMIDREDPQSGNAIIHHILPRKSVFVRKAAGTTHDIQVVAANIDTVFICMALNNDFNLRRLERYLAIAWDSGAIPVVVLTKADLCGDLSAKLSEIQKIALGVDVLVTTSMTGDGYKVILKYLGANQTVAFIGSSGVGKSTLINRLLGEDVQKTLEIGKDDKGRHATTQRELFILSSGGAVIDTPGMREIGVESVDLAKAFTEIDDLASMCRFNDCRHEEEPGCAVRKAIQEGALSEDRL... | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A411ZYY9 | MNYRVIIPNMFTSGNLVFGMCSIISTFNGNIFWGAVFILLALVADGLDGRTARFFGVSSEMGKEMDSLCDCVSFGAAPGFLAYSFVIHEFSYFGWIAVIFYAVCGMWRLARFNVNASVIHGYFMGVPIPAGGCLIATWILLSTHLGITPAMQIDTLGYFLPILIMFVGYLLVSTFKYPDFKGKGEKISKVALGIIAIFAICVLYFGRDAIGYAILFDIFISYALLGILNTIFSLGRN | 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: 237
Sequence Mass (Da): 26027
Location Topology: Multi-pass membrane protein
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A0A0D9X1K9 | MAASVTAAAPSRPPLPPPSKGGKFVTILSIDGGSIRGLIPATVLNFLESELQRIDNDPNARLADYFDYIGGTSTGGLISMMLASPNKEGRPLKSAEEIIQFYKDNGQEIFTPNSVGWFNLILDLSKYLGPAFGHLFIQQMLIENGQADDATALQQANDATTMPLLQLHLATMELMVSKKASHLSFKDKIAYALVQPKYDNDHLREAIGNVLKTGIPKLSLRQTLTNVVVPAFDMKANQPVVFSTHQAKKRALMNPLVSDVCVAASAAPTYFPPYEFTTEDDYGAKQEYNLVDGGVFANNPTMLTMEEIRKRTIVKQEEEF... | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 513
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 56143
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A0A7Y2CAS6 | MAVGGCAPPFIDNLDLDSPPGQCQCGEKADRACANDQHLWLVSSEHGSISLGSGGTGHHESCDSAVHKHRDSASFRSRGKDYAHAGAVGGLCLEANENRTSSDSYTTPENYSAVPVVDNTERAIFAAGCFWGVEHYFMRAEGVKSTRVGYIGGHTSNPTYREVCAGTTGHAEAIEVVYDAAQTSFEDMARLFFETHDPTQRNRQGPDVGEQYRSAVFYIDEEQKAIAEKLIGLLRAKGLDVVTELEPAATFWPAETYHQQYYEKTGKSPYCHFYTKRFD | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A7Z0D3N5 | MTPAGRTAIDAAMMQAVDESRRGAGLTAPNPRVGAVILDADGNVVGSGYHARAGSDHAEVVALRNAGDRARGGTAVVTLEPCRHQGRTPPCTQALLDAGIDSVAFAVADPIHSGGGDQLEAHGVAVRRGVRETEAREANHEWLIAEETKRIHVTYKAAATLDGRIAAADGTSQWISSEASRQDAQTLRRRADAVIAGIGTVLHDDPRLTRRGPDGRELPDQPLRVVIDSSGRTPPEANVRNGRAPTLIGTTDEFGADPAGRVDLDRLCADLYARGHRGALLEGGPTVAGEFLARGLIDRIVVYVAPTLLGTGRPLIGDIG... | 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... |
A0A0D9VNX2 | MSSLGFTSMAAAAVYYRFASQMDGGGDAVPGEEEVGAADVPGGGGDVQPRHHVNGRRRRLLPLRLANGDFPSHQGGGEIPVTEMFGTFALSVGAAVGMEFWARWAHRALWHASLWHMHESHHRPRDGPFELNDVFAIVNAVPAMSLLAYGFFTRGLLPGLCFGAGLGITLFGMAYMFVHDGLVHRRFPVGPIANVPYFRRVAAAHQIHHMDKFEGVPYGLFLGPKELEEVGGSEELEKEIKKRIKRKKTLDAIQ | Catalytic Activity: a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+)
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 254
Sequence Mass (Da): 27858
Location Topology: Multi-pass membrane protein
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A0A2N0WZK1 | MKVIQTSIPDVKIIEPTVYGDDRGFFLETFQTERYKELVGIALPFVQDNHSRSLKGVLRGLHFQKTKPQGKLVRVVKGKVFDVAVDVRKSSTTYGKWEGVILSEENKRQLWVPPGFAHGFLVLSEIADFEYKCTDFYDPADEGSLMWNDPDIGIQWPLTARELKKLQLSEKDRVAKAFKDL | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence... |
A0A3B9M1T0 | MGWYIVKQILLNQKEKALSFWNKLSKIQKILFGSGFAVIILAAIIMIFWISKPNYVPLYTDLNTEDAAAITEYLKENKITYQLDEGGSTVLVPKSQKYDIRLALANEGLPTGGSIGFESFNETRFGETESERRVRYLIALQGELERTIGKLDAVDDVRVHIVVPEPSLFLENKKDATAAVLVKIKPGHHLDAAQVKGIMNLVASGVEGLEPKNVTVVDTGGNILSTGVENEATTQSSSMTARQHQVEQEYEERVENSVQKMLDQVVGKGKSVVNAHISLDFDQVEIHREIYGDKTVRSEETEEEQTTTNNTPGGTPGSDS... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 519
Sequence Mass (Da): 58021
Location Topology: Multi-pass membrane protein
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A0A7Z0IIX3 | MLSAASECADTRHLSSSHFKGKTERNAMAAHSTITATAADALTILPEESVISSTGELAIGGCRVSDLAAEYGTPAYILDEVGLRRQIRRFVDGLAAMRPNSEVLFASKSLPAVAMYSIAASEGLSIDVAGAGELVMAFSAGVPPDRIYLHGNAKSDSELQMAIDAGIRAIVIDNFDDLSRLERLVTGPQHVMLRMIPGIAPQTHASQSTGGNDSKFGLRPDQLEQAVHRIRSHRHLVLDGVHVHIGSQVLDTMPFDRAVRSVAELGTFDAYDVGGGLGVRYNSADAAPSVDEYLHTIVRAAEQLPATARLLIEPGRSIVA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Le... |
A0A8J7TDI6 | MIGKLKQNLLLACLVISSITVFYLGRHAMECHHRIEEQGQPGATLRTGPGRNSSAFAYNKDMPLIFIGGVPRSGTTLMRAMLDAHPDVRCGEETRVIPRILAMKQMWSRSGREKMRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAAYLCNKDPFALKSLTYLAKIFPHAKFILMIRDGRASVHSMISRKVTIAGFDLGSYRDCLTKWNRAIETMYAQCQEAADKCLPVHYEQLVLHPEKWMRKLLKFLNIPWNEAVLHHEDLIGKAGGVSLSKVERSTDQVIKPVNVEALSKWVGKIPADVLRDMPAIAPMLARLGYDP... | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
EC: 2.8.2.20
Subcellular Locati... |
A0A7Y2GAQ4 | MKFVDYVTIAVRSGKGGAGAVAFRREKYVPKGGPDGGDGGDGGSVILVADPQLYTLLDLRYNRHHFAENGRPGEGSNKKGKDGEDIVLRVPVGTLVRNTESDIVIEELLEADDRLVLARGGRGGKGNTHFKSSTRRAPRYAQPGEEGEELDVILELKLLADVGLVGFPNAGKSTLVSAVSAARPKVADYPFTTLAPSLGVVYVDEYASFVIADIPGIIEGAHAGKGLGTRFLKHIERNALLLFVIPIDAEDVAGQYNTLLDELESHDALLLQKPRMLALSKTDLLSGETDDSYIKELRATLPSDIDVLPISAVTGAGMTE... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0A0G1BYW1 | MKVLIIGSGGREHALAWKIKQSRQVKKIFIASGNAGTATWGENIEIKANDLTGLLNFAKKEKVDLTVVGPEEPLVLGIVDLFKKHNLEIFGPIKKAARLEGSKIFAKRFMKQFRIPTAEFKAFKNLTKAKNYLKTVNFPIVVKADGLTAGKGVVVAKNFQEAKKALTRRVVIEECLIGQEVSIICLTDGKTILPLLPAQDHKAVGDNDLGPNTGGIGAYAPVPIVGPALINQIKKEILQPVITGMNQIGRPYQGVLYAGLMLTKAGPKVLEFNCRFGDPETQPQMMMLKSNLVKLILACIKGRLKNEPIDFYPGYSVGVV... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A0G1EAB2 | MIIQNDRELKTYQKGVDLAMKILLQLNQSLKPGILPINIDQLAFQLCDQYHVRPAFLGVGGKHPAYQYATCISVNDTAVHGIPSRTEVFKIGDIVKIDFGIIYQGFYTDFCVTVGLKQLTSAQTKLIQVAKKAVRESIKQAIPGNTTGHIGSVIHAIAKKSGFDVLKKYTGHGIGKTLHDSPVIPAHGTPGQGEVFKPGMVVCLEAQLVSGKDQVEVSEDGWSVKTIDHGLVAMFEYMVVVRDKPLVLNSTFDWPIIV | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
A1R4A8 | MVATCTDGSRGDIQNPALEDAPHPKRDMAGARRLEMANAAEVLGIQQRWLGFVDSGLPEGDPLPPLPPGCFALQPLERATAPLVRLVRKFKPHVILSYDENGGYPHPDHIMAHKVAVEAFEAAGDPERYPGMGEPWAPSKLYYDRAFSPERFRALHFALEEAGLQSPYAERLAAWLEADAEGHTAPVAGHQTTTQVDCGDFFEARDDALRAHRTQIDPLGFFFAVSPDLQRTVWPWEDYTLIKSTVPSELPEKDLFAGIR | Cofactor: Binds 1 zinc ion per subunit.
Function: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylatin... |
A0A7Y2ES20 | MSSEKGPQKTYEQINREISWLAFNGRVLQEAADESVPLISRLQFLAIFSSNLDEFFRVRVASIRALLRLKDKHASKLDFNPARLLKEMQNVVVKQQRKFGDIFSHSILPALEDEGIVLDLDVSLGSSQTEFVSQYFDEHVSRHVYPLIITAGSTPPFIENRGQYLVAELWPSSASTLFVEEPSYGLVEIPQDIDRFVPIPTEDDVHHVLFVDDIIRANLYDIFPEYEVGESYSVKVTRDAELYIEDEFTGNLIELISKSLKKREQGVPTRFLYDMRMPYPMVTVLKNYFRLSDEDLVVGGRYHNFSDFFGFPDFGRKKLS... | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n)... |
X5MMC3 | MTGETLSQALSRGRAFLTQHDIETAALDARVLLQAASGLSHEALVMHGDDAIAPEAGQTFQMFLDARSQGKPVSRILGRREFWGLELGVSGDTLDPRPDTETLVAAVLDRVGGRRRPFIRDLGTGAGAILLALLSALPQARGLGSDLSYGALRMARANARAIGVDDRAAFVLSDWGRVPTRLADVVVSNPPYIARGELPGLMRDVRGHDPMRALDGGADGLEPYRRIAGQLPLVALPGALLAFEIGPTQAAAVQGILSGVGASVFGPGLGMLRDLAGRPRVIVARAPRH | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A101G373 | MIDEVTTEGPSVEDAIDSALEEMGVQQDAVEYEVLAEPGRGLFGSSGRPARVRVWLKPGAVDSGDDIDDDADDDESGVDDASSEDVELTDDELDAIADAGADAIKEILRALGIEGSIDEYEGDEGEIILDITGDDMAVLIGRHGRTLDALQVIVSTITNRRLDTRYPLVVDVSGYRHRRRVKLEEIARGAADRAVRQRRAVQLRPMSSFERRVIHMALREDRRVHTESEGMELRRMVVVHPR | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 242
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
A0A158SMW8 | MTAFATNGLARAHHTWSTATPAPGARQILLVNLMPTKEATELQFLRLLDATGVNCDVTFAYPASHQLHHQRAAVLKHYLPLDRLWGTRFDALIVTGAPLEELSFDQVDYWAEFRRLVAWSKTHCRRAIFECWAALAALNVRYQIPKAPLPHKLFGIFEARVNPASPLFGGLTKLRMPQSRHSVLRLPATLPADLQVVAKSQGIADGLLLATKDTRELFITGHPEYATDTLDQEFHRDQARGRTINPPQNYYRHHQAVNSWRTTSCRLYANWLTI | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
EC: 2.3.1.31
S... |
A0A1F2P5N9 | MSLMSQDEVRIGVYVCHCGINIAATVDVAKVAEFASRLPGVVVARDYQYMCSDPGQELIKNDIKELGLNRVVVASCSPRMHEPTYRTVVAETGGNPYCFEMANIREQCSWVHKNREEATRKAMDLVAGAVARAYLLEPLETREVDVIPACLVIGGGVAGIYAALGVADKGFKTYLVEKSPSIGGHMAQLDKTFPTLDCSACILTPKMVDVARHPNIELITYAEIVDVEGYVGNFRVRIRKKPRFVDVEKCTGCGLCAEACLLAGKIPNEFDLGKGKRGAIYVPFPQAVPLKYTIDPERCIYLTKGKCGKSPACQDACPRD... | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.... |
A0A540L275 | MSGGPSWNVLKGRKDGGVSKANETINLPAPTFNVSQLIQSFAKRGLGVKDLVALSGGHTLEFSHCSSFESWLRNFSSVHDVDPTMNNEFAQKLRNKCPKPNRDTTAGELFYSTSSTFDNNYYKQLVAGKGVFGSDQALFSDYRTRWIVESFAKDQSVFFKEFAGSMVNLGNVGLIEDGEVRLNCRAVN | 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: 188
Sequence Mass (Da): 20764
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A0A848VP58 | MGGGTTIAAIATARGEAALAIVRVSGPEALRIASEVFKGFDLTSAPERSVWFGRAVGSAGQVLDEVVATVFRGPRSSTGEDVVELTCHGGDAAPSAVLRALFDAGAEPAEPGEFTRRSFINGKLDLEQAEGIMDLIHARSAAAHSVSVRQLRGRLKNRLATLRENLLRTCGLVELELDFGEEDLEFADRTELTSLLSDAEGTVQELLASAQLADKWRDGLTVVIAGRPNAGKSTLLNALVGHDRVIVSSTPGTTRDFVECEFELDGLLLKLVDTAGLRVTEDEIEADGVRRTEALIASADVLIYVYDSLEGLSETEIQAL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 481
S... |
A0A540NCX7 | MRVAASACFLQRTFNSNPMGSGVVTLLHLQSNFPVSPLPEEIISPLSTDAIIHDDKKQVGSFLMRWLGVVFKRDISKYIQLLGHWIVYQLLRNPNNFQQLELELSVESHLVFALLGFLIGLFLAAYSIIFGVEPTKGFRQLLEKNSICGASGILLREKFNSDSSKAHLWFGCIVGPLGVWIWWFLARLNEHGLGTMGCLKWVPFGTLIANISAACVMATQSTVKRVVSSCDMISVHIHSMI | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 241
Sequence Mass (Da): 26850
Location Topology: Multi-pass membrane protein
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A0A7Z0IJ25 | MVDIAPRQKPGRQGDGRRRSGLADWFHAPTTSYYLIIGSTVALTVFGLVMVLSSSSVDSYDGGQGSSYSVFDRQAIFAAVGVVLMIVASHVPLSVWKKMSWGLIALAVVAQLLPFVPGVGISENGNNAWIHIGSFTAQPSEAGKVALVLWLGVVLGAKHKLLGQWRHVFIPVVPVVAILLGLILLSGDLGTGMIFMVLVLGALYAAGVPLRMFGVAGIGLAIIAGAMLVSSPNRMARATNWLSGGGTSDPLGGSYQSTHGLWALASGGFWGEGLGASRQKWDYLPEAHNDFIYAIIGEELGLPGTIGLLIVFALLAIGLL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
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 = [GlcNAc-(1->4)-... |
A0A553AMP3 | MSEDQPFNGGTSDLFDRDPGHVRVVDLQFRRFGLNTRFHGRCVPLWSAGSHQPVLAVLSMDGRGRVLVVDGGGDLTIGLMGDRLAGIAIQNGWAGIVINGAIRDSAQIDGMAIGVRAMGTTARRSLAEPPAPPAGPVRFGGVVFTPDDWICADEDAVVVSAADPAQGGFAGDGSA | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A378STB2 | MTRSPGAGRFAPSPSADLHIGNLRTAVLAWLFARSTGRRFLMRVEDLDDRTHTDIADHQLADLAALGVTWDGDATRQTEHPERYDAVVDTLAGRGLLFECFCTRRDIAQAPRAPHAPEGAYPGTCRDLSDADRERRRHETGRPPALRLRSDTTSHTVHDVLHGDYTGLVDDFVVRRGDGVPAYNLAVVVDDAASGVDQVVRGDDLLSSSPRQAYLARLLGHPEPVYAHVPLVLNADGARLAKRDGAVTLAEIGLSKALAQIADSLGYTARSVGDMLDEFDPRRLPREPWVYQPG | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC an... |
A0A540M111 | MVYIGGSEEEERVAAKSMAMGSERTKALHNFNLPWDLKWGNQRHLRCQKESSEAGGSGGEGSEANRRSSAQRMESSPAVTRRRDLEFEKRKFRAPRPRIENDDAEEGIDAFRQKLMSDLKTAADKMKDAILREEEVAVAGAAAYTDVAAAEEDVEMAEVGESEPPVGPEPEQPEARPWNLRTRRAACKAPMGGGGAKVVRIEEKKANYSPLRSEGNNGVKSPRLVRGASVSGPEKNKEEEKPKFSLTLTKKEIEEDFMKMLGHRPLRRPKKRPRNVQKQLDGLFPGTWLTEVSAETYKVPEFPENTKVLSVGKALSIQAH... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 636
Sequence Mass (Da): 70933
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A0A969YWH2 | MKNHYVNWLITIFIISLTAWIISSSSEIKNIPYLFEITNKRCILVAILCMICYWLIDALIIQAIFSLFHLRLSCLSYLLIAMIGQYYNLITPFSSGGQPAQILKMTNDFKVNPSLATSVTINKFMVYHIVVTIFSLFLSVFKADFILQQSTLSKTFIYLGLTLNALGILAIFATCYNTYIAEQIISLFFRIIKNLPVGKKIRQEAVTRYIHEYRISLFAFLQNIKVLFYVSLLSLAQVFVYFSVTYFVYISLGLSKALFVDILAMQALLYIAVNFIPTPGNAGASEGGFYILFGLFFPSNILVYAIVLWRLIVYYFNLVA... | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistan... |
A0A0E9N6V5 | MSNTRVAHRYSKALMDLAIETNQVDAVKADIDGIRKATTGELERALVSPVIRHDKKCQIFKALFGGKVLPITEKFFDLVFTKGRELSMVEILDAFNDRYRELKGIRIVELTTAVPISDELRNDFRNRLLKMERYQGKTVQIQEKVDANILGGFVLQMEDDLFDASIQRDLKDIKTQFIENMYIQKIR | 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... |
A0A8C5U7U4 | MRRVRCCPLSSPVTSLPPSPRSSSPVPLPSPVATAASLRGCHGNGAGEGRTRHPQWHRGDGAGATLPPFGEWCELQPRDAAKMPESAWKLLFYSVSWSYGAYLLFGTDYPFFHDPPSVFRGTGSATDIAIAYLLQGSFYGHSLYATAYMDTWRKDSLVMLLHHVVTLTLIASSYAFSDVGSWSFLHDSMGPLEFTKLNVYFKHRGGVRHRLNDRGLVRPIGSVKVLYATSHSSLQAVPDIPFYFFFNALLLVLTLMNIYWFLVGAAGQMQEVNDVREYDVEESGTRDSGTRDSATRDSATRDSATRDRLRAPREEPGVPL... | Pathway: Lipid metabolism; sphingolipid metabolism.
Catalytic Activity: octadecanoyl-CoA + sphinganine = CoA + H(+) + N-(octadecanoyl)-sphinganine
Subcellular Location: Membrane
Sequence Length: 348
Sequence Mass (Da): 38291
Location Topology: Multi-pass membrane protein
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A0A345P761 | MSELTQPNNDAAPSKPRPIIGQRFRGFLPVVVDVETAGMDAKTNALLEIACIPILFDENHQLVPGEAVHAHIKPFEGAKLDQRSLDFIGIDPFNPFRMAEEEKPALLRIFKSLEKTRREQGCNHCVLVGHNAHFDLGFLQAAVARTHTKNQTPFHSFSVFDTVTLAAAAYGQTVLARACQAAGIPFSNGEAHAALYDTQKTAELFCKIVNAWPVMQVLGAAEGTEENANDESE | Cofactor: Binds two Mg(2+) per subunit. The active form of the enzyme binds two Mg(2+) ions in its active site. The first Mg(2+) forms only one salt bridge with the protein.
Function: Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of t... |
A0A1E4IJP0 | MARTARGGSAPRAPGLALWLALAALVIVADQLTKTLVVYGFQLGDARPLTSWFALVRAHNPGAAFSFLAGASGWQRWFFAGLGLAASAFIVWMIRSHPTQKLFCFAVSMIMGGALGNVIDRLLHGHVIDFLQVRFDFLAPVFRGGYFPAFNLADSAITLGAICLILDEILRVRRAG | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A4P8IIP2 | MAKEKFQIDEGFIQLDEIIKQLEQEDVKLSDAVALYTKGVEVLKECRDSLDKVEKELIILEQDGEQNGSF | 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... |
A0A8J7UE78 | MIPQSFIQELLNRVDIVELIGKTVPLKKTGKNLMGCCPFHKEKTPSFSVSAQKQFYKCFGCGASGSAIGFVMQYEGLSYPEAIRKLAESVGMQVPEEPGERQRNARAKTLTDRMQQATQFYCDSLRHNQHIIDYLKSRGITGETAARFALGYSPDAWQALKDVFAEHYDDPEMEEQNGCGLVIVNDNGRRYDRFRGRLMFPIRNPRGQVIGFGARTMNGDEQPKYLNSPETAIYHKGLEIYGLYEAQDVIRQKDRAIVCEGYMDVIQLSQAGFTESVAALGTSITSDHVKKLLKLVDTVYFSFDGDAAGQKALRRALEAA... | 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: 624
Domain: Contains an N-termi... |
A0A8J7P337 | VTSATLGVEVHPLVFHTNRGAIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEQDLQV | Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Subcellular Location: Nucleus
Sequence Length: 166
Sequ... |
A5Z7Z3 | MFLLEVVHDSKYLLSDNYETIKATEILAKEGFVVMPYMYPDLNAARELADVGAACVMPLGAPIGSNKGLATKDFIQILIDEIDLPITVDAGIGRPSQACEAMEMGTTAVMANTAIATAGDVQVMAEAFKKAIEAQKLGATYISAGHIFATDCKKDLPPRGLEFLKEVCNSVTIPVYAIGEIKLSDVQMDEIIKCGAKGGCIMSGMMSL | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
... |
T0S7H7 | ADYLSGVTEDAILSDLIGAYTVLFDQLNNLGGEWLQIEEPALVLDQTEEEQQLFIKIYQELLKNKNKLKVLLQTYFGDLRDSYQEIIKLDFDGIGLDFVEGRESVKLVQKYGFPQDKLLFAGVVNGKNIWRNHYQKTLSLLKDLGNIDNIVINTSCSLQHVPVTTENEIKLSKEILNHFAFSKEKLVEVSEISEIYVKKNTSLLDKNIALFDKNRVQENIQLKQKITHLTDKDFIRTPSLVERRADQIKALRLPLLPTTTIGSFPQTPEVRKARLQYKRGELSKSDYEAFLEEKIKECLELQENIGLDVLVHGEFERNDM... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
EC: 2.1.1.14
Sequence Length: 590
Sequence Mass (D... |
A7BNM0 | MNNNAHPLVPPHGEKSASTYTSCCAPCSGEIMATLIEIRFEYPLFFYNPNIQPLTKYEIRKKENNISPQK | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O ... |
A5ZAF5 | MFGKIIGTGSYAPDNVVCNNDLKEFFETDDQWIRERTGIKRRHIMTNESTSYMACRAAEKAIENAGISCEKIDLIIVSTVSSNTILPSTACIVQDQLKATNAMCFDINVACTGFITAYNIAQSYINAGLVETALVIGAEGLSQIVDWTDRTTAILFGDGAGAAIIKKDEKARFETVMHSDGSMGGALTCENSIQYREINDSKKTFVSMNGQEVFRFAVRKVPECIEELISKMKIEKSEIDLFLLHQANKRILESIGKRLKVSMDLIPENVSEYGNTSSASIPILLDEMVRDGKIQKGNKIIMAGFGAGLTWSAVYLEF | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the tot... |
A0A540NA13 | MTIKLKYELIVNSFKTIDGRDVNVHVHHCKPAGNTNIASSPTHIGWRGKSDGDDISLFGARKIWIDHCSLLFCADGLIDAIMGSTGITISNNYFTHHDEVMPVGTLTFQRRQH | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-redu... |
A0A2T2QWS3 | MAIRRIIQSTDSGGSRDEQEVLTSQSTFITTINEEVRGVVKDLVDTMSAYKICVGLSAPQIGRLMNVAVARVQENGQGGGEESETVVLINPEVIQTSGKKDVKRESCMSVWGFVGSVERRHKLLVRYQTLAGQETERDFRGFPARVILHEINHLQGKMYSHYVAGGLEETDLFGGVSQQGTSDD | 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 ... |
A0A1I5IQL6 | MHDQSIKARKQIISILILLVLIVITILYYLKGYTLQDLQNALANANFAYLFGGFCMIIIFVICEAINIYLILKTLNHKIPFFRCFEYSSIGFYFSSITPSASGGQPAQIYYMKQDKIPMAASSITIFFIVYVYQIAMILIGFIMTLLRFSEALYFISKLRYLFIYGMIMNTGAIFIFFSLMYSKKLAPSIVAFILKAGNKLRLVKNIDETKNRFDKSLVSYHEKAMILKTHPLLFLKILLFSIIQMLALNSIPYLVYCSMGYRTKGILDMITCQSILTISVSAVPLPGAEGVTQGGFLQVFNAFFPSDMLTYAMLINRVI... | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistan... |
A0A388SBP5 | MDYTLPIALITAVSGILWVLDRWVWAPARHLSSGGTARQPKWLEYSAGLFPILFVIFIFRSFVVEPFRIPSGSMEPTLIPGDFVLVNKFSYGIRLPLSHLKVIDASSPERGDVIVFRYPPNPKLDYIKRVVGLPGDEVVYLDKKLVVNGEPAPLTRPPRKAVEAAKGYKHNWQILRIEKLGGKKHAIVLNPNISSEVQPVAGMSPTDSCRYSRRGVVCRIPEGQYFVMGDNRDNSEDSRYWGFVPEKNIIGRAFFIWANFHNMRRFGRIH | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 270
Sequence Mass (Da): 30678
Location Topology: Single-pass type II membrane protein
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A0A942G908 | MLARVEQYVQSNRLAGQGDRLLVGVSGGADSVALLLVLHELAERHSFALVVAHLNHGFRGEEAAEDSRFVKELSARLGIACECGYTSVPTLLMGRNASPQVVAREERFRFFKGVMEKHALHKLALAHHQDDQAETVLLRLIRGTGMRGLRGMSPHDHGLFGISIIRPFLAVSQKEVLEYLAARGQQYRTDSSNLGTEYSRNFLRHVVMPELCKINHEAPVALDRLARQVAIDMDYLEGRVLLELAEAVEPLGLGVGVKLTHLRKLHQALSRRLLMAAYRQIAGEEDHSLEAVHLAAVEDLIGKQPGRRVVLPAMMCALRT... | 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)... |
A0A7Y1ZN69 | MIAVQELIDTLTRNDLLLSQERVSQVLINTVTNDSRRVGPKDLFIAIKGEQSDGHMFIDKAVKNGAIAIVYEVASAATLGLPAGVTGVHVRDARKAEAIVAAALYGNPATSLRMIGVTGTNGKTSTTYLIHGLLQKAGISSGLIGTVETLTGKRSIDSKQTTPGPLDLHELLNEMRENDCTACAMEVSSHAIRQDRIFGIPFHVAAFTNLTQDHLDYHSSMDEYFNTKKRLFDELPSGAFAVTNMNDARGSDIIRDTRAARIRYGSSSRNDVGFVLKNQNMNGLEIEINGRSAHFNLLGEFNASNLACAYAVGLAMGIDE... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A7C6NIL8 | MSQDILIIIDGNSLVHRAFHAIPPLSTSQGLMTNAVYGFTNMLLKIIAQEQPARIVVAFDKGRITFRHDQYHDYKANRSPTPDDLRPQFPILKDVLNALRIKTYELDGYEADDIIGALSAKAEQAGLTSIIVTGDRDALQLVSPLTRVRLTKKGISELDEYDEGKIWDRYGITPRQYTDFKGMTGDPSDNIKGIPGIGEKTASRLLKEYGSLENIIAAADELTGRTGEQVKNYREQAGLSKELVTIRREIPLEIDLDGCVWEGPDYKKLLDIFKKLEFKTLIKSIYQDNRGSGGEGKKQAGRSRGRKTAREALAGPEPAP... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 899
Sequence Mass (Da): 100403
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A0A3P3XYU2 | MVAPVLDAIGVACWAFFATNMDDLLILIMFYTEASLPPSLNPSGFHRHHIFVGQALGFTLMIALSLIGFIGGMFFPVHYVGMLGFLPIFTGCWRLRDLRPDTARARLHPEESVRADPEVTTPTAVSFVLTSPRTYTRVINMNVARVTTMTLLNGGDNVSAYTALFVSMDVASLVACISTLFALLAALVTFADYFARIPAVAEKIVNSAKFVVPFVQMALGIYLLFKTGASKVLASDVEKCAAESATDSDTFAHPSMPRQFQMSLPFQRVQGKRFVRIRAHVNPLSFSDQYVCPDGPSSVVWKEYFPKFPGVSDDAPAGLD... | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.33
Subcellular Location: ... |
A0A7Y1ZQW6 | MQNAPFRQIMRIPGLVASGLVRVYQLVVSPFFPPSCRFSPSCSDYSIQALRKYGLLKGTVLSIHRILRCNPWGGHGYDPPVWYSERTVNDTEADMNVKEDDNGI | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 104
Sequence Mass (Da): 11745
Location Topology: Peripheral membrane protein
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A0A940CQI1 | MERIEFILLRYIIVFLLCLTLLPAPAAAQETPPDLTAQAAVLLDARTGQWLYEKNPDQKMYPASTTKILTGLLALEKGDLSRVVTISEQAAATGEASIWLKKGEKLTLEDLVWALLLNSANDAAVAIAEEVAGSVPAFVDLMNRKARALGATNSHFANPHGLHNPGHYTTARDLALIARAAMKNDTFCRMVGTKTHNIKREDPDALKLLINHNDLLWRYEYTTGIKTGYTTQAGTCLVSSAEKEGRRLIAVVLNSQGPQVWTDAMKLLNYGFEAFQTVEVVRKGQQVMTLPVAGSKEEVPVVTGSSLSYTFPDAGYRQGV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
G2NDP3 | MSTPRSRLADARLYLCTDARKRQGDLPAFLDAVLSSGVDVVQLRDKGMEAAEELEHLAVFADACARHGALLAVNDRADVAHAAGSAVLHLGQGDLPVPAARAILGDDVLIGRSTHAEAEVDAAVAEAGTDYFCTGPCWPTPTKPGRHAPGLGLVRYAASLPTTRPWFAIGGIDAGNLDEVLDAGARRVVVVRAVTEADDPAAAAAELAKRVRARSL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-met... |
A0A942J9V7 | MKVVLVTGGAGGIGRATCQLFAERGYLVLVHYNASQDEALAITANIKSQGFGAEVCRANLADEAEVNAMVASIVATYGRIDVVVNNAGIARDSLVLTMKLSDWQDVLEVNLTGAFLVCRAVAKVMLRQRFGKIINVSSVVGLTGNVGQANYAAAKAGLIGFTKSLAKELARRGITCNAVAPGFIDAGMAAVLPAEVKKALLATIPQGRPGTPAEVACAIAFLASAEADYITGQVLRVDGGMSM | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
EC: 1.1.1.100
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-... |
A0A4U0YJZ7 | MRPPASLTTRLTLLFVLVSSSVLLGLAWVLHTAVERHFVEMDRDILQSKVNVLERLLKRPPAAEELTALQSAVVDMFRSDPELKVFVETADGNPILSPGDIAFPGEKLRNLANGSTPRVFSWWDNGSRYRGLVKAVQPALPDFKPMIVVAAINIDHHERFMERYSRTLSAFIPVAAILSGFLGWRATRRGLAPLRLIEERAASVTASQLNHRLPEDAAPRELTGLAYELNCMLDRLEEAFRRLSNFSSDLAHEMRTPVSNLLTQTQVALSQPRSQREYQEILASSSEELDRLSRMIGDMLFLAKADNGLSLPSVQDIRMH... | 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: 474
Sequence Mass (Da): 52610
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A0A1H1EU99 | MSSSNEMSDEALALQWEAASSEADMDMDMEAAMSATPSQQTTAAPERGVSDQNVDRNLDAVLGIPVDMQVVLGSATMPVASLLKLGRGAVIPLDHRVGEPVDIVVNGRTVARGEIVVVEDDNSRFGVSLTEIVGAKGSYA | Function: FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
... |
A0A5K7ZPB5 | MLNKIRIRHKLLISYSVVLILSISIGSAFIYMVVRDKITAQLERELNNNTTAILNMVKTAAAVSIKNHLRAVAEKNLEIIRYFYDQTQNGRLTPAKARQMAAHVLSAQTIGDSGYIYCMDSVGRVKVHPQSALLGTNVADFAFVREQLARKIGYIEYNWKNPGETAARPKALYMVYFAPWDWIVSASTYRNEFNSLVNVRDFERSVLEPRFGETGYAFVINGSGRILIHPKLQGVNLFEARDLPDKYLKEMQRRKSGKIVYPWKNPGESRARMKMVIFNHIPEYDWIVASSSYLDEFYDPLRTIRNLIIATAIMTFMLVL... | 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... |
A0A0D9VM54 | MDPSAADAADEQDTTDWEEPVEEEEEDANPECGEKEEDDTEDLGGGPSGEDAAADADDDDYTGWGEPEEEEEEDASTRVPHAKDDADDLGRVPSGEEADDADADADANESTDWAEPEEEEEEDASTRVPHAKDDADDLGRVPSGEEADDADADADANESTDWAEPEEEEEEDASTRVPHAKDDADDLGRVPSGEEADDADADADANESTDWAEPEEEEEDDANTRSGEKEEDDAEDSGERRSGEGGADDGDIASPNSADSNLILLPADPMKHRIASLLRRKKLILVLDLDHTLMNSVKLRDLSQEERDNGITRDDPSREL... | Function: This promotes the activity of RNA polymerase II.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 598
Sequence Mass (Da): 66904
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A0A3N7IH48 | MDKKRDISAIADIARKAGEAILDVYHTDTDQWEIQQKHDNSPLTLADTVSHRIIADGLKSIFPAIPMLSEEGKDIPYEKRKKMDRYWCVDPLDGTKEFISRNGEFTVNIALIAGNEPVFGVIYVPVTGVLYYGLKDEGSFKTEGGETRRIQASPSHNPVAVGSKSHKTAEEEAFLSSLDIRDVVSIGSSLKFCLIAEGKAQVYYRHGPTMEWDTAAGHAIAVASGARMTQADGSAFVYNKPSLVNGSFICYSVNLHHKIAALSSGV | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell membrane
Sequence Length: 266
Sequence Mass (Da): 29079
Location Topology: Peripheral membrane protein
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A0A8J5CMX7 | MMFSFKKALAGAPRTVTREGQGPKQISHHIMLEILCCLSVLLTVRLMFGCPVLQTLPLPNGSVSKKTSDGGLFGTAPRVSADHAKTSRSLRGSLHRTCSSGGASGGVGDRHGVCGSKGGSGSLVGSGSLRETSAQTPVSATPVSCRRATANHRAAAVVTTEGPPPRYHVSEYTFEREHPDSPYPEQKESSRTKKMRWEAYSWRHWCVLAALLLLSGGVVLAVALPLAARRDAQPRQHDALARVHRILSTVPLIDGHNDLAWNIRNFVHNKLEKVDMSQNLSTVEPWGSSPWSHTDLARLRHGRVGAQFWAAYVPCGAQYL... | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 402
Sequence Mass (Da): 43759
Location Topology: Lipid-anchor
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A0A3P1WKP2 | MKQGCLIVALGTPDAPTPERIREFLRSFLSDRWVVDFPRFLWKPILHGIVLRVRPKKVAPLYRHIWLEDGSPLEVYTRAQRDLLAAALPDIEVRHAMSYTSPSVAEAVAGWDVDHITVIPMYPHYAPSTTNTIIEQVDAAAENARWRHKLVRSWGTAEGFIGWYRSRLRDELTAEDVDRVVFSYHGVPQRKVHGPDEYRAQCLATTEAIMAGFDIPHEVSFQSKFGPGAWLSPATVDRMSQLPGEGVKRLLLLTPGFVADCIETLDELDLLNRDTFLAAGGESFRRLAPLNDHPEVGAVLAEVFRTA | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
E... |
A0A1H3HY68 | MKISSTLYSIQQGIKNIWRNKMFSLASIATMSACIFLFGLFYIIVNNFNGMVQDAEENVAITVFFNEGTSKKQIDEIGKKIKKRSEVAKCDYVSKEQAAKDFGKKMDIKQETNSKQDDKKDPKKATNQQNSVSVHNTKDQSQQKATEKKEELPKNSSEIISDALKDSAHYEVYLNDVSMQKSLVKYVKGLDGVRKVNHSKEIAKTLTAFNKLIGYISAGIIIILLGVAVFLISNTVTVGISVRREEIAIMRLIGATDFLIRAPFIVEGIIIGLVGAILPLILLYTLYGKIIDYIRVRFSVINNIVSFIPVGDVFRTLVPV... | Function: Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation.
Subcellular Location: Cell membrane
Sequence Length: 343
Sequence Mass (Da): 38189
Location Topology: Multi-pass membrane protein
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A0A223KTY7 | MNTQKHYFLAVKLPETIKNDFALYTEKIKDELPFQRWVHREDLHITLAFLGYATEEQLHNINKIMPSIAKKYEALSLKLTTLNTFGKKESPRILWYGVEDNSELHALRQDIFLECERLGFSLDKRPFHPHITLARKWKGGNFSEEFLIPFHTINRLFLASEFVLYQTNLQSVPKYEIIHSYTFKEG | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 186
Sequence Mass (Da): 22019
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A0A7K2ZCJ8 | MGVPGDPAALDGVLSPEGLARIAEERELTPTPVGDDVAVGAYVADRLGREVVDRLVEPLLGGVYAGDAYRISMRAAVPQLFEAVKEGGPLLEAVRRIQQRAAARQQTGPVFQGIEGGIGTLPDAVADAVRAGGGRILTETPVLGLTRTDAGWAVRTDTGVITADGIVLATPAWSASALLAAESPAASAELTGVEYASMALVTLAFRRTDVEAYEALRGRSGFLVPPVDGHTIKASTFSSNKWQWVADAAPGLFVLRTSVGRYGEEDHLHREDGELVAVSLRDLRAATGLAARPVDSEVTRWIGGLPQYPVGHHTRVARIR... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular... |
A0A1Q2T5E9 | MKNGSAVLIGGFSGGILRAALGLVVVTPIATLLVNLVGAFLLSFWTYWSIERGAFPSWVNLGVGTGLIGAFTTFSTMSTVTVGLLSTNVVLGLAYLLVTAVAGLAMAGLGFWLAKKVGKAQ | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 121
Sequence Mass (Da): 12393
Location Topology: Multi-pass membrane protein
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A0A5P9GJY5 | MGGGAEMTNEDLIAAAREAARHSWSPYSDYAVGAALLFDDGAVVTGTNIENASYGLALCAETVAVAKAMAEGRRGGLVSVAVVGPEDKGDGAPITPCGRCRQVLNEIAQLGATDPEILCVGGDEVRTVQLSALLPHAFGPAHLD | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 144
Sequence Mass (Da): 14692
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A0A3D3WCV5 | MTKKTIRDVELKGKRILLRAEFNVPMKDGVITNDSRIQAELSTIRYILEQGAGLVIMTHLGRPKGKPSPEFSVEPVAAHLSKLLGQPVQFIPYGDPRSIQQAAKKIKPGEVALLENVRFWEGEEKNDPDFSRLLASLGDIYVNDAFGAAHRAHGSTMGVGYYLPALAGFLMEKEMIALGSVVDAPKHPLVVVMGGSKVSDKMGVIENLSAKADYMLFGGAMANTLLAAQGKDMGASKIESDKLDIAREMMAAVAKGKCKLVFPVDLVVADAFAEDANHKVVDADKVPKDWMALDIGPATVAQWTEIFNQAATIIWNGPLG... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Subcellular... |
A0A0V1PQE8 | MYQSLDIENIIEKMTVLEKAQLLAGVDRWHTAAIPRLNIPSIRFTDGPNGVRGTSFFPGIKSACFPCGTSLGATWDKRMLYEVGELLAIEAKHKSAHVILGPTVNIQRSPLGGRGYESYSEDPVLSGLLAAAIINGIQGKGIAACIKHYVCNDIEDERIAININISERAIREIYIKPFMLALKYANPAVLMTSYSKVNGTHVSQSKKLLKELLRDEYGWGGTIISDWYGTYDTKLSIKNGLDIEMPGPPKLRIPFQVSLQIKSKELHVDDLNDRVKNILKLIDYLKDSYIPEGGTEDENNNTTGTANKLRAYSSNGIVLL... | Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Length: 837
Sequence Mass (Da): 93339
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A0A4Q7K871 | MHNFAILILALATPAFAKTGDGDWGQAYDKAAAALAKLSTNEKISIVVGTNPNGTPGRCIGETAAVPSIAYPQFCLLDGPLAVHAANATVFPAGIQVASTWDTSLMYARGKALGRKIPAAGRNWEGFSPDPYLAGISMANTINGMQAAGVQACAKHLIDYEQDTNRNKLSSNVDDRTNHELYLWPFADAVRANVTSVMCSTNLVNHTLACQNKVVLQSLLKDELDFQGFVVSDWAAHNSTADAVNAGLDVSMPTDAENNSEWGVKRESLAEAISSGKVPVSRLDDMVRRTLAAWYFLGQDVXXXXXXXXXXXVIGEDAVA... | Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Length: 470
Sequence Mass (Da): 49954
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A0A4Q7K6Y7 | MRFSAAFFLGLVSLTTALPSPPPHDTRAVPPPKRSFRKPDSDWNHVISGADVKLSKNYGGQLANYNLRANAVDPAKLSVDKVKQYSGYLDDNSTDKHLFYWFFESRNDPKNDPVILWLTGGPGCSSMSGLFMELGPSHIDKNGQLVPNQYAWNNNASVIFLDQPVNTGFSYSNSPVDTTAAAAKDVYALLTLFFEQFPQYAKQDFHISGESYAGHYIPVFASEILSHKDRNINIKSALIGNGLTDAYTQYAYYQPMGCGKGGYKAVLDDQTCQSMQDALPQCQKTIKACYDGDHSSCVSASDDCDGPLLGAFEQTGLNVY... | Pathway: Steroid metabolism.
Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of lanosterol to form eburicol.
EC: 2.1.1.-
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Length: 880
Sequence Mass (Da): 97826
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