ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A0G1N2F7 | MNIILGIESSCDDTAVAVVADGHKLIGSLVASQVKLHSQFGGVVPEVASRQHLATILPLVDELFQKTKLTRDDIDAIAVTTGPGLLGSLLIGINTAKTLAYLWKKPLIPVDHLVGHIYSNWVSHHIPAQWPLLALVVSGGHSELILMQGPTKFVSVGGTRDDAAGEAFDKAAKILRLGYPGGPAIAAEAAKLKTHPVRNLSTGIKTFPISNGVKNEKLKIELPRPMINDGLDMSFSGLKTALSKIANKFDRAAVAHEFQKAVVEVLAAKTNRAIKKYRPTALLLAGGVAANQVLREKLAQVAQQQKINYYVPELKYCMDNAVMIALAAYFLRKRENNQWYNVKVKTNSEFTEKNSPPARGGVRGGGSIN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
EC: 2.3.1.234
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Subcellular Location: Cytoplasm
Sequence Length: 369
Sequence Mass (Da): 39804
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A0A8T7GR96 | MTSKEMDNTLRLFISLDANNKRPLVDLQNKIILDNKNNSLLKPTAEENLHFTIAFLGQIENNKIIEDIKSKLNEVKFKPFNFHYKGLGVFPSLKFPRIIWVGVDESNKDKMNEIFINVKNKLTEIGIKLEDRCIYVPHLTIFRTNKIFEIEKMVNKYKNETFGSDMIDKLSLKKSQLSSEGPKYSTIHVVNAI | 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: 193
Sequence Mass (Da): 22377
|
A0A1H3CFM1 | MDSYEITACAKLNLFLRVRGILPNGYHSLYSIMQEIDLADSLTINIYPERETGFDIKCIGRNDIDPDKNLCSKAKDRFFSYLRKKEGSIDKIPYIEIVLTKKIPSESGMGGGSSDAAAVLMVLQEHFGNPFTDEELNQLAVNVGADVPFFLYGGTCLCEGVGEDITYLESLAEIPLLIVKPSKGVSTPECFHAIDSKPLPEFDEQRYAGYIESLKNEEKAPLERFLAGDDLLTNDLEIPSLEMLDDIAEAKEALTGTGARFVRMTGSGSAVFAMYDSEDIRDKAYEQLKNDSKFKDCDLFVAKTI | 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-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 305
Sequence Mass (Da): 33853
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A0A968XQY0 | MPRLALKAPVHLYRWTLKPLIGQQCRHMPSCSEFALDALELNGAWRGSWQILGRIIRCRPGGTHGWDPAPDVRNERRWLAPWRYARWG | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 88
Sequence Mass (Da): 10302
Location Topology: Peripheral membrane protein
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A0A2D7A6A8 | MNLTRPIIYTADICDAHPEARVCEIQFKNFAMREDFHGLAVTFSTFENNSGLREILIQGGAGKVLLVDGRASMRRALCGGNIAALAHEHGWAGLIFNGAIRDSHELILLDFGVKAVGVTAMRPRSEGVGRQDEPLSIGGIVIRPGEYVYADRDAVIVLPNAVHERGAKQ | 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: 4.1.1.112
Catalytic Activity: 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate
Sequence Length: 169
Sequence Mass (Da): 18350
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A0A1F3KWY0 | MHFLIFVVMKKIFLPLLTVLLFNISMIANTKLHSDSIDVLHYKITLNFEDYINQQISGNTELRIASKINNLDVFCLDLLKLNVDSVKINSSDVNYTYNDTLLKIQTSGFSANDTFLVTVFYHGHPVTDPSGWGGFYFYSGGAYNLGVGFADYPHCYGRTWFPCVDDFVDRALYDLYIITPFDKYAVCGGTLQSVTNNDTLSKTYHWKLNNSIPTYLTSVAVGDYAAVIDTFNGIQANIPTYLHVRPADTTKAKNSFINLNNILAAYEDCFGPYRWERVGYVGVPFNSGAMEHATNIAYPNACIDNTLYYEELLAHELSHHWFGNLITCKTDSDMWINEGWATYCEEIFRKHVTGHDAFKSHVRARHAEVVRYLHVEDSGYRAVYGLPLDMTYCSTVYQKGANVVHTLENYLGDSLFFSAVKAMLDSFAYNNISSIQMRDFLSQHTGVDLTDFFDFFVFSPGFTHYSIDSFIVTPAGQNFDVNIYVRQRLKGVTQFANSNKFEITFMDSAWQQTSRVISFNGETGNAVFSLPFYPVAVMADLEEKTADATVDNYKVIKTTGTYAFDKAYFTAIVSNLPDSAFLRIEHNWVAPDGFKTPHPSYTLSPNRYYKVDGILSDGFLAKGKFSYNATPSTQLDHELLINTTDSIVIFFRENSSREWRRTKFTKTGNAYVGFLTVDTLYKGEYALATYSWISSLESNTEGTMHLNVYPNPTDSQVTIEYEIKKTGKIEITNSMGKIIYIQNISKGNNKIVWDSRTHIKGEYFVTVYEGKEKISVKKLVLQ | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.2
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Sequence Length: 782
Sequence Mass (Da): 88801
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A0A832JMV4 | MPRGKGAEELLVAVDLGTNKVCVVVAEMGIGSTPQVVGVGSVPSRGIKKGVIVNMEEATNCVRQACEEARRMSNCSFDRVLLTSSALDVGCVFNRGMISLGKDARRVTQDDVKRVVEVAGSVPIPTDRFLVHVLPKEFLVDGQGGIDNPLGMSAVRLEVEVQVITALASSVKNVISAVEGAGLSVEGFLLKPVASAYAVLGHQERYLGTAVVDVGAGTTGVAVFHQGTLRYVSLVPLGGDHITNDIACVLRVPLPSAEELKVRWAVAHQDFVDEDAEIEISMPGSRKSRVVTRRELSEIVSFRLEEIMGMVSEEISKSGVDMLPGGVVVTGGCAMLPYVDEFASELLGVSVRVGYPVGVGGLSDILMQPVYSSAVGLLKASVEVPEALVLGGGGLGSSPRRQVQANRGPSAWSRLKDFVLSILRDFF | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 427
Sequence Mass (Da): 45154
Location Topology: Peripheral membrane protein
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A0A3D2WB79 | MIYTVTLNPALDYVIQVNHFKAGQINRNTSEHIYYGGKGINVSCILNELDVKSTALGFIAGFTGRALSDGLKEMGIVSDFTEVKQGMTRINVKMKSDEETEINGTGPLIEETDFDALKNKIRKLTEGDTLVLSGSIPSCMKSDAYEKIIECMSEDVRLVVDAEKDLLLKVLKYSPFLIKPNNLELAAMFETEIHTEEEIVFYAKKLQEKGARNVLVSMAKDGAILCDENGDVHRIGTAKGTVVNSVGAGDSMVAGFLAGYLKTNDYAYALKLGTACGGATAFHSGLAKREEIEEVLETLQEEK | Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.
Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
EC: 2.7.1.144
Catalytic Activity: ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate + H(+)
Sequence Length: 303
Sequence Mass (Da): 33110
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A0A960F2P8 | MTTPPDTTDTADRAGVVGAGLTGSLLAIRLARRGIPVDLYDRRPDLRINDVDQGRSINLALSTRGLDAMARVGLAEIVQRSGVPMRGRMIHHRDAELRFQPYGTRPEHHLLSVSRDGLNIALLDAVDREPLVRTHFSARVRDVDLHSTSLILENGENSSSVPHEVVYGADGAYSAVRSRLQRTDRFSYEQAYLEHGYKELTIRPDATGGFRMEPNALHIWPRGSHMLIALPNADGTFTCTLFWPFEGDVGFDRIDTDDEILAVFEEQFPDALELMDDLAEQYRTNPTSSLVTVTCRPWHRGAEILLLGDACHAVVPFYGQGANAALEDVTVLMDCLDEHADRAAAFEAFFTRRKPDTDALAELAVDNFEEMRSRVASPVFLVQKRLERALARLFPGRFDPLYTMVTFSRRPYAESVARAQANDTLVRRLAITVLVLLLALLALVVVILVR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3.
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
EC: 1.14.13.9
Catalytic Activity: H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + H2O + NADP(+)
Sequence Length: 450
Sequence Mass (Da): 50187
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A0A554KPY1 | MGTKWVPLEERLTEGLTFDDVFVIPHRSRVHPREVDITTELCRGIRIATPFVSSPMDTVTEEKMVIAIELFGGAGVLHKGMRGSRLKEALTTIKRFMAGQIKNPIKATPNQTLRAVKAMNSLYTGFPVVSFEDGDKPKLLGIITRRDMDGKEPGSLVRDSMTPRERLVVADPSISFDGALNLMRLHKVEKLPLVDSNDYLVGLVTRRDLDRRLKHPKATVDSQGRLLVGVAVSGANPESAVEHVKELIPLGLDFVVVDSAHGGNSAIIASTLSLKNTFSDLPVIAGNVADRSSAEGLVEAGCDALRVGVGPGSICSTRIVTGIGVPQITAVAECRGIVESLGSSVPIIADGGISQSGQVIKALAAGASTVMLGNLLASTIESPGEVITRGNQKFKKHRGMGSAEAIKKYGGDRYFQDGDGESEAVIVPEGVSGTVPLRGTVSELLAFFSVALRNGMGYNGAKTIPDLWEARIVKVTAAGLREAAPHDLTSIESETSTSKQEIGG | Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
EC: 1.1.1.205
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Length: 504
Sequence Mass (Da): 53519
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A0A533QT30 | MRGLIVEKGGLTAHATILARSLGIPTLVQVPEATAKIRAGDLVIVDALAGRAFINPQADILRKYDQVDANLKAHQGVLKGLIGLPTVTHDGVEIKLCANIGQTADALAAANVKADGVGLYRTEFVFLVQDHFPSEDEQYQFYRATAEHLQPAETVIRVLDVGSDKPLSYFPLPREANPAMGFRGIRLLLAHPTLLHTQLRAILRLSASHPVAILLPMIDGIDELRAAKAAIEHAKEELAAAGQSFAPLIPVGAMIETPSAAILIEHLADEVDFFSVGSNDLVQFLLAADRIRGEMKSTYDPLHPAVIQVLAKLATVARRKGTPISLCGEIASDPTYTNLLIGLGFRSFSVSPGRLLDIKHAIRSTDLQQAEKLAEQVLSVHSTRDIRAQVQDDWNRRRPVASPEFNGPTGPVGTSLAVRHNVARQRFEAQAGESAPAFLSYRGEGERVILKHTFVPDALRGQGIAADLVRVALEEARQRHWKIVPRCSYVAGFIERHPEFCDLVDRQEGNLD | Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 512
Sequence Mass (Da): 55767
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A0A9E5DYB7 | MIKLFLIAIGGGLGSLARYGLNGFISEHQTKHFPLPALFPVGTMIVNVTGCFVIGVIAALSDPPLGRGGIKPEWRDFMMVGICGGYTTFSSFGLQTLNLAHDGEWLWAGANVIGSNALCLLGVYLGWVCGRFIQAKLHGGTL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 142
Sequence Mass (Da): 15068
Location Topology: Multi-pass membrane protein
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A0A7C1YSZ0 | MSCRRPARSWVPSSMSSPAEPSGPVPTSESRDLLQESCRGFFAELLAHGVEAVVASPGSRNTPLLVAAARTPGLDLQIHLDERDAGFVALGRARASERPVVLVCTSGTAVANYLPAVVEAGHGGVPLIVVTSDRPPELRGWGAGQTIDQNGIFGPNVRWSAELAVPGPAVDPGWYRRVAARAFVSATDPDPGPVHLNWPFREPLGPQPGTTVPTPPTDPLVRVTPPGPYSRPFEVVRLAELAADHELGLIVVGPLDTDPATAEGIRELSRATGWPLLAEPTSKLRFVDPADSGEPCPVIGAYDQILRSARWADVHQPDVVLRFGSSPTSKPLRLWLERHPPDHHVLIDPHRRWNEASFTLTEVLAGPPGELCSAATRRLRSLDLAHGTTSWTRSWVRAETSAQAAIDAVLASEPLMEAGIARVLSDNVPSGASLMVANSMPVRDVDSFWRPEAACRAVYANRGANGIDGLTATAVGLAIGGGHRPVVLHIGDLALLHDLGALPAAVAAGVDLTVVVPDNGGGGIFSFLPVTELVDGHEFERLFHTPPGIELSDLGRFGGIEVYEAGSATELAQLLGRSIATGGVNMIRVRVDTAANVDQHRRITAAVAEAVRGST | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
EC: 2.2.1.9
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Length: 615
Sequence Mass (Da): 65026
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A0A7C6CWM1 | MNKSSFIEELEKRSIRCSESQLAKLWDFMYHVLKTNEQFNLTAIKDEETFVEKMIFDSALLLLDNRLENQDILDIGSGAGFPSVVLAILSPNSRVYALDSTTKKVEFIKLYAEKNNLENLTVINERAEDYAKTHREQFSFVTARAVASLRILIELAVPLLKVGGSFIAMKGLGFEKEVNESIDAFKELNCKIDYIYEDVLPQSKESRSLIFIKKTRKTSKKYPRTFSEIKNRPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 234
Sequence Mass (Da): 26877
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A0A2E6VXN9 | MIPKSTNIRRARQEISLHKRWEKNSHASGVIWFTGLSGSGKSTLASELEQLLFDRNKQVVSLDGDDLRYGLCADLGFLPEDRAENIRRVGEVASLFSASGAIVLTAFISPYRADRLKARKAAVGNFHEIYLSADLNTCIDRDPKGLYAKAQRGEISHFTGISAPYEAPESPELTLDTGLLDVKKSLKILDEYVEKAFSL | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 199
Sequence Mass (Da): 22045
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A0A663DKG7 | TATGCVSKIDADKPQVTGQVLFRQHYSHGRLEAIFYLDGFPLDNNQSGRAIHIHELGDLSNGCDSTGGHYNPFGVNHPRHPGDFGNFFPKEGKIRKYKTNLFATMFGPYSIMGRSVVIHEQEDDMGKGNNKASLENGNAGKRLACCVIGICNKNLWEEKLSEKCVSLCRVSFL | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 173
Sequence Mass (Da): 19150
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A0A7Y2ICN3 | MLLLAAESAEEAANPILPVIPEMFWGGLMFALFYLLMRYVLLPPVQRTMEDRDQALRDEWDAAKAAEAKVANADAVVADALAPARAEAAQIIEAARLEAEAERSQIIGGAQTEIDAMRQLATAEIDAARTEAMSGVGSHVAELTAQATSRVINRPVDAASAMGVVNRIISERG | 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: 173
Sequence Mass (Da): 18472
Location Topology: Single-pass membrane protein
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A0A663FI25 | MHACVGAQVSGSAPHKGTRHRDLPTPPAPRNLGIRVSSLTRTQAGRVSPPPPKKDQASEHFPPHLSQGCPLPQRDKATGLPPPHLASTASTCCQDGGHGWRGVPTPVPPPHPLLFFFFFFFHPPPVPGYLNRLRVHNAEVLHELVERRGPLTPLLTLSNHQSCMDDPHLWGSLKLRHVWSLHKMRWTPTAADICFTRELHSRFFSLGRCVPVCRGDGVYQRGMDFILEKLNQGDWVHVFPEGKVNMGQEFVRFKWGIGRLLAECRLDPVILPLWHGGERGRITVVVGRPFSVRPLLERLRAEGTSTVSARGAAPRQRWGAQNYVSQAGQEQNCLQPPRVGTWQSCG | Catalytic Activity: 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-3-phosphocholine + a cardiolipin
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 346
Sequence Mass (Da): 38569
Location Topology: Peripheral membrane protein
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A0A2W6BDE9 | MDEANTLQALLRAATIQLGSAGVPPARVDAQLLVAHVMGISRSELQRLAVLGDTCLNATQQAQLAELVWQRSQRVPLQHLTGVAPFRRLQLRVGPGVFVPRPETELLAGWGIERLESAASRLATHVVDLCAGSGAIALALATEFPGAQVSAVEREPEALVWLRRNVADRRPSAGFRVEVVAADATAADTLAELNGTVDLVLSNPPYLSPDEEVTKEGLLDPPSALWADDTGLSVIEAVAARAAVLLRSDGWFGVEHGENQGDRVRALLHSDTWRHVETHLDLAGRDRFTTAQRL | 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 factor] + S-adenosyl-L-homocysteine
Sequence Length: 294
Sequence Mass (Da): 31633
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A0A961CC92 | MQATVTRVPLRDRIGGFVALTKPRIIELLLVTTVPTMVVAEQGLPSAWLVVATVLGGTLAAGGANAIXXVDRDIDALMERTRKRPLVTGVVEPREALVFAVSIEVLAFVWLWGFVNLLSAVLAVSACLFYVFVYTLWLKRTSTQNIVIGGAAGAVPVLIGWSSVTDSLALAPWLLFGVVFFWTPPHFWALAIKYRDDYSAADVPMLPSVVDHHTTAVRIVRYSVVV | Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Membrane
Sequence Length: 226
Sequence Mass (Da): 24594
Location Topology: Multi-pass membrane protein
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A0A960NFP3 | MTATARPATESEKLPAERQPGQSPDELVHIGERRVDALEIEWIVYDSDRIDRRLVPNPSDIPSLLRDTPDGMTQWLRVTGLHEVEAINQLADALGIHPLARQDVLNTHHRPKVEQYEDCLFVTVKLIGDPRTYVEDEIGTEQLSVFLMPRLLVTFHESHSTHFHPVLERLQQGNQRIRQLGAEYLAWAVLDVAVDHYFPVIDWLEDRMDHLEEQLFEGTEKVEAHDIFVCRRQATTLSHIVRPLRDVSVRILRMDSPLLTKTTEPFFRDLADHGGHLAAAVESLREASISLRDFHSIALSNQLNEVMRFLASFSALFLPLTFLAGIYGMNFESMPELKKPWAYPALWCVFAIISACMFFFFRKKRWI | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 367
Sequence Mass (Da): 42287
Location Topology: Multi-pass membrane protein
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A0A1H3FX01 | MIYTITLNPAVDVSLHVKDGLMPGSINQSYGVRTDPGGKGINVSKTLKVLGKESVVCIGICGDDGDRLLKMLGDVGTEVISVRYPSGNTRINVKINGENGVTTDINGEGPLYDKGTVDELKTLIRSRIVTGDTVVISGRPPLGSPSMIYADLIKCFKEVEGVKVILDASDRYLQEGLEERPYAVKPTCEELGIDNDTDSAKYEASDLVMRGVTRCLISMGSVGAVYCGRDMEATYARALDVKVNCTTGCGDAMTAGLAYASEEGLSSEDTLKLCMALAAAEAETEGTNPPLRARVEELAGISPLLGQ | Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.
EC: 2.7.1.144
Catalytic Activity: ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate + H(+)
Sequence Length: 307
Sequence Mass (Da): 32537
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A0A3N2DQU4 | MAGRIPQGFIDDLLERVDIVEVIDARTVLKKAGRNYKGLCPFHDEKTPSFSVNADKQFYYCFGCGAGGNAVSFMMDYERLDFPQAVEALAASISMQVPREEDTAVSIAASANKALYALLEKCAEWFHQNLRLEAGGQPAVDYLKGRGLDGQTASNFQIGYAPPGWDNLLKKFGDTPDQVKLLIEGGMLIEKDGGGCYDRFRERIMFPIRDHRGRVVAFGGRVLGDDKPKYLNSPETSVFSKSRELYGYFEARKSKQAVERIVVVEGYMDVVALAQAGIPYGTATLGTATSSSHLERIFRLCPEVVFCFDGDKAGRAAANRALESVLPLMRDGLQARFLFLPDGEDPDTLVRQVGADRFEHQIESAQPLSEYLFEHAADGLDISSMDGRARLSTLALPMIDSIPAGVFQSLLHKELATRTGLEAETLEQIRLQAKQSQQQEQQRKQQQDRRAEQRYQQQRDGSTATSQPKQGADNTSTAAIEGADEAIGYLNAEQANDYNNYQLPDGDPYADAHNSYRDDDYTGRSYNNSSGGYRRKDGDKPWKKDRGPKQRAPRSELPQPRCKIQQAITLLLFYPINIDAIHSAEVLDQHPGPDSLLLKEMVEFLKKQPDTPTYTLLGNWIGTEHYGRLQQLLKDDQLITDQLGAREELADIFAFLDKRQSRSQLEEELNQLAAIPFNEMSREQKQRYGELLLTHSKH | 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: 698
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 78203
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A0A0G1Q654 | MNFLRQIKIFLWEITKLTVISLLIVGPIRYFVIQPFFVRGASMEPNFYDRDYLIVDEISYRFSEPKRGDVIVLKYPQDTSQYFIKRIIGLPGERVKIEGGIVKIFNRNQPEGFVLDESAYLRGRITRGDLDASLGSDDYFVLGDNRDFSLDSRRFGKLSGSYIVGRTWLRAWPINKAQAFETPNY | 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: 185
Sequence Mass (Da): 21524
Location Topology: Single-pass type II membrane protein
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F8L5V9 | MSLEGYKVITAREMARIEKLSIQEGASDEGYMLKAGAGIAERVALFIKEKRLQKRVTLLVGKGNNGGDAFVAGTLLLKKGYIVQAYHLFPTEESSPLCQKHKQAFTDAGGLVFFPKKAAEISCKGVLLDGLLGTGFQGQLEGILLDTVEHVNRSKQPILAIDIPSGVNGNTGEVNPIAVNAAETIFLGLPKIGFFLGEGYNYIGKLSPVDFGLELRYVHQACGMAHMLNEKNLPSLLPELTRTRHKYQAGYVLAVSGSPGMPGAAMLTCLAALRAGAGIIRLFHPMGMENELLHAPYEVIRTPYKDDPAALLLEMSRAAAMLIGPGLGRAQERGTFLKSFIDHITVPTVIDADGLFHLKGMFAKFPFPCVLTPHHREMLQLLGKEKFDDMFDECQKFAHENAITLVLKGAPTFIFHKDKPPLIIARGDPGMATAGTGDVLTGMIAALLAQKLPPREAAALGVYMHARAGECVAEMNTSYDLIASDLLEALPRVFKELSDLSLM | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 503
Sequence Mass (Da): 54441
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A0A2M7J8B5 | MIIELIHGLLVTFKHLFTPSVTIQYPTQRRPVAEGFRGLQRLNVDENGQLLCVGCGLCARYCPAEAIKITTIVMDEPNAQGCDKKVESYIIDISRCIFCGLCVEACPKDAIRMTDCYEMACYNRDKMIYDIEGLTKEPGVTRYK | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Subcellular Location: Cell membrane
Sequence Length: 144
Sequence Mass (Da): 16265
Location Topology: Peripheral membrane protein
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A0A928A8E6 | MIYKGLVIRLIAGEYLVYDLNSKEILNAKPRGVMRIKSSAPKVGDYVDYTLTDDGKGVIERIHERRNDLIRPYISNIDQAFVIFSVKEPDLNLNLLDKFLVTLEFNNITPIIVFNKWDLLSYCEIDETKKVISYYESIGYKTIITSCSKNLLNDLKDYIKDKISVFTGQSGVGKSSLLNLIDPALSIETNEISQALGRGKHTTRHVELINVESGWVADTPGFGTIDFEGMEKIDLAQNFIEFFKYSSLCKYNGCLHINEPSCKVKELVLEDKILKSRYENYLAFINDLGKDKKEYDSSPINSNSKRRRKR | 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 catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 310
Sequence Mass (Da): 35468
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A0A960IWU8 | WAIFLRNHDELTLEMVSEEERDYMYRVYAHDPQMRVNAGIRRRLAPLLGNDRRKIELLNGLLLALPGTPVIYYGDEIGMGDNVYLGDRDSVRTPMQWSPDRNAGFSTANPQKLYLPAIIDPEFHYEMVNVEVQQAHENSLYRWMRQVLHVRSRHPEFGRGTLRMLLPDNPRIVAFVRSHEDAHVLVVANLSGSAQYAELDLADHAGARPVELFGRTEFPPVGELPYLVTLGPYAFHWFSLSRQETDAPVQGAATGGPVPVVDVDGPWTSVFEGKARRALEALLPAQLVQRRWFPAKDRAIASVRVADTVPLTARTAAVPSFLVLVQVRFREGEPATFAVPLAIVGGERADALRSDLSLGVVAELHRDGERRVLSEALWEPQAAHALLDRCRSRRPRPGGSGALLGSPTPALRARAEALADQEPTVLRGEQSNTSVVFGDQAILKVFRRLEPGVNPDLEVSRFLNDRGFEHVPPLLGAVEYQADRREPTTIGILQGYVPNEGDLWQHTIDALGRFYREAFDETPPAEPVGHPLDRVLASDDGGDAVADLPDVAVVSTGAHLEVCDLLGLRTAQLHRALASPGDDPAFGDEDLSLLDQRSLHQSMRSAAARTLATLRRRLDDLPAEVGAPAAALLEREGALLDRYKPLRVSRLGGRRIRTHGDLHLGQVLFTGRDVVFLDFEGEPLQSITERRLRRSPLRDVAGMLRSFHYATLVALRREEERGLLASGSEAAWRAGAWARSWYGWAASRFLGAYLREAGDAGFLPADPAALRTLLDAFVLEKAVYELSYELANRPDWSWIPLSGLLDTLAAGEGP | Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.1.175
Catalytic Activity: ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+)
Sequence Length: 814
Sequence Mass (Da): 90086
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A0A1X6WQ98 | MSIYTKTGDKGTTSLFDGQRVKKYSTRVDTYGTFDECNTCISIAEKFCQKQENKEFLIHLQYKIFQLSGEIATMNQQKFQNKSEQISAIDIQELEEKIDEYTEKLPKITTFILPGTSLAGAHLHQSRAVCRRGERMLVLLSEEEEIRSEVLQFVNRLSDCLYIIARDEDHIERKEEQVKEIIRRYYEKECESVE | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate
Sequence Length: 194
Sequence Mass (Da): 22738
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A0A061II52 | MHVGSVGGSDLTPCKTLNDSVKCPIPSSCGAFCAVKFAVSIGYWHDPYIEHLVRQSKERKAPEINRDGQMLDSKRYAIIGADLRDLSELEEKLKKCNMNTQLPTLLITECVLVYMTPEQSASLLKWAASSFETAMFINYEQVNMDDRFGQIMIENLRRRQCDLAGVETCKSLESQKERLLLNGWETASAVNMMELYSGLPRAEVNRIESLEFLDELELLEQLMRHYCLCWATRGGQELGKRVCVFSQE | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 248
Sequence Mass (Da): 28189
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A0A9E5DY61 | MLDGWMISHDTVTPSGGRVRSKARSGFSGVPCEARTNSGATPLRRLRGSLRTPAIQIHGIDSRPKRRGYFLLRSRSTLPFFHSSPLSLSSAAMRVLGIEGGGTKTSAALLDGSGRVLARARAGVSNSKLLTESELAAVFRTIQKQIGKFPDVVSICLAGAIASSDHKKIRTVAGKVWPKAVVHTATDRESALMAGFGKLEGIAVICGTGSSTFGMHRGKLAKSGGWGHMLGDRGSGYDIALQGMRAAIRNYDETGKVGKLASAFLQSLRFNSPEELIPWVQAASKADIAAAAVTVFRAAKNGDPLAMRILDFAANELAESVRIVAEKLHWKNPNVCLKGGVFEHQPEFFRSVRKGIRKLLPRASVHAPKYDGAVGAALLCVVGRVPPRGGEGRPTPAGGSGPTPMKDVATALTEQRNPRTLAIDKKSVAQLFDVMMNEESRTIPAIRKQKRDIVRCIETIVASFRRGGRLFYVGAGTSGRVGVLDASECPPTFSVPPDMVQGILAGGQRALYNSVEQAEDDPHAGTAAMRNHGVGKRDVVVGIAASGRTPFVLGALREASDRGAKAFFLTFNPRSAIRDPRYKTIAVATGPEVVTGSTRLKAGTATKLILNMLTTVSMIRLGKVISNLMVDVKPTNEKLRDRACRIVMALRKCTYQTAWERLEHAKWNVKKAAQTH | Pathway: Amino-sugar metabolism; N-acetylmuramate degradation.
Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
EC: 4.2.1.126
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 676
Sequence Mass (Da): 72508
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A0A960XHW1 | QGGRETSVRQLVSRVANSIADWGLIDGYFGSREQAEIFNRELTYLLIHQRAAFNSPVWFNCGLHHTYGAGKDGDSGNFYFDLQRNKVARVSNQYEYPQSSACFIQSVSDTMESIMELAASEARLFKYGSGSGTNLSSIRSTREKLTGGGTPSGPLSFLEIYDAVAGAIKSGGKTRRAAKMNVLNSDHPDIREFIGAKLKEERKAWALIEEGYDSSFSGEAYNSIKYQNANLSVRAQNDFMQAVEADGHIWTKAVRSGEKIEKLRARELLHAIAEGTHVCGDPGIQFDDTINAWHTCKASGLQNCSNPCSEYYFIDDSACNLASINLMPFMENDSFDVEGFSAAVRVMIIAQEILVSRSSYPTEAIAYNSHWFRPLGLGYANLGAMLMTQGLGYDSEKGRAMAAGITALMTGEAYRTSAMLASGAGAFPGYLNPRAFGGPEQTAETNADCMLDVIRKHRKALDEISNTCPDNVLLAARERWDQALEMGEEHGFRNAQVTVLAPTGTIGFFMDCQTTGIEPAFALVTYKTLVGGGFLTLPLLTVKPGLEKLGYHGEKLKKILKHLEDYGTLEPVESQGQLKTSGIREEHLSVFDTASQSGQGKRFLSYRGHLQMLAAVQPFLSGGISKTVNLPRETKIEEIENIYLEAWKLGIKGLAVYRDGSKRSAPLSTKKTQNEEKPGKQVQVVTEPYRRHLPDTRSSLTHKFSIQG | 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 Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 708
Sequence Mass (Da): 77857
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A0A832EUR6 | MARRAPGATVSDQLDADRRRGDQISARTVVAGVIGDPVRHSLSPALHNAAFQALGLDWVYVAFPVAAHDAAAAVRGAVALGVQGLSVTMPHKQAAARGADQRSVAVERLGAANTIVVRSGVTVAHSTDGGGLLDDLERALDFGAAGARCAVLGAGGAARAVVLALAERGAASVVVVNRTAAAAESAALLAGRSGRVGTLADVAEADLVVNATPVELVSPSSGATAGAALGRGQIAVDMRYSPPTTRFLDEACARGATVRNGLGMLVHQAARQLVLWTGEDAPLEVLFEAARRATEGSAPVG | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 301
Sequence Mass (Da): 30293
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A0A971FWH9 | MARAGRAGERSAVEVAAGRVDPRPPRLPRDGHQRLRRHADRPGEAARRRPRTGTRDRVGARPVSRVRRRRHLHRGTGPAPSILLVAARDSCPGRRVPRATSGGGGAGRHHGSVSSARLVLASASPARLTLLRAAGIEPDVVVSDVDEDALTAEVGTDDPDVVVAALARAKAEAVAARLANPVAARVANPVAARPATGPASGESERGDGRTLVLGCDSLFTIHGRTWGKPSGPEEAIERITSMGGSEGVLATGHHLVDLRDGRAVGGVARTTVRFAPMTGAEVAAYVATGEPLRVAGSFTLDGRSAPWVEGVVGDHTNVVGLSLPLLRDLLGRLGVSVVDLWDRSEVSP | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 348
Sequence Mass (Da): 36259
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A0A8I0AIG3 | MENTRKIYFKSKKKFLKYALLKEHEWYLYCFQKKLRAEENASNIFSKFIYRLSKNRLGSKLGIYIPAGVFDEGLHIWHYGNIVVNAESRVGKNCMLHGDNCIGNNGKTEGCPIIGDNVDVGTGAKVLGPIRIANGVKIGAGAVVVKNCLTENATIVGIPGKEIRRK | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
EC: 2.3.1.30
Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Length: 166
Sequence Mass (Da): 18474
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A0A6P6PHE2 | MIQEPHNVPPSSAALGRISLGRSLRRRQRRPTWTPTTTSRAKSPRGRALPASLATNRSLVANLAAANCYKKEKHLDLEENWKLVEKAQVYYIAGFFLTVSLESILKVAKHASENNKIFCINLSAPFICEFFKEALMKVMPYVDILFGNETEAAVFAQEQGFEVSGWRITP | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Length: 170
Sequence Mass (Da): 19112
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A0A3D4VQR7 | MALLKVESVESAVLSLRSFIEHHYLNRTEVIPLLRSQNRIVSETLFCVEDNPNFNRSTVDGYAIFAHESHGASENLPTVLNCVEQIEMGKAAVSELRPGECAYVPTGGMLPKNANAVVMIEYCDVFEGNQILVYQSVSEHENVVLKGEDMRQGSPLLEVGSRMSFKEIALCAQNGITHIPVYQNLKALVISTGDELAEIHEALSLGQVRDINRLMLIELLKQVNIDCVEQQLVRDDFDGLKATVDLWIDQVDLVILSGGSSQGTKDYTQRLFESYGSEALWLHGLAIKPGKPTLLGSWHETLLIGLPGHPLSALLVYLNVVQEALIQAYQIKKQKPILAKLATNMPSAAGKDTYLLVNLERHSDYYEASVCHTKSGLIQAFTHANGYIHLSKDTEGAHQGTWVEVFPLTL | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 410
Sequence Mass (Da): 45362
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A0A950GYM3 | MNRPAVRLRLATRGSPLARRQADRVAERLAARGVETSVVVVETEGDRRSTVPIDRLGGRGVFVREVQLSVLHGEADAAVHSAKDLPASDDLAAGGLVIAAIPERADPRDLLVGSTLHGLPAGATVAT | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 127
Sequence Mass (Da): 13258
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A0A1Y1SBV4 | MKISYQWLSEWAETKLSAAQAGEVLTMAGLELDDLEPAAPALDGVVVAEILNAERHPDADRLQVCSVDAGQDQPLQIVCGAPNARPGIKVALATIGTRLPGDFKIKKSKIRGQESFGMLCSGGELGMDETDGIIELPQELTVGSALSDALALDDSILDIALTPNRGDCFSVRGVARELACLTGVDMTRPFDASAPLVSLEDKPVIRIEDAADCRRYAGRVVRGLDRTAATPLWMAERLRRAGLRSINPLVDVTNYVLMELGQPMHAFDLSKLEGDICVRRARAGETLTLLNEQAIELNEQSLVIADKRAPVALAGAMGGLDSSVDEKTTDVLLESACFTPRAVAGTGRRFKLSSDSLQRFERGVDPSLQELALDRATNLLISICGGQAGPASIEEATAWTPPQIELSAQRVQALLGSPVAPEAMVDILRKLECTVTSDGALLKVTPPSHRYDLNEAIDLVEEIARIHGYDNLPGRERRVGVALSAPRADAASRIRRELVARGYHEAVSFSFADSGTDDALNGDSALAPVMLDNPMSAAMAQMRRSLWASLIPVWKHNAARQQERIRLFELGRKYGKRDDRIEEIECVAGLISGLAQPEQWASTKRNVDFYDLKADVTALLGDKAEALQWSDQNPHPALHPGRSASLLLDGECVGVLGEIHPRLKKPLDLPHSPLLFEIQRRVVDTLELPKLSPITATPSSRRDLALLVDQTLAAENLIQYVKKQAGDILREVRVFDVFTGDALPKGCKSVALGLIFQDFSRTLTDEDVDAAIQKLTSGLEREFGAQIRD | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 789
Sequence Mass (Da): 85657
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A0A2D7A6Q8 | MFVSTAYAQSGSGGGGLEALLPLVLIFVVFYFLLIRPQQKKMKQHREMLAAVRRKDTVVTGGGIVGKVVKVDNDVELTVEIAKGVEVKVRREMVSAVMSKTAAVSGSAANEEKPRGGFLGSLFGGGAVQKAEGVSSADDKNTDSQSDNVSSDEKKKKTD | Function: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
Subcellular Location: Cell inner membrane
Sequence Length: 159
Sequence Mass (Da): 16835
Location Topology: Single-pass membrane protein
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A0A2E5MZN8 | MAPRKNSKTGPLSNTEVDSFMTSVGPFENKPHIAVAVSGGADSLALTLLCNNWVKKRGGKLSAISVNHDLRKGSDDEIKQLGEWLAVHAIEHITLNWKSKKPRNGLQDAARIARYNLLESWCRENEVFHLLLGHHQDDQAETFLLRLAHKSGIDGLAGMSSVIEKSHVRLLRPLLTIPKSRLYATLEALTQPWLEDPSNKNEDFERVRIRNLSPKLSELGLTREKICETADCIAHARIHLEAEASKLLAKSCYVGSAGYVCFDAAILFSGPREILLRALTRALLCVGGGVYPPRLVKLQGLYKKMRSALKNSNGSWKGATLAGCRILLTISKSGAMIFLLCREERSLPESMKISDSLIANWDNRFQLYLTGLNLTDNTNLNIQPLGRKGWSDLCREFPSIINSHVPHPVSFTLPTLVDNHGILAVPNLNYRRANMVLHGLDSIRAIFRPRQTLSGSGFSVAK | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 462
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 51246
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A0A520XI04 | MFNFIADVLAFFYDLFPSYGLAIVGLTLAVMIVATPLTLKSTKSMLQMQRLQPELKEIQNRYKDDRQKMNEELMAFYQDNGINPLGGCLPMLIQLPIFLVLFRVVQGITRRATDIGSQMGWPAGRLSGGGELDPSQITRVERTFDP | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Subcellular Location: Membrane
Sequence Length: 146
Sequence Mass (Da): 16461
Location Topology: Multi-pass membrane protein
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A0A2E3L570 | MSKNNIPELLQVAIQAHTAGDNSVAEKYYMMILDKQSDHPDACHNLGILLAKTNTERALLLLKTALEKKPNHGQFWVSYIEVLILAKQKAEAINTLSKGMQIGLKGERVDQLAQQLGVDESSGSEPGVDDVLHLYNGNNFDGVLEKGISLLERDPNNEILLNVLGATYQKLGRLDSAVEHYTKALTINPRNYDIKNNLGLALKDLGRLEEAALYLDEVLRDNPNYADAYINLGLIYLNSNKFREAVPLYEKYLEIVPDAYGVRINLGLSLNEIGRTKEALEQFDMVLKESPISHEAYYNKGGALLKCDEFDAAADTLKSAILLAPDLFLAYYNLAKSLSNQQKVKAEATTLKYATKLVQNYPDLWNNLALNQEKQRDRYGCIYSFKKALILDPTDPKPASNLSGVFFRLQNSGESLKQILRALSIDPMNQLFQDQYVYSASQAAIGEGNLHKATLVRSKLGVITFDLDNGITLSDGGRK | Catalytic Activity: L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP
Subcellular Location: Membrane
Sequence Length: 479
Sequence Mass (Da): 53304
Location Topology: Peripheral membrane protein
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A0A2E6W101 | MVTRRSFVAGNWKMNGLKKDGLSLAKSLVSKVKKLDNSNVEIVICPPFTLLATTGSALKGTKIKLGGQDCHFSNTGSHTGDISASMVKDAGCKYVIVGHSERRINHREGNDIIKKKAEAALLNGLTIILCIGETLNQRITKKTQTVIRRQIVGSLPKSSRSKNTIIAYEPIWAIGTGKTATPSQAQEIHKFIRYQLVKCIGPSESKKMRIVYGGSVKPENAKALLGQPDVDGGLIGGASLVSSDFFSIIQSCS | 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: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 253
Sequence Mass (Da): 27226
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A0A832JNT2 | MKGLALEIALKVVEGNPLSREESEELIGEILEGGLDEALAGAVLASMRLRGEEVEELIGGARALLSRCVPLKGLEEAFDTCGTGGDRKGTINVSTAVALVGAAAGIKVIKHGNKAVSSRCGSAELLLSLGARLEMSPEELSECVSSVGFGFVFAPLYHPALGRVSDLRRRLRFRTMFNLLGPLVNPARPIYQLVGVSEPRLVEPIAKALKELGRRRFMVVHGGGIDEISLWDSNLVLIVEGDKEERLVLEARDFGLRNCSLSDVQGGSPEENARHIVSVFEGRGGPMRDLILANASALMVLAGLAGDFVEGTAIAAEVLDSGLAMRKLSDFLSFSGRLGR | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
EC: 2.4.2.18
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate
Sequence Length: 340
Sequence Mass (Da): 36185
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A0A1Q9N437 | MDLKNKKILIEGIGGIGGIIASRLLAVGYDCTLITGNKEITSQIQSSGIIEHLENDKQKIVFPQNVYTTLSELDETMKFDFALLAMKAESVVEAAKSTIPYLFSHGFVVTLQNGIVEDLIVKEIDDGRLISAVMAFGATMIQLGQYKQTSPGSIFIGELHGELSTRLTQLGEILHEVLPVSLSENINGVLWNKLAINATAKALGAISGQTWGEMLDTKPKRTLFLKIYAEVVNASKANNVKLEKITVNPLLLYLPVNAGFFTRFKKDIFLRMAARKYKDIKSSSLQSLLRGRKTEIDYLNGFVISESEKHGLKAPFNKILLEMVKEIENGKREIDPKNIDEIIQKLVV | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Length: 348
Sequence Mass (Da): 38583
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A0A7X0VX13 | MSGEDRREESAKLNETKGEERRETEEEAPTEGSAGTSAEGAGTTPTDAPAEGDNREDVPSAEADSGAAGAGADPNGRKPEGEEQASAPKQVQAAAEPKTGPVDAKQAAEGEPAAPPAKAAEEAAAPAASSAGGEAPVRRQETDEEKAARRKAALEAREAAKAAAAQGAARPEAAGGAAAAGRNPAAAAGRAAPAAADAPPPPPSPNQPRLDRAAQLLRELVNEDAVEEASINEPNDHLPTLVIKRDRWQACAGLFRSHPELNIDYLRNVAGVDHETHMEVIYHLLSLDSGHNYAVKVRTDRESPSVPSVTPIWPTANWNEREIYDLLGIDFPGHPDLRRIMMPDDWVGHPLRKDYAPLDPEV | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 362
Sequence Mass (Da): 38092
Location Topology: Peripheral membrane protein
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R7C215 | MSDSTFTPYPVKPAVIGDVTVGNGPVRTLASLTSSTESGLLEEQHTLGELPVDILEWRLDHFEQITKQSLISAAMSLRAHANKPILGTLRTINEGGACEISDENYRDLAVFFAGTKFLDAMDYEIRRGEAQAAAKAAHDAGMPVIMSFHNFEKTPPAKEIRELFAEMAAAGADILKIAVIPKKPEDVLLLMQETLAARKKHGLPIISIAMGPMGAVTRAAGRLFGADATFVAGTEASAPGQLSAEESTKLLPLFDPFTAA | 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 (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 260
Sequence Mass (Da): 27776
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A0A357R0F7 | MYTVILMKTYTLTASEVLIRKIEHVYEDEIVDKPIPYGRLFIKTEGASLTVYTSKKIVIQGPNADQVLQIIEGLSDERLAIKTAETKGETNKVKTASQYSTFFAHAGSDEVGTGDYFGPIVVCAAYIDSENSVSDLPIRDSKQMTDDLVMTLGPTLMERFKYSVLILDNVKYNQMHQRYNMNQLKAILHNQAYIHLYKKLNFKPKSIIDQFTPETSYYRYLQDQKEIVKPLTFETKAESKYLGVAIAAIIARYHFLISLQKLEETFQVKLVKGASAAVDQAAVEIIKKHGMQTLAKVAKMHFKNTEKAKEMI | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 312
Sequence Mass (Da): 35443
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A0A940D6Y2 | MKIFNVVAFLFALTLLTGCNMIDSENSGSWFLNLFVNPFSVGIEGMATVFNGNYGLAIIMITVIIRFLLMPMTLKQQKQSKLMKEKLDVIKPKLEEIQQELQKATTPEKQKELQLKTVQLYQQHGVNPLSIGCLPMLIQMPILMGLYYAISHSENIASHSFLWFDLGSPDLLLAFIASAVYFLQMHLSLRNVPKEQQSQMKIIGFISPLMIGFISIGAPAALPLYWMVGGIFLIFQTLIAQKWFLTSRNRSENVQ | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins.
Subcellular Location: Cell membrane
Sequence Length: 255
Sequence Mass (Da): 28853
Location Topology: Multi-pass membrane protein
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A0A1H3CAU7 | MEKSVVKTGATVDEAIEAALTELGCTKEQATIEVIEEGTEGGFLGLGRKDAQVKVTVNAEDAAPSESTEADDTYYGDDENFEGDAVSEAEDAAANFVAEVLSGIGIHGNMDSYREDDTIFISVTGSDCGAAIGRHGETLEAISYMTNLIANKHSEQRVHVYLDVGGYRKHREQVIKGLADKAVSRVRRSGRKVTMEAMSPAERRIVHSYLQDVNGVTTHSEGVEPNRCVVVTPEEKK | 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: 237
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and R3H).
Sequence Mass (Da): 25595
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A0A7C1UGM4 | MPRPPPGAGRSVASPVRAAGTAGAVDRRSSSVDCTGGTSLRPVPEVTVTEETLVLLLVVASLVAIGVSFLRVPYTIALVVVGLFLGLGQSFQSVDLTRDLILFVFLPPLLFEGALNMDLEDLRDRWFQVGILASLGTVIVVGLMTVGFAAGLGMDWTMALVLATVLAPTDPVSVLAMFKEQGIGGGLRTILEGESIFNDALAIVIFLIAVEVAFPEPGSSVTAADALYEFGSEVILGLGAGLLVGFVAHRLMSAVDNHLVEITLSIVTAFGSYLLADQFGGSGVIATVTGGLLIGNYGVHFAMSASSRVSLIDFWEVMAFVVNSLLFLLIGLKIRVEDFTDPHILWATVLGILLMLGSRAVVTYGMMGAVGRFGGDIPRGWLTAMFWGGLRGAIPVALVLGLREPDLDGTDAVTVVFGVVLFSLVVQGLTYRPLLNRMGLTRGNPDLEEFERLTAEALVLRASLHELEDLRHRGEITTPLYARMKAEFTEELAGVEERLSRTSLDTSAVHDRQVQLTARRLAGAQRAALADARRRGILSDRTIHAYSERIEEALEQGRIAPYDAAQLEPGLYPPGDEAD | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Subcellular Location: Cell membrane
Sequence Length: 579
Sequence Mass (Da): 61839
Location Topology: Multi-pass membrane protein
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A0A3D0VBM3 | EVLGARIRQISNDQRVLAIIIAFCFGALLESLAGFGAPVAISAAMLMAAGMKPLKAALVSLLANTAPVAFGSMAAPIVTLSAVTGIDMHTLSQMAGRQTPFIAVIVPFILVYLVDGRRGLRETWPVALVAGVVFALAQYVTSNFIAAELTDIVASVATVPAVLLTLRWWKPKNELAFETTAAEKDETRELGAAGTTQTITRLDTDSVRSGGRFTFLAVLPYLIIIAVFCISQIPAVKSLLSTIGSVTFAWPGLNVTDANGKPVAAQMFKLDHIKATGSLLLLAGILVAACYRITFAQAVQAYKDTLIQLRFTIITVMSVLGLSFVMNLSGQTATLGFALASAGGLFILFSPLIGWIGVAITGSDTSSNSLFGLLQVTAAGHSGLSPVLAAATNSSAGVLGKMLSPQNLAVAAAAVGMSGREGDIFRKLLGWSLGLLVLFMGLVYLQSTPILGWMVPQ | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 457
Sequence Mass (Da): 47788
Location Topology: Multi-pass membrane protein
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A0A2W6BQU3 | MVPNVLASRYASPEMTAIFTPQRRIIAERRLWIAVLRAQHELGVDVPEGAIAAYEAVAEQVDFESIAARERRTRHDVKARIEEFNALAGHEQIHKGLTSRDLTENVEQAQLRDALLLLRDRMIATLARLAELAAQHAALVLTGRSHNVAAQPTTLGKRFATVAQELLVAYHRITMLIERYPLRGIKGPVGTAADILELFGGDRAKLVELERRVARHLGFDSVLTSVSQVYPRSLDFDVLAALVQASAAPANLATTIRLMAGHELVTEGFRAGQVGSSAMPHKMNSRSCERINGLAVVLRGYLSMVSELVGDQWNEGDVSCSVVRRVALPDACYAADGLFNTTITVLDEFGIFPAVISAELARYLPYLATTKVLLAAVSAGLGRERAHEIIKEHSVAAALGAREGQDRDLIGALAGDPRLPLSRAQLEAVLADPLSLTGAAAEQVAAVVAQIEPILTANPQAASYTPGSLL | Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
EC: 4.3.2.2
Catalytic Activity: (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate
Sequence Length: 470
Sequence Mass (Da): 50664
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A0A2U9GCD2 | MQLILSHHLTMAGRVELVTGPMFAGKSTYLKNIYQQENGGNKHCLFVKHSLETRYGCGTGTIVTHAGEVIEGCTTVSSIKELISVLPEVVDVILIDEGQFFTDLVLVNRLADKGKRIVIAALDGTSDQQMFSPIHKLLPYTNSIVKLASKCMICKNDTKEAPFTVRFGNDNDNNVICVGGAEMYAAACRDCYKKINKKKNKGKLVVLEGGDRCGKSTQAKLLLTNKNSPLYGGEYMCFPDRSSHTGKLINDYLTKKIELDDHAAHLLFSANRWEVCSKIKQLLDDGIHVVMDRYYYSGIVFSLARGVDTVEWCSASDEGLPQPDLVLLMLLDVEKCSNRDTFGVERFETNSIQERARALFLDLANKDEKNVWIKVDARGTIEEVQTKIINIVYNIVEE | Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.7.1.21
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 398
Sequence Mass (Da): 44431
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A0A1W9P6X4 | MLTLFSSLITGRLKIMDFQQTIKKEVELKGVGLHSGEVVKLKFKPSLPDSGINFVRTDLPGKPVIKADVSNLLEQSRELRRTSIGRANAEVHTIEHLLASLFGLGIDNLLIEIDGSEVPGMDGSALPFFELLENAGIVKQDVRRKFFQVREPLFIQSPDDATLVILPHPNFKVSYTLDYSPFYALRGNPPSSPQHLIINFFSDGEENKKIFREEIAPARTFCLKNEVERLRKDGLGKGANYENTLVVDGDKIVNNKLRFEDEFVRHKILDLIGDIYLLGASLKGYIIAVKSGHWTNIRLLKKIEKQEEKIREAGVPSFSSGYPFKTVLDSRDIQEILPHRYPFLLVDKILELEEDKRIVGIKNVTIDDYFFQGHFPGHPVMPGVLIIEALAQTAGILMLSKKENRGKIAYFMGIDKGKFRQRVVPGDQLRLEVKVMRLRKNTGQVYTRALVEEKIVTEANLMFALG | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Subcellular Location: Cytoplasm
Sequence Length: 466
Sequence Mass (Da): 52697
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A0A0Q8W111 | MVTALYRRYRPETFAEMIGQSQVTEPLMTALRTDRVNHAYLFSGPRGCGKTTSARILARCLNCAEGPTDVPCGVCPSCVELARGGGGSLDVVEIDAASHNGVDDARDLRERAVFAPARDRFKIFILDEAHMVTPQGFNALLKLVEEPPEHIKFIFATTEPDKVLGTIRSRTHHYPFRLVPPGPMLEYVQQLCTEEGVEVAPGVLPLVVRAGGGSPRDTLSLLDQLIAGSDGPTIDYERAVALLGYTHGALLDEVVDAIGAADAAGAFAAADRVVQTGQDPRRFVEDLLERLRDLIVVAASSPETAAAVLRGVPEDELARMATQAAAFGQAELSRVADLVNQTLTEMTGATSPRLHLELMLARVLVPAADDTERGALVRVERLERRVGVADAAGSLPAASDSRPVARPEAAAPAPRVPAERVAAPMAATPPMSPAPVDAAPATPAPVPTPVAAGRPESVAPAESEPAAAPAAAAPSKPVGPVTLQQVRDAWPEVLSSLQRTKRSAWMVAFTAQVRDFRDGEVLVLTFPSEHDVAGFRGGAPGQSVSELLRGAIVDVLGVRVKFVARVDGPGGSPAAAPQTPSTPPAPAEPSAPAEARGPSAAAPASSSARPSSSAPETAAPAQPSASASAAPAGPVDSWATVAIPRDPITDAGAESAPTSARTATAVAERPQVAPAAEAPVASSVAPVPTRGGVDELPDDADAPPEDEEPPFDPGPEPEVIVEASAPAPAPAPAPARAPKRTSRPLPTAGNDGGIQRYGEAVVREVLGATFLEEVEAPPRPGFGERG | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 786
Sequence Mass (Da): 81288
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A0A350IWR1 | MKILLVNDDGINAPGILALVKQFAEKHEVYVCAPSSQRSGYSHGVTYFHGATHVQPVGIAGAVKAWAVDGTPADCSYLGIYELMDEKPDLLISGINQGQNMSADIVYSGTIGAACEGLIAHIPSIAMSWCSFTDTDFSIAAKVAEKAVVFFMEQPDHDYVLSVNVPALPYEQIKGVKWAWPQACRDFERPLARNYREDGSFDVVTTEPLSADPILNQEGTDLYEVSSGYVTLTPIGLDPTIRSDVFSKEKIRNFF | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 255
Sequence Mass (Da): 27876
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A0A847CK35 | MYSYFIEKNIEINDIYKFSKDDAHHIKNVLRLKSGEIVRLVFNSNAYFAKIGYSNKEPNAFVYDIDKTKNELDINITLIQALIKNDKFELVLQKVCELGVSNIIPMNSKYVNVNSDIIRNKKDRYNKILLEAAKQSKREVVPILADIIKLEECLGYKSDINIFAYESEFEKTNNISKYIEKGKNITIIIGCEGGLSSEEATFLKNNNFIPVSLGKRILRAETASIYALSVISSVNEVNQ | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 239
Sequence Mass (Da): 27278
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A0A930Z035 | MRPSSPPTIAIVGGGIAGLAAAWELVKDADGGDHTPVEVHLLEAGDRVGGKLRSADFAGRRVDLAADAFLARRPEATALCHELGLTEDLVPVGASGASVWARGQLRRLPAGLNLGVPTRWLPLFRSGILSPGESLRAARDLVAPHRGDQTADDDRSVGAIVGERLGRPIVERLVDPLVGGINAGRVDDLSAAVTFPQLLAASRQSGSLMRRLAQPPAGADGLSPPEPGPLFWSLSGSTASLADSLAEALSRRGVTIHTGVSVRSVEPHPDGPSGAPQWELALQGTDGSEQETAGRPHDPPSLRADRVILAVPAGEAAVLVGPHAPEAAVLLDSIAYASVAVVTLSVPRRAIRAPLRGTGFLVPLASPIAGGPALITGCTYLARKWPHLAGADDELLRVSVGRSGDSRHRDLSDDELTASAFGELTELLDIRDVPLDSLVTRWDEAFPQYAVDHATSVGRIERAVAALGSVAVAGAAYGGVGIPACIGSGRAAARRMLDSLSLDSLSLSPGSGSPGSGASGSDASGDEPAPPELGK | 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 Location: Cytoplasm
Sequence Length: 535
Sequence Mass (Da): 54846
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A0A960E0T7 | ELLSPAERSAQVFVDEARRPIPPGHVMGVPTDLDALTAGGLISPRGATRAAADLTRPADPEDPAVAGGDVAVGPYLRRRLGDEVVDHLVDPLLGGINAGDTATMSLAAVVPQLDAAARSGDPSLIRSCLEQKAAATADPEAPIFAAPTGGMARLIDALVAFAPAVEHRLGRSVAAIEPRGAGARVVLDDGATLDADAVVLTCPAHVATGLLADWDAEAAATLADIDHSSVAMLTMAFGRASLGDTTGFSGCLVPRDQGLFVTAVSYATSKWAQLRDPERDDVILRTSVGRTGDVRFSDLDDAVLTERVVADLDRIVGVSSDPTEVRIGRWERSLPQYAPGHLDRVAALEASLAAGPLRLAGMYLRGVGIPACVRSAEEVVADLGVTWPTRRDLSSR | 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 Location: Cytoplasm
Sequence Length: 396
Sequence Mass (Da): 41187
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A0A961ATQ7 | MSNLNPRQIALEALITWDNGSKHADDILGALSQRHRLQGADHGLVQTLFYGVLRHITRLDAFIDELKRGRMNHENRCVLRIGIFQLFHTDIPPHAAVNETVSLARGMRGVINGILRNAQRKQKELEALAKTWPLAVSQSHPEFLIDRWIATHGEDATRKLCEWNNEPPPVYVRTNRLAPDGADSEAIVTEATHLAAKVKGKGGFHRLTSGAPPKEWLDAGLIYVQDPSTSVACDLLEPHRQERILDACAAPGGKAALLYDRMKGTGNILATDVSPDRLETVRQNLKRLGLWDRGIETAIMDWQRPAKNKVAQMPKFDGILVDVPCSNTGVIRRRVDVRWRLRPDEFLEMQRVQLAITESCLPVLKPGGRIVYSTCSLEPEENRGVVDLLLERHPDKLELEEIAESLPWRDGFDGAFAARLRLKK | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 424
Sequence Mass (Da): 47642
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A0A1M6FLP4 | MLSLDLTFLWTIIDLIILFLILKKFLFKPLLAVIEKRKSLIDDSLSSAEEKEASAFALQEKYEYELNVSKVKSDELINESREKAQKEYERILAEAKLEAARIMETAGKNIEMQKKSEFEKMQSSIVDIAAAIAMKASEESIDEEKSRKLLKELLMKAGA | 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: 159
Sequence Mass (Da): 18150
Location Topology: Single-pass membrane protein
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A0A6A7LBC3 | MKALLMVPVMLKVSFSSPLVLNSSLSWTASNFVSEMKFPWLLSIGNIRRSFISSISSCLYRMLTEVIESNDNTLELKLRDEDISVMLIIQHELLSKKDIDFAGVILKHPLIRDYIMRIVTKKEDPAVALKEASANASKYLEELGASIKTQLRS | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 153
Sequence Mass (Da): 17276
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A0A927X1U9 | MIYTLTLSPSIDYYVLLDNLKIGKINRSKTEYLRVGGKGINVSKVLKELDIESIPVLLTAGFTKDKILEDLNNHKFNYYNIEVNGINRINVKIQAEEETAINTNGLFINDSHIDLIVDYLKRLTKDDYLVISGSIPSGVRRDVYEYIISKLDYENLNIIVDAEKDLLLNTLKYKPFLVKPNKEELEQLCNKKLKSINDIYNEGCKLIKLGAKNVIVSLGEMGLLYISSSLEKIYLPSIDVNVISTVGAGDSLIAGFLAGHSLNKETIDCLKLGLASACATVESAYLARKNDINRKLKLIK | Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.
EC: 2.7.1.144
Catalytic Activity: ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate + H(+)
Sequence Length: 300
Sequence Mass (Da): 33595
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A0A927X7F8 | MKKILILLMILFCNIISLFKYSKVSAEETLSLNGDKSLVMEVTTGRILYASNEHSKAYPASMTKMMGMYLVLEAINNNKLSFEDMVTCSSFASSMGGTQIFLEEGEQMSVNDLFKAVAINSANDAIVCLGEHLFGSNEAFVDKMNKKAKELKMENTNFVNATGFDDENHYTTPYDMGIIARRLVLDYQEVLEYSSLTEDYIKGNRNEEFWLVNTNKLLKHCDGMDGLKTGYTSKAGYNLASTVKRNGIRVISVVMNEKSIQERSQDTIKLVNYAFSKLKVDRLFSKDDILSKYIFENSMGKEVDLYLNENVDIVHLENEDIKDFNYRIELLDNKLPLKENDIVGKLVVEISENCYLHYDLIIKEKVEKMNLFKLWINNIIKSIV | 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-alanine.
Sequence Length: 384
Sequence Mass (Da): 43901
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A0A927XCN5 | MIGKVLGLDLGEKTLGIAESDIMGIIATGVENFRFESCDFDKAMERVHFYVKRDMIKEIALGLPLHMSGDESDHSIMCREFKARIEKEIPGIKVVLIDERWTTKQATRTLLEADLSRNKRKKVIDKMAAVVILETYLQMRG | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 16058
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A0A0F2L5M7 | MPEVSSFVGDYYLANEFVVTPWEVKGSVDYLRLAREFGVQLITEENLKVLQELAGDLHYLIRRGYFYAHRDLNVILDRQRRGSRWALYNGRGPSADIHLGHLVPWILTKWFVDRFRIDYFFELTDDEKFLVKEGHTLEETNKYAYENALDLIALGFTPDKLHIIVDSDDIKYLYKIAVKISKKLTLSTVKHTFGFTDSTNVGAAFFPTLEMAVAFLPTELYSEQVPVLIPTAIDQDPYFRLARDAADDLGYPKPATIYSKFMPGLTGEDKMSASNPDSAIYLIDDERTVRRKIMNALTGGQPTVEMQRKYGGDPDKCVVYKYHLLFQENDESVRRIYEDCKAGKLLCGECKVMLFERISNFMKEHKERRERAKDHLEEYKISIKFK | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
EC: 6.1.1.2
Subcellular Location: Cytoplasm
Sequence Length: 386
Sequence Mass (Da): 44731
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A0A395JJF8 | MDFESALKLRSSRLLETGSGRSIEVCEFAQSAYSDAHSAMLEHVSKSVDDDINNDQIWLLEHERVYTQGTACQLQTLLPSDIPTIKTDRGGQITYHGPGQLILYPLLHLKPLGLGVKTLVASLEQAVIDTLASLSVLAERRQDAPGVYVDGAKIAALGLRIRRGRSYHGLSLNIDLDLSPFTNIDPCGYQGLRVTQLSDLVPQFDAAKVRADLVANFVSLI | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 221
Sequence Mass (Da): 24157
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A0A2E5MZ36 | MTSRGLHTDVLISHGDWASAINDVDSLCQQASLAAYRACSEMELEQVEISILLSDDKNLQALNKKYRGVDKPTNVLSFPNHDWKKLSHATVIPQLLGDVVIAFETTMSEAIRDGKKLEDHLSHLVVHGVMHLLGHDHEHSVQAETMETLETTTLAELGISDPYDETEVVDTG | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 172
Sequence Mass (Da): 19026
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A0A2G9PI01 | MRLFLCFETPRLDELQSRVRNLGVHASYPKEFHCTLAFWGGEEPRKIIDALQGYSFKPFECVLKGTGFFPHERRPRVFWAGIESGGLLEVYEDLVERLGLEPGFTPHLTIARIKSGKNVEALRALARETQEKEWARFTVSELLLKKSVSTPNQGHEHETIFCVNACES | 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: 168
Sequence Mass (Da): 19223
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A0A928A5F2 | MRIATYSRTFQILKDYGIYANKSFGQNFIIEYKIIDKIVDAATIDKETGVIEIGPGIGALTEGLLLKAKKVVAFEIDKKLIDLLNNELKDFDNFTVINQDFLEINIDEVVEKYFKDFERVVIVSNLPYYITTPILIKIFEESTKIESVTAMMQKEVGQRICAKKGGKEYNNLSIMSSYYSDCHIALHVSKNIFTPRPNVDSCVVKFILNKKKENVKNEKLFLNVLRSSFAMRRKKLINNLEIFDKEKVKEILLKLNINENVRAEELELNDFINIANNLE | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 279
Sequence Mass (Da): 32196
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A0A329MYH7 | MGNSIFKKLLFSSLLMVVSLSVLIGTIAYSIASRTMIHETEKDLVNELKQIDRSLLTIVEDVNQSTEILQNNEALMQVFDSNPKQSFQRYLDLLEMDKLLKTAMSNNDAILGFSILSRNQNFSSGSRMDNYTYENFIELPVYQEKIRTLKNDQYALVRAEELQLTASAPSFKYEWIDKANVIFLIKKISSYPGNEVIVISFLSTASIMQNSNYGNVYALDGMDRLVWRGMPQIDESALFSRKASSIDKPEGSERAGSRRYVYLKSSVMDWFLINVISEREIVKPLGEIRTFVTLSIVVIIIVCMIAAMTASRGLTRRIRHLKNAVHLKGTDDPLLRTIPYDQRAGSPFQFIHSLKFGYKLFLYYICIVIIPMLVLSILLYHKTVVIVENRLEQSFRQPLALAASRIDMLMNRHIRNVKYLITSENVQQLFVTPPSESLEEFEKRQSRITNEIMSKTIYHTGLNNVEIYSHNGQLMYTSSQLHSERPSDNAIIPPKSIEGSIMWEDTYSDAFQNQVFSLVHEIKGNILFSEGFALPIGYLKIVLNESLLSQILKDIRFSEGSEVFIENRKGQIVSSNDKQFIGKTRNEIPAVSMSDNMLTAVKELGYNDWSLQAIIPAGKLMSSKKDLITYNLFVLSIMLLVIVIICIRRSVLYVRPIHALIQAMKKVKDGDLHVRFQERSGDEIELLGRSFNAMLDRLQQLIEEITKSKLREQELETKKRSAELNALQMQINPHFLYNTFESINWLVIQNENDKAVTMMTSLADLFRIGINRGENIVGLDEELMHAEAYITIQKIRYNDKLNVIWDIQLEARLYLTMKLVLQPLIENAIYHGIELMEGAGTIRIKSFIKEDRLILQIIDDGLGIEDERLTELMERFKNWYREPSRSIGLLNVNERIKLLFGEEFGLHINSKVNEGTIVSVTLPVVRKNASEGETA | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 935
Sequence Mass (Da): 107128
Location Topology: Multi-pass membrane protein
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A0A927XBI7 | MNTHILIFTRCILLLIISTFISNRICKVLISYFNKKRRGQEISSYLSSTHQNKKNTPTIGGISIIVSILITSLFIFDSYFDYQFLLGIIILILFFVIGLVDDLLKLIFRSHEGLSPLIRILLEILVVLIVYLILDNKGIFDYSFHFNDKYKIFLGPLFIIFSVLLIVGSSNSVNLTDGLDGLASGLFLISILPFIIFLLLDNNTNLVYLLIMVYGATFGFILLNLHPAKIFMGDSGSLPLGAILGYIALMSKKELLLLIVGGLFVFETMSVILQVLCFKITKKRIFLMSPFHHHLELMGKKEYTIVMCFYMIGFTLSLIGLIIGLKL | 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, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
EC: 2.7.8.13
Subcellular Location: Cell membrane
Sequence Length: 327
Sequence Mass (Da): 36944
Location Topology: Multi-pass membrane protein
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A0A098C195 | MWKDIIYVGIGGGIGSIFRFIVSRVIIRFVNQEWIFTGTLTVNITGCFLIGLLSGWMLSHQPENQLFRLLFIVGFCGGYTTFSTFAFENLRLLETNQRGLFTLYTSLGVALGLIAVWGGMKLTM | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 124
Sequence Mass (Da): 13897
Location Topology: Multi-pass membrane protein
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A0A1T2KQP2 | MRFWVSNGIYALLGRGFPYGTLMVNVLGSLVMGLLYVMFIERMMVSPEMRGALLVGFLGAFTTFSTFSIETLNLIEQADYMKAVMNMIVSVVACVFAAWLGLAIGRQL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 108
Sequence Mass (Da): 11944
Location Topology: Multi-pass membrane protein
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A0A973JUY8 | MIRSMKLSDLDEVSKIELEAFSHPWSKEDFEVELQSNPYALYFVLVDEDIIKAYIGVWIIYERAQITTIAVNKNFRRQGLSKKLMEFLDNLCLENSVEEISLEVRVSNEKAINLYHSFGFVKKGIRKDYYQDNHEDAYLMVKVVKGD | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 17250
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A0A7Y2NA68 | MGTVGEAGQVPKQLRRIGGIRVLEHSVRAVAAVSEAVIVVAPDGFVEDHRSEHADLVTVVVPGGSTRSASVKAGLDALAHLHPSHVLIHDAARPAVPPEVVERVRDALDSGAQAVVPVVPVTDSLRSVGGEPVDRTQFVGVQTPQGFDFGVIMAAYRAGGDATDDATLVSAMGGTVTTVPGDPKNIKVTVAPDLAVAGILMGMQPSAEFGRLRTGQGFDVHRWSADPHRQLVLGGVVFPDASGLRGHSDADVIAHSVIDAMLSAAGMGDIGVMFPDTDPRFEGASSIELLRLAAERLRMAGWTIINADCTVVLDAPKISAEREAMEINLSEAAGGPVTIKGKRTEGVTALAEGVQCFATVLMVGP | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
EC: 4.6.1.12
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Length: 365
Sequence Mass (Da): 37819
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A0A395JJ90 | MVGFITAGFLVVQFSRELPDASQIQGLELKVPLRVYSSENILISEFGDERRKPLAYENIPQTLINAVLASEDDGFFEHGGIDLKGLVRAALSNFKSGSSGQGASTITMQVARNFFLTRDKTYSRKIKEILLAIRLEQLLSKEEILGLYINKIFLGHRAYGFGAAAEVYYGKPINELTLAQTAMLAGLPKAPSTFNPLRNPERATIRRNYVLGRLHELKLITQEDLEIATEEAVSAEKHSRPTGLNAPHIAEMVRAQLTEQFGEEAYWQGLNVYTTIQAKPQLAASKSLRSGLKDYDRRHGFRGPVGKVDLASFEPVDGILDEAYENALSAYPSSQEQVPALILSVTKESAVIWTRDYGQASISLDSAKWARRHKTADLIGDAVKSMTDLVAAGNIVYVEPATTKPATVNATEATAQQIPEQIQWQLSQIPSVSGALISMNPNTGEIISLVGGYDFFLNKYNRAIQSIRQPGSNIKPFIYSASLDQGFTPASLISGAPIVITDPAHGTVWRPENYGGKFYGPTRMREALAKSMNLVSIRLLRAIGIEYAREYVARFGIDMQRFSRSLTMALGSGGATPLEVLNAYSTLANGGYRINPYFIQTITDRNGKILYQAPEPKFCDECYGKYIEMPPLLEPAKQEIRLDDSEQPNTDYSTEANNSPLTADQAGSPSEYEAPRVMSHANNFLTVSMMKDVVQNGTARRAKSLNRTDLAGKTGTTNDYVDAWFTGFNSQIATTVWIGFDDPTTMGRGESGSKAALPIWVDYMQTALKGIPQDSTDLPEYIEAGYVDRATGRRTTEDSPDAIPEYFVVKPLTPEYALYRSLLRTHLDDGTLSAEQFIEQLREEGVQPNQQAMESLDNLGIDGELDPDSLEDESQLIEPEERIIETEEETEGLF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 894
Sequence Mass (Da): 98792
Location Topology: Single-pass type II membrane protein
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A0A927X6I9 | MNKRKNSWISYVAPYLIILLIILGVSFLFGGNHSSKWNYTAGDIVTGSSDETIKDNAEESVLWTDNIQTLVIEYNNGNFIDVSGTVKKLDSNGKEVNYAYSVRLPSDEHTENILSYIVSNRTVTLDNGSVAQYYTSSNFQIVDPNQGNFWSDVFPIILISVVGIGVLVFLVTRMSGAVSKSNSQAMDFNKSRARREDGSSVRFDDVAGCDEEKEEMKELVDYLKNPQKYALAGAKLPKGVLLVGPPGTGKTLLAKAVAGEAKVPFYSISGSDFVEMFVGVGAGRVRDMFKKAKQTAPCIVFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFADNVGIIVIAATNRSDVLDPALMRAGRFDRQITVGLPDKVGREEILKVHARNKKFDETVNWAQVAKRTVGFSGADLASIINDAAILTVRLKKEKISIQEIDEAIDRRIAGPAKKSKHLTELERKTVAYHEAGHAIIGLLVPESDKVQKVTIVPRGMAGGYVLSTPEDDRFLMTKGELIARITGFLGGRSSEEIFFNDISTGASNDIEQATRIARAMVVEYGMSSLGPIQYESHSGSVFLGRDYTSSQKNFSGAVANEIDKEVRNIVETAHENAKKIILEHREDVELIAEALLEHETLNGEEIDYLLANRKMPDYRKETPNYGKPVEDKVEKKEDKNDSPFDPVIVFPDEIGENKEEE | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 694
Sequence Mass (Da): 76498
Location Topology: Multi-pass membrane protein
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A0A1I4IIQ3 | MKHVIVLKCGGSTLENLKADFFESIAAMQKKGLHPVIVHGGGPAINRRLEKDHVPTEFVEGLRKTTPQVLEAVEKALTGEVRRKLVQALEESGAPAHGVTGSENDLLQASPVDVETLGLVGAVDTVHTKRLEELIESGCIPVIAPIASSESHGRLNVNADAAAAAVATALGAGELVFVTDVDGVLRDGRLEETLTESSVTKYIDQGIIYGGMIPKVKAAAACLKGSINKVTIANGNGKNKNEDGTLKGTTVVKEPTSTDHKIEMLDN | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm
Sequence Length: 267
Sequence Mass (Da): 28082
|
A0A9E3Q5D6 | MKREVVVRVRQRRWLVDREGLTRLTEAFLGEELGLGEWCLGIQLVGERAMSEQNERWLGHEGSTDVITFDHREGPGEALHGELFVSVDDAVRQAEEFGSTPSMELVRYVVHGVLHLQGYDDRDGVSRRAMKRAEDRWVRRLARRFALRELVARLG | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 155
Sequence Mass (Da): 17896
|
A0A520XQT4 | MAKSTVTVEDLRRSTRITLEQAGIESSEIESNILVCEAFGWASSELIAYAPNPAPLEGIECLNQMLARRIKHEPIAYILGKQPFWSLEFLVTPDVLIPRPETEGVVERALSCLKEIGNPLIVDVGTGSGAILLSVLHERKDATGVGLDVSASALDIAKLNADKLEMADRAQFVLSDFLSEFDQRADIIVSNPPYITDKAMKNLPRTVVDYEPEMALRGVRHGLSAYEAIIAKLTEALKPQGSIVFEIGYDQGEAVAGLLRAAGFTQILIDQDLAGHDRVVSGKISA | 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 factor] + S-adenosyl-L-homocysteine
Sequence Length: 286
Sequence Mass (Da): 31027
|
A0A960XIA7 | MKAFDFLHPVLSSEASLAFEATLFGGDEAKEWIAMNQAGAAIARQALLDVQETLGNEPLNTILVLVGKGHNGGDAIIATRHLINRFPSATAKLLFPSGLSRIRPLVQRSLDDLQSAHGANLQFLSLRKNTIGDQLEAFAGDGSIDLCLDGIFGMQFRPPLRSPLRELIDWVNRNQSIRCRIAVDVPSGVGDTSDADPFRADFSYATGIAKQGLFDSDNRKSVGRIRYLDLGFFNGRSVEAGTQVVASSLLNFRRELRKPQTHKKTFGHLFVVGGSETMPGAILMTVKAALKSGA | Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
EC: 4.2.1.136
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 294
Sequence Mass (Da): 31865
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A0A6A4UP50 | MENLIELLKALILGIIQGITEWLPISSTGHMKIFNALWPMTSSEEFTNLFIVFIQIGSVMAVLLLFYKILNPLRKTPEGTRNTVNLWIKIVIASIPAAIIGLLFDDAIDALLSEYMLIVIAGTLIIYGFVFIFIENQNIPVKVSQLKDITYPQALAIGAFQTLAIIPGTSRSGATIIGSLWLGLSRTVAAEFSFMLSIPVLLGWGTIKFIKAGFSWTLLEWAVLFVGFTFAFIVSLLVMKMLMNYVRKHKFTPFALYRIVLGVLILALLSFQIL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 274
Sequence Mass (Da): 30524
Location Topology: Multi-pass membrane protein
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A0A7X7ZEM0 | MQKNKITNWLPYLIVIVAIASLFSLSSNASTQTLSYKELKSALSEETIDAANVSIGSNITTIKVLVKDANGRNTTMEGTLPSTNDEIAETLKSLDKTDAKVTIVDAAASNLFVETLVSLIPFVLLAGLAVWMINRMNGAQSANGKAFEFSQSRAKLEGKIRVRFSDVAGCDEEKQEMAEIIEYLKYPKKFEKMGARIPKGILLSGHPGTGKTLLAKAVAGEANVPFYSISGSDFVEMFVGVGASRVRDMFKKAQQTAPCIIFIDEIDAVGRQRGAGFGGGHDEREQTLNQLLVEMDGMEENTGVVVIAATNRPDVLDPALLRAGRFDRQITVSLPDRKGREAILAVHARNKHFAPDMDLNALAKRTPGFSGADLENVLNESAIMAVRHNETEITMADVDEAIDRVMMGPAKVSRTYDDKTKKLVAYHEAGHAIVGLFMDNAQIVQKVTIIPRGEAGGYNLMTPKEEKMLETKSDLLATITSYMGGRVSEEMFFDDVTTGASNDIERATNLAKDMVTLYGMSDLGPIKYNSGTENVFLGRDYNSPNNVSGQVAFEIDQEVRKIVNSCHDTARNLLEKHKKELENIANALMEHETLTAEQINRLVKGEDISADFVIEKTVNAPAAPQEPETKKPEIKETEPKTVSLTTDDEAKDASFKDSSDDQQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 664
Sequence Mass (Da): 72642
Location Topology: Multi-pass membrane protein
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A0A3D0DZH2 | MEAYPVMLNLHGKKALIVGGGKIAYRKAIGLLKAGAEITMISPDIYSEFHILLEKGQIRWKQKEFEESDLRDALIVIAATNKKSINREIAQLASDHQLINVVDDSRISNFHVPAKITRGKLTIAVGTEGASPILAKNIRDELAGVYDESYRDYLHFLEDARKLVYSKEKNTLMRTQLLTEIAERDYQNAGNQRKFFERMKSNNEGKEV | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 208
Sequence Mass (Da): 23594
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A0A1Q9NGI0 | MSRIRIHKFGGSCIRDAKGLARLYEILVAEEKPVIVTVSAIYGVTQYLIETLDNSATKLNIPSIISHLKKIHLDIFDSTNKNFVELDNELRKLERLYYGIAYTEEITLRTRDLILSFGERLVSCVLKRFFDDKNEKSRILKPENFILTNGIFGASTILLEETEINCNAFLEKYSKIDEIIIFPGYYGASKDKIINLLGRSGTDYTATALAYGFNADDVIIWKDVMGFMTADPNIIENASTLENLSYEEAAELSHFGAQILHSRSVIPAKLKNIPIYIKHLYNSEVNTKIWNETNLRNEDIVKSVSYLKDLAILRIYTTLGSNIDGVFNKISEKLVDVQTNIISIATSQTCISMLISEDQIKASLENLETLKPHIVDEIDCDKNIALIGIVGLGLGDTPGIVSRVFNSIAKIKVNVEMISSGASKAAYHFTVKQRDLNRALNIIHDEFF | 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: 448
Sequence Mass (Da): 50362
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A0A9D5RWB2 | MSIIYHIDLNAFFATAETTKDPSLADKPVAVGGSGRKGIISTANYIARKYGVHSAMPVFEAMKLCPELIVIPGDYELYERLSAKFINLIREYSSKVEQASIDECYADMEEAITNFYKPLDLAVEIQRRVKEELGLTCSIGIAPNKFLAKIASDLKKPNGITVLRKKEIRSKLWPLSIDAMGGIGKKTSPYLKQAGIYTIGDMADPNNRTIIEKYLGKNTDTYINYANGIDDSPVTTYHEVKSMSQSTTLEENILDFADVKVIFSKLTKRLCDRLTEENLYGNTVTITVRFYNFKNITRSRKLEHDTNSYEEILASALMLFEENDQNEPIRHLGIALGNIKSIQNDHNIDLFTMDEEPNAIETLKNEINSKLQHSEVILASDLVTKKKSKFHGIFKH | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 396
Sequence Mass (Da): 44666
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A0A832NGQ9 | MRALGLGVIGFGVVGRGFASLFLRRRDLLEEAFGRPVRVVGISDVARGNAFDERGLDLERCLRAAESGVDLGEATGAGGLPGMELASHPAVDVVIDLTPTNLSDGEPGYSHLRRALESGKHAITTNKGPIALRYGELKELACSRGLHLKFEGTVMSGTPVLEMAQRELAGSHIESVRGILNGTTNYVLTRMEEGLSYAEALREAQRLGYAEADPTADVEGFDALAKALILSHVIFGAGLRPEEVPRKGISGLSHETVEEAHSQGKRYKLLVEVSREGGSVRASVAPTLVGPEEMLYHVRGVENAISFRTETLGEVFVKGPGAGATATAQAVLHDLLSLARDLRGR | 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: 345
Sequence Mass (Da): 36726
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A0A9E8UCK2 | MDDLPLPLMEIPQINDQELNTLNDSLAETLAQVNSLQQLAGQLTALRDALPLSPEDLGLRLLRLEEQLERGSRQLERELLQARDNAEQLRLAPASLLFGPLQRAARDAARAVNKQVHFEGSGGDVKLEGGVLNAALGALVQMIRNAVAHGIEAPEARLAAGKPAQGRIELQVLRDGHQVRLRCSDDGAGIDMPALRRTAVARGVPGAGQWDEATLIDHLLRGGLSTAQQVNALAGRGVGMDLVRDTAERLGGQLTLQSRPGAGTTVELRVPLQLGAVRALYVMAEGLAAWVPLEAVEQVVQRPLIQGQQLVWGQDLLPHVRLSELLAPERLAAASAPGAALLLRCGNRRGAIGVDSVDGVATVVWRPPPALLPPSPLVTGLTLDAGQQPLPVLNPDGLITAAGRARPPLVPPERRTDTILVIDDSLTTRMLEQSILEAAGYRVHMASSAEDGLEALRRHAYAVVLVDVEMPPGMDGFRFVERLRADEALRHIPAVLVSSRSAPEDLARGAVVGADGYIIKGEFSQNRFLDQVAALVARSHLNAQVHRSAQPERVGP | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 556
Sequence Mass (Da): 59480
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A0A849XV16 | MSDQIFIEGLQVMTHIGVTPEERASPQMIEVSLVMDWDLAPSARTERLAMTIDYAEVRERVIHCARERPRALIETVAEDLAHELITVYRMRRIQVEVRKFVLEHARCAGVRIVRSGR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 117
Sequence Mass (Da): 13527
|
A0A927X5K6 | MYRYKCTVAYDGYNYMGFQIQDDLPTIELYIKQAIYKMLNVDVKIYASGRTDRYVHAFNQVFHFDLENEIPARGIQKGLNSYLPEDIYIKNVEIVGEDFHSRFSAISKEYRYYININEYNPLTIRYAPNITNLNVDKMQEAIKLFEGTHDFKGFASASIDPRKDTVKTIFNASINKRGDYLEFIFIGTGFLKYQIRRMMGLLLEIGRGKEAKDMILEVLEKKDPSISHKVADGCGLYLYKVNYKDE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 246
Sequence Mass (Da): 28718
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A0A7C6D006 | MKKKKTALFLETIGYFLLVLAVLISGALLFHTFYYELIYVSGTSMAPTLSQEGDIVDFGILDTHESAKKHLKRFDIVSSYYPTSVDYYDLSNNILRPNAKKKLKRIIAMPNETFEIKNGLLYLLKDDQFELIEYPFETLPNNPSFIQKDTFGAITLEDDEYWLLGDNRANSYDCASPTVKKPVKYENLAGVLVAIEGRAKLYIKHYVCSNCGKKYSTNVNTCEDCNHEVEPFYDLKDKRYHWPRYF | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 246
Sequence Mass (Da): 28476
Location Topology: Single-pass type II membrane protein
|
A0A960PMD1 | MTSSKDRPEGTISWRELLAETILALGEAEAIEAPELEARWMVEEASGLSGPEWVLGLDELATVRGVAHLDSMIKRRVNSEPIQYVLGHWSFRELDLLVDERVLIPRPETEQVVEVAFRELDRLVELGPHRQVPTVVDLGTGSGAIGLSFVVERPRSRVWITDASQSALSVARANLSALGMAAGGVRVGAGSWFEALPSDLQGEIDLLISNPPYIGEDEQLAASVREWEPTEALISGPTGLECYEVILAQAPQWLSEGGSIVLEIGASQGCALVEMAQGAGFGDVRLEQDLAGLDRVLVANLSPLSPERRD | 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 factor] + S-adenosyl-L-homocysteine
Sequence Length: 310
Sequence Mass (Da): 33507
|
A0A6F8PXM5 | MQRWNPLYWLFYLIIRFYQLFISPLLGPRCRFYPSCSHYTIEALQTHGVLKGSWLALKRISRCHPGNPGGIDFVPPCDCQNNKETTADKVPEKTPSASVNKTPQTPD | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 107
Sequence Mass (Da): 12268
Location Topology: Peripheral membrane protein
|
A0A920SH26 | MLTASGGPFRGRTRADLAMVTFEEALDHPTWSMGPKVTVDSSTLMNKGLEVIEAYELFGIDYDRIDVGVSTHSRSSTPW | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 79
Sequence Mass (Da): 8707
|
A0A3C2CW62 | MKLDNKKIFKTLNPNKVWVPIIIGLGIVFAMFYLDPSITAESLKGVFDASIPWLFFAILVLFFRDFGYVYRIREITDRQLTWTRAIYVIILWEFASAVTPSVVGGTAVAMFILNKEGIKMGKAIAFVMVTAILDNLFFVIGAPIILYFAKGNIFPDSKLLETQMENSLQAIFWISYSLYASYSLVMAAALFYRPRVFKWVLIKIFSIKFLRKWKHDAQEYGNQIIEASRELRGKKMKYWLPIAGATVFIWTSRYLMLNALISAFVPLSFEQEIIVFARQVIMWIVMMISPTPGSSGTAEFFYAQFFTQFLGGYTFVTSIVWRLFSYYPYLILGAIFLPRWIRQVFFKKKPGGEE | 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 resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Cell membrane
Sequence Length: 354
Sequence Mass (Da): 40933
Location Topology: Multi-pass membrane protein
|
A0A5Q4GRF8 | MTEGQDKNSGQRHLQPISPSNQQLAQYDPLLHSSQHSEEVISLHELWLVFLKRKWTVISIALIFVVGAFLSTTLTVPEYRSTAQVQISPQQTRVLGFGEFDYSQRAGRVFDEYRATQLQLLRSTELNQRVVRNASLYEYPELRGEIRQRSVTGELRGLTRTVRNSVRDMLNGSATDAAAAEGNTARDPVPMAAAILRSRIEVQPIRDTHLVNISVIGFEPRFTAHAANALVAEYIQDSMRRRLDAGGEAREFLSDQLSEMRITLERSDQALMDFARNNQIADLSERLNTQQRALSQLSGRLSEVQRELVRLDAWQNLIDQGRINSLEPVANSNAIRDLDSRLLEARTRLRQLRNQFSDAAPEVREAQSLIAGLEEERQDRIQRIVEETEGRRDSLLAEQASLNNAVREQENAILSLNERSVQYNILRREFETSRELYDGLLQRMKEIGVASGSQENNIAVIETARMPGAPFRPNLQRSVLMGLALGLAAGLGLALMLEFLDRTIRSIEDIERLVDRPVLGMIPLVKLRGRDGIRRRKRPKVVENPEHSISHYSAIHSSSAVSEAFRSLRTSLSFSTAEGMPRVLMVTSSMVGEGKTTNAINLATVLAQNGSRVLLIDADLRKPRVHREFNRPRSPGLTNRIANVDAGGEENGAICPTHATGLFIMPAGHTTPNPAEMLNSPRLNKVIESCRRVFDHIIIDAPPILGLADSLILSRQVDGVMLVVKAGETTRENFKISMKRLGQVQAPVLGVVLNAVDLENPQYAYYASYYYNYQENAESDNEAEPAPPRAHAAT | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 794
Sequence Mass (Da): 88818
Location Topology: Multi-pass membrane protein
|
A0A2M9MVT2 | MNIHIIGAGSLGLLYAGKLAASGCRVTLWCRSEEQADKLRASGITIEDMGQHQVVDAHTFSICSWSSFSESGGAADADYLFLMMKQQGIEEMATEMLALFGQDHRRLLCFQNGTGHLERLQGLLPMWTIYAAITTEGAKRTSSVSVLHAGQGTTTIGKMKPAGSPFDAFSQEDHEIELVKQLNRAGFEAFLSNEMEEMIYRKLLMNAVINPLTALWRIPNGELLSSPERVRLMRQLYNEGIAVYDAGGIPYGSGLWEWIVSVCQSTSGNTSSMLKDVMDGRTTEVAWINGSIVRLGQKYGVSVPTHELITQLIEGMNT | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 318
Sequence Mass (Da): 34932
|
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