ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A914IUW0 | MEPEKRQELLSKCAEKLAVLSNDDRSKTNMEVFSKLYAKFLTERATIDWKTWKLPPEDRFIDSGELEHVEFAEAQQLLEKLAVVRLNGGLGTTMGCSGPKSLIKVKNGKSFLEIAIDQIAALNQKYNVHIPLLLMESFNTIQETKNELEKLTKNKNVKIVQFEQAKCPRIYADTLLLVPESPESENEMWYPPGHGNIFETLESTGLADKLLAEGKTVLFVSNIDNTCAIVDPRFVKALLDKEHEYIMEITDKTAADVKGGTLIEIDGRLMHLEMPQVPPEGIDEFCSTRTFKNFNTNNIWIDLGAIKSXXXXFGGRKNGP... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: UTP--glucose-1-phosphate uridylyltransferase catalyzing the conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor for the production of glycogen.
EC: 2.7.7.9
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-... |
A0A6J4ISX5 | MFNVGTPELLVILLVALIVLGPSKLPDAARQVGKFVGELRRMSSGFQDELRDAMQEPVTSVKQTLKGDPVPKATPASEVKPVSQVIDQSLPGESAAADPSASSLGGPAPEDLPALPPVPVAGSPALDEGVVPEDRAGDDDEAAAVAAPEQAESRTGADPA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
E9SCB2 | MTGHIHSTESFSSVDGPGNRFVIFFQGCPMRCLYCHNPDTWEVNGGREVTAEELLDEFDSVKEFLKGGGITCTGGEPCLQMGFLTELFEKAKARGINTCLDTCGITFRASDTSAFDRLMQSTDLVMLDIKHIDPVCHKKLTSHDNANILAFAQYLSDIGKPVWIRHVVVPNITDNEDYLYRLGRFLAHIKTIKALDVLPYHTLGKSKYEKLGLEYPLGDTPPMSHEGAHKARDIIMRGLKDELRDELKK | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'... |
A0A1F5E6M6 | MNENFFLPALCPLDGRYHHKMADLARIFCEANLIKNRLVIEIEYLLFLANKRLIPAFSSKEKNALKAILKNFDQDNALAIKTIEDTTHHDVKAIEYYLRGELAKAGININYWLHLGLTSEDINNLSYGLMLRQSRQEIIMPALKKLIQTLIDLAQTHKGQVMLARTHGQPAVPTTVGKEIINFAVRLSEEVKNFKHLPIAGKLNGAVGNYNAQALVFPKVNWPRFSQEFVKSLGLEPCLYTTQILPYETTLRIFQSMRLINGILLGLVQDMWRYISDNYFLQKVEGSRVGSSTMPQKVNPIDFENAEGNLGLANSLFDFF... | Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
Function: Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]... |
A0A914ERY1 | XGIHAAQGYARTSGRTGVVFATSGPGATNLVTGLADAMIDSNPIVCVTGQVFASLLGTDAFQETDVINITAPVTKWNYQVTDATEIPAALAKAFYIASTGRPGPVLIDITKNAQMQLFDYFGYEKCNHVRSYRPAPQVRKEYVEQAAELINNAKKPFVLFGQGIILGKAEEEFKAFIEKTGIPSASTVMGLSALPTDHKLHVGMLGMHGNYAPNVMTNECDVLIAIGMRFDDRVTGRLDKYAKQAKVIHLDIDPAEIDKNVQTTVPVWGDCKESLPMLTELVNATDHSDWLAQFRELEKEEIKEVIQNELHPQTDIMTMG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: (2R)-hydroxyhexadecanoyl-CoA = formyl-CoA + pentadecanal
Sequence Length: 812
Sequence Mass (Da): 90712
|
A0A5P9JAQ8 | MAHIDFTTKINTARQVNPLKTLHTSLESDRGRIINSSGIRRLQQKTQVFPLERNAAVRSRLTHSLEVQQNGRFIVQKLFSKLNAQERAHYGFTDMERPFETLVEMACLMHDIGNPAFGHFGEAAINHWFSRYLQQRFGPLPTLAQTHPLKHQLMLDLQSFEGNAQAIRAVHSLLALNLSYSQIAAILKYTRPGTMAKDARPEDKSYLMKKVGFYHSEAAFIAQLGDALEMDNGCRHPASYIMEAADDIAYCLADMEDAVEKGILSVEKLVHYLDDAYRQRLAALDTAEQSYSDLVAKACEFARQKAGEAEFNYNNTFFIY... | Function: dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.
EC: 3.1.5.1
Catalytic Activity: dGTP + H2O = 2'-deoxyguanosine + H(+) + triphosphate
Sequence Length: 487
Sequence Mass (Da): 55792
|
A0A9D1M188 | MKKKTLILFMILCIFISNTVHADDQIEEEEYKIEDIIEASNSPKEEPILNARAAVIYDRRTNEILWGKKENERRPMASTTKIMTAIVVLENGNLKDIVQVSKKAAGTGGSRLGLKANDKVSVQDLLYGLLLVSGNDSAVALAEYIAGSVEGFANKMNEKAQELGLENSHFVSPHGLDMKEHYTTAYELAKLTDYALENKKFAEIVNTKYYTVNLGGRTKNLSNTNELLGNLEGVNGVKTGFTNGANRCLVTSVTRNDMSIITVVLGADTKKNRTADSIKLIEYAYQNFKEVKIDEKIKNEFEDWKEKNENNIILNKGFSK... | 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... |
A0A3A9G3T8 | MAAYGLIGHPLGHSVSPQIHQQLFSLEGLSCPYELYDLPAETFAEGFPAELEALDGFNITLPFKEKILPYLETLHESAAFYGSANTVLRQKDGTRIGFNTDCDGFLRTLESRQIPISGSVCILGAGGVGRMFALECLRQGAKTAVAVRETGLSRAKQLAQEAREKCGKPLEILDIGTLSGPFDLLINATPVGMYPNIQQCPISETVITQCKAVFDCIYNPGETLLLQAAKKAGAQVAGGMDMLVWQAVSAHHYWNGTAFSNHAVQKIISETAETVRMQFGGE | 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-dehydr... |
A0A7S3RAC3 | FFCIIMLLRNILSRTTLAGQHKFSFSAAIKRRGGGAARPVGMRASSGPCAIIVDYDDTCTERDTIGTLLSAAVDAQCKAAPGKDRKQLDATISQLASNYAARREELFRQILPAQASSAPNPDGLAYFLEKLSDFDVDMNKVVADAGVLGGLSFQQLEAAAQSVQLKPGCAQTLQRMASMGVPVHIISVNWSSRFIAAGMQHLRFEHDSIAAKDAVIQTGRLPAVPQSNQQQSAAGFVFANELSFGPDGVSTGGIVGAVQSARDKGMLLRGLLQHYEGQGHTGAGSLVYIGDSVPDLQPLLAAPFGIIIGHNALLRRVCAC... | 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.
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidin... |
A0A7Y2T6S1 | MNLPNTITLFRLVLTAVFCGAASAEGVVGYAIALSAFILGAISDWLDGYLARKLNLVTSLGKLLDPLADKILVCSGFVYLSAKGLCPVWVTALILCREFLVTGIRQIAVEKGTVIAADGLGKWKTTFQLIFIITALVYLTFESVESTHFIVTTLQYLSNKDHLLFPLSLWPAVALTVISGWSYFWSSKSIILDQD | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 195
Sequence Mass (Da): 21311
Location Topology: Multi-pass membrane protein
|
A0A0A7RZA7 | MIIITRPSPYGETLTKICQTAGFAAKHLPFFKISAGPDLPILQHKLNALNDNDIVIATSPQVIEQINQYSMLIQFPTTIQYFAVGQQTATLFSQLTKKKVISPSFNESSEGLLNYLVERNISVTNRNILILCAKNGKTLLKDVLLSRRANVENIYIYHKDRILHSNTILDDNADKLSNINIIAITSQAHLLELEHYCQNKQKSQFTLIVTRKQIKQLAETLGWKRVYLAINANNYNLFRTISTLCSNETIVNTLDENLSW | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A2G9YHT9 | MKPEIILALDVDSLERAKYFVNKLYPAVKIFKVGSQLFTACGPKVIDILNKKGASVFLDLKFFDIPNTIAHAVRNAIRLKVKMMTLHILGDEEMIKAAVSAARDESKRLKIKKPLLIGVTVLTSKEARSSDVLTLARIGIECGLDGIVCSAREAKFLRQAIKKKFLIVTPGIRPKGAGKNDQRRTATVREAIQSGSNFLVVGRPILEAREPLIKAKEILGDIHGRRN | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 227
Sequence Mass (... |
A0A6S6ZXA2 | MTALLSRETFNRQANGGDANASPTPESCGSPWSGQGLGALAARSLWLEVHTWPKPGLVSHVDAGSHDDMNAATFERSALALQPFFTELAQAGSDNAPMSTLRKIGLRAETAMFAATGGINTHRGAIFGLGLLCAAAGLRAKQEGASTTHGPALGDIVRTRWGADILGGPRLPGSHGETVVRRYGVGGARAEAACGFPCVYELGLPALRQALAGACMDDNAARVHACLALVSQVQDTNLLHRGGEAGLQYAQLQARRFMAAGGVFQAGWHARAQRMHQSFVQRRLSPGGAADLLAMTLFAHAAGD | Function: Involved in the formation of 2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A, the prosthetic group of the acyl-carrier protein of the malonate decarboxylase.
EC: 2.4.2.52
Catalytic Activity: 3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + adenine
Sequence Length: 304
Sequence Mas... |
A0A0N0RFD7 | MTNPPFEKILIANRGEIAVRIIRACRELGVRTVAVYSDADAHARHVFLADEAVHIGAAPATDSYLRGERIIEAALQTGAQAIHPGYGFLSENADFAEAVNAAGLVFIGPPPDAIRAMGSKTAARETMQRAGVPVVPGYQGGGAFEDYAAAAERIGYPILVKAAAGGGGKGMRIVEHPNTLRDAIEAAQREAQKAFGDGRVYLEKYVREPHHVEVQVLADTHGTVLHLCERECSVQRRHQKIIEESPSPLLDEALRERMGAAAVAAARAVGYVNAGTVEFLVDADRNFYFLEMNTRLQVEHPVTELVVGLDLVKWQLRIAA... | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form ... |
A0A0C1R9F6 | MLDQSELLQFIPSRPLDAHKWQSACWVIAGSPGMEGAAILAARAAQRSGAGYVRLSVPNAESVEAPLEVVVTKIEKNLELEDIDRFASLVVGPGIGTDSAIMEGVRGLLQKIRKPVVVDGDGLKALRNFSFKEEVSVSTVLTPHDGEFESITGIKVTKDRERSAVQLSKETRAVVLLKGPTTVVASPQGQIEKIKAGDQRLATAGSGDVLSGIIGAFLARGATGFNAACAGALIHGKLLSKLPMTGVVAGDLDEPLPRLLERFGLDSQREINE | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
R6DRY9 | MLLSDILNGIDYSCDNFADFDIKDITYDSRKAGEGKCFFCLTGTLTDGHKYAMSAYDGGCRCIFAEHKLELPEDCVQIITEDTRHALALASVNYFGRPCDKLKVVGITGTKGKTTTAHIARRLIEASGVKCGIVGTNGASFGDVHEETQNTTPESYELQKFFRRMVDAGCKYCVIEASSLGLKMHRTDGIPFEVGVFMNLAPDHIGTIEHPTFEDYKNSKKLLFSMCRHVVVNVDDPAYEDMLDGSSADDVIGFGLGDADIRAQNVELLRSNDILGISFDCIEKGEKIRVEAPIPGYFNVYNVLAAIGICKALGIEVKNP... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosyn... |
A0A6J4IFS6 | MDDAPAGPAAPTAAQAASRRRWSRLAVVAAVVVAADQLAKTWALRVLADRTIDLVGSLRLRLVFNTGSAFSIGSGLGPVLVVVGVVIVAVLLRASRDLDGAPALGGLGLVLGGAVGNLLDRIVRGGDGLFNGAVVDFVDLQWWPVFNVADMAICAGVAVLAVTLGRAGSGEDAGGERGEAARPGRSSVGGGGSAEPPGSAVGGAGPSAVGGGGGAERPGADAGER | 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-, ... |
D1Y4V5 | MTYGIRLLVFLKEGVLDTQGKTVAASLKGMGYGCLKDLRVGKYIHLDVDAASEAEAVAQVEKMCDDLLVNDIIEEFTIEPEAPRA | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A3A1Y7Z3 | MEQSKIYPVLLAGGTGTRLWPVSRTSFPKQFQTFFGDKSMLQQTLQRLDGLNVAKPIVVCNEEHRFIAAEQLRQLNLLDNNIILESQGRGTAPAIALAAFEAIQQDEQAVLLVLPADHVILDNEKLKLSITQALSSVFKEKIVTFGIKPTSVETGYGYIEQGEAFLEQSFYVKSFKEKPSKELAQELIASKRYLWNSGMFMFTAKAYLQILEAVDQELYTLCKHAYANAQKDLDFKRVFDQDYSLCKDISIDHAIMEKTTQAVVIPLEVTWSDIGSWEALWSISDKDQYGNVVHGEYLAIDSKNNFVMAENSLISTIGID... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Length: 471
Sequence Mass (Da): 53498
|
A0A3L8B439 | MSVLYLDFGNSRFKWRLSDGGITAQSYEGFDAWLHSLSGHGDLTAVVFASVLTERRQEGITEQLKSALSLPLQRCVVTSSALGVQCAYRDLDRLGIDRWLAVVAAWARYGEACAVVDAGTAATLDFVDVAGHHLGGYIVSGLTLALQGLLAGTDNIRPDPAGFESAALVPGVNTAEAIYHGALYSLVALIESSYQNLLKSFPQAKLILAGGDAALVGSHLYSQHELVEDLVFEGMQLLESAALLIDA | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A941WWY6 | MYRKVSTDMNFVEREKEVLDFWKREGIMEKSFHHRDGAERFTFFDGPPTANGRPHIGHIETRAIKDLIPRFQSMKGKDVLRKAGWDTHGLPVELEVEKLLGLDGKPQIEAYGIEPFIAECKKSVWKYQHEWEEMSDRVGFWADMKNPYITYKDDYIESEWWSLKEIWKKGLLYKGFKVVPYCPRCGTALSSHEVAQGYKEVSDVSATVRFKVVGREDTYILAWTTTPWTLPSNVALCVNAHEDYCEFQLDGQTYILAQALLHAVFGEKAHEGQVLKTMKGAELCGTAYEPLYRFEGITYPREKGWYVVSDDYVTLTDGTG... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
A0A2K3MY14 | MASTRQVHCLMRRFYRGSRTFAVATQPTASSSSQTIIDKEFQHSAHNYHPLPIVFAHAKGSAVWDPEGNKYIDFLSGYSAVNQGHCHPKILKALKDQAERLTVSSRAFYNDRFPVFAEYLTALFGYDMVLPMNTGAEGVETALKLARKWGYEKKKIPNDEALIVSCCGCFNGRTLGVISMSCDNEATRGFGPLMPGHLKVDFGDAEALEKIFKEKGDHIAAFILEPIQGEAGVKIPPDGYLKAVRDLCSKYNVLMIADEIQTGLARTGKMLACEWEDVRPDVVILGKALGGGIIPVSAVLADKDVMLCIKPGQHGSTFGG... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1.
EC: 2.6.1.13
Catalytic Activity: a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-glutamate 5-semialdehyde
Sequence Length: 342
Sequence Mass (Da): 37311
|
A0A4V0P1F7 | MVLRRSEVLKVLSMKDEIATVEEAFREKGMNAVQMPPKQYLFLEGGDLRAMPAYLPRLGIAGVKVVNVHPGNRERGLPSVMAVIELVDPYTGRPLAIVDGTEITAYRTGAASAVATKYLSRDDSSKLCIVGAGAQSRRQLEAIVEVRDIRKVFAYDVVRAAAEGLVRYAESMGRNLSAEVADATRECVESADVLVTATPAKAPVILNDWVKPGTHINAIGADAPGKEELDPAILLRSKIVVDDYEQTIHSGEINVPISKGILRKDQIYGELGEIVAGKKPGRTSRDEVTVFDSTGVGILDVATAFSVMRAAGARGLGLTV... | Function: Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate.
EC: 1.4.1.1
Catalytic Activity: H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate
Sequence Length: 325
Sequence Mass (Da): 34825
|
A0A1M5TIV6 | MYEHLDRRYALALYEVAEEEGRLEEFLEDLKALIALTKNNKEFMEIIKHPQIPTERKINIIKNIFNDKIHPKLLNFIIVLLKKDRILFLEEKYREMVKIYLERHSTIVAHVKTAIKLNDSERDTLINKLEEKYDKIVLLKEEVDESLIGGVFLRIGDDVIDSSIKTRFAEIRQLVGGLY | 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... |
A0A6C0SMX7 | MEEEDSANGGDLGLEVLVEGAPVKSADCAGSEEEGTVSESSVVKQSRAEILLGMMFPQLTLNGGSHTLTMRRSVLVIFTLYTSHSFSAWGDRMWGFVLSLFLVYLYPGSLLLPGVAGVMVQLLVAVFGTLVGDWVDSSPRMRVVWVSLLIQNGLLTLCSILLALMFALDWTVCNNIVVFASLIPLVIVLGAGANLATIANTISIEKDWIVVLADKQKDTLAVLNSNMRRIDLCCKLLAPFLTGVVLQWAGPLVTTLFVAGWNILSFFAELGLIWLVYRLIPPLAIKKLRKKSEVVEVDNDETKEDGEDSLEPIVVTTKVS... | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 668
Sequence Mass (Da): 72900
Location Topology: Multi-pass membrane protein
|
A0A925LJ35 | ICDPFGWTAQGLETITRKEENNLVQTVARLKEIIGGYNVDKIILGLPKNMNNTEGERVDKTLVFKRRLEKEFELPVETWDERLSTMGAQRILLEAEVHKKNQKKVIDKMAAVFILQGYLDAHRST | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 125
Sequence Mass (Da): 14384
|
A0A0K8QZ36 | MILSKDINTVYFVGIGGIGMSALARLFNHQGLRVAGYDRTATNITRQLVEEGIHVHYDDLGSEVSTLISEPEQTLVVYTPAVPSDHEELKWLKQNKYLIVKRASVLGLLCSQFQCMAVSGTHGKTTVSTMAATIMNNRPEKCGAILGGISKNFHSNLVLPDKESNWMITEADEFDRSFLQLSPDIAVITSIDADHLDIYSNVEEIILSFNEFVGKIRPGGILLLNEKVRDKVKSEGVKTYTYSLTGPSDFKTENLKLDESTRCYSFQLQTPSGTTSEITMQYPGLLNVENAVAAGAASWLAGTGLREISLGIESYLGVKR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 464
Sequence Mass (Da): 51647
|
A0A533IZI8 | MSFNFEFFLTMAVIISGAIALIDRLIFAPIRQRKKIAHPSMLIEYARSFFPILLLVLLLRSFLAEPFRIPSGSEKPDLLIGDFIVANKFSYGIRLPVLHKKIIPIGEPKRGDIVVFLWPKDPSIYFIKRVIGLPGDVITYKDKVLTINGQLAPQTLLGEKTDRDGLNEKWPVLLKRENLLGVQHDIYLRPDQSSTDFSVHVPPGNYFVMGDNRDNSLDSRYWGFVPEKNLIGKAMWVFFSWDNEQHRVRWDRLGMRIH | 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: 258
Sequence Mass (Da): 29807
Location Topology: Single-pass type II membrane protein
|
A0A2T2R506 | MKDAESDTFSITNKTNGSYSIPELPFSRIKKTVLGAEYDLSLVFIQDGRSAILNEKYRDKEGPTNVLSFEVGDDIGEIYINIDAVSREYESYADDAKSFAGYLFIHGMLHLKGYPHGSKMDKEEQRICDQFEIQTI | 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: 136
Sequence Mass (Da): 15431
|
A0A7C4W1T6 | MIAAVVVAAGKGVRMGGPLPKQFLPLRGMPVVCHSLKAIARHVNAVILVAAQQDIAYCRDEVLTRIDLPVPIDVVAGGKERQDSVYRGLCAIEGHAELVLIHDAVRPFVPEEALTVAIRQAQEMGACILGISAIDTLKQVRDGWIEGTLDREGIWQAQTPQVFRTDRILEAHRQAIRDGIVGTDDAALVERMGHPVAIVFGSRFNLKITTPEDLLIAEALFDRVHEG | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A7S3VH23 | MEEEEQGVPSMASPPIQPVQPPIQACWACNTNVQVPLCGEARCKATAFKCGWCGAVTETFAAQQKRLDARRKRRGMAVRVWRVVRAFQWATVLVVLGLIASIVLLGTAFVLPALFSSSPVAFALDHAATMVLTAMVIFNYLASILCSAGTVDECFELSPAHEGTVRQGAYDNHYLCLECQNHKPPGVHHCSTCRRCIVDMDHHCPFIGNCVGRVNMRNFIHFKVWTILAMLFAIANCVALMAQEHEWRNFSGLVAKSWEIAWAERDPILFPGLVFSHCPTYFLATLYVVVISTLILITVGILFACIVRHLLTNASAVRVP... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 419
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 45682
Location Topology: Multi-pass membrane protein
|
A0A0P7XUC0 | MRLKLIAGTVLAAVMAGAASATIVGAPVDGALGLQQAVTPVMENTVSFHNLLLWIISAISFLVLGLILWIAARYRAKTNPEPRKFSHNTLIEIIWTAVPVLILIVIAVPSFRLLYFQDVIPEADFTIKATGNQWNWTYEYPDHGGFEFVSNMLEEGDITSENWEQARLLSTDVPVVVPSGATVRVQVTASDVIHSWALPAFGVKIDGIPGRLNETWFVVPEGNEGIYFGQCSEICGIRHAFMPIEIHVVPQEVFTAWTEAANEDPYAASTVLASYYASQRATRVAAAN | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A2S8BEW2 | METTDVAMHLRAADAPVLLDCLGTWLTARVDLHRAWEGAGLDAVHADIEELVTAWRECAVPAVAVSNEVGSGVVPASASGRYSRSSVLVRAASRCPAPVANDQPASTTPCAAGWMRILAGVSAPCTQPAACTAASARSSRRCIQA | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A2D3R7K5 | MKAKVIVAMSGGVDSSVAAWMLKKQKYLVEGLFVKNWEKDDILGKCAFENDWNDAKLICKQLNIPIHYANFSEEYWEKVFKLFINEYEQGKIPNPDIICNKEIKFKIILKYSMLKLGADFLATGHYAKISYKKQLYNNSPLFQAKDKKRDQTYFLHAVNPKIFKYLLFPLGDHYKMDVRKLAKKLGFTNYNKKSSTGLCFIGKKNFKNFLQEFFLLKPGFIKNVNGKILGKHDGVFFYTIGQRKGLGIGGKKNTDQLPWYVQHKNIKTNTLIVVQGINNFLLYSKNIYCEPIHWLLKPFKFPFNCFAKIRHGYNQELCTV... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
Q5ANN6 | MPLHPKSRRRSSRISPLPDEDSLSFINSSVENLDQSPFESIDDLVEDVNKYDLKSPSDEQQQQQQQESQTQNLKHKPSFTSTPKASYIPPWTEPYIIGIAGNSGSGKTSISQKIIQDINQPWTVLLSFDNFYQPLTSEQSKLAFANNYDFDCPDSLDFDLLVETIGNLKKGGKTTIPVYSFTSHNRTSKTNTIYGANVIIVEGLYALHDQQLLDMMDLKIYVDTDLDICLARRLTRDILYRGRDLGGAMQQWEKFVKPNAVKFINPTVQNADLVIPRGLDNSIAINLMIKHIKNQLALKSRNHLQRLKKLGVNIKFDIDK... | Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
EC: 2.7.1.48
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Length: 545
Sequence Mass (Da): 62060
|
I0IH52 | MKVLLANPRGFCAGVEMAIDTVQELVDLIGTPLYVFHAIVHNKHVVERFVEQGVTFVERIDEVPEGETVVFSAHGVSPAVRAEAAARGLKMIDATCPLVTKVHVEARRYARMGRHILLIGHADHQEVKGTLGEAPADTTVVESAADVAELDFPPDQELIYLTQTTLSVDDAQTVIRAIEARFPRCTAPPKEDICYATTNRQHAVMELASQADLTLVVGSANSSNSVRLTEISENRGTPGRLVDDASGLDPAWFEGVETVLLTAGASAPEDLVEGVKRWLIERFGAEVEDPEPVDEGMNFALPVELRVMINRGGGKPKTHR... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of is... |
A0A0F3NN14 | MIYLTKIFSAANDSFFYLSSFIFIISIIVFIHEYGHYIVAKICNVKIETFSIGFGPELFGIKDKSGTRWKFSLIPIGGYVKMFGDANIASTGATSSNLTAEEKLYAFYEKSLLQKFCIAFAGPLANLLFAVIILTVFFNVQGIMHPLAVVGKIEKNSAAEKAGLVAGDVILKINNHDIKWFKDIQKYVIENGNQKLSILYLRQNVQDTTTIYPEMRTVGKSQIPFLGILASQLRQDYQLQKLSVTSAFTNSCIYTYNLIYTTLLMIWQMITGQRSINELGGPIQIAKYSGYSVKNNEVLWFMGIISINLGIVNLLPIPML... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 372
Sequence Mass (Da): 41802
Location Topology: Multi-pass membrane protein
|
A0A101FM39 | MRAHLLLVDKEPGLRSTRCVEIVRSRLGRNIKVGHAGTLDGPASGLLLILLGSATRLSDYAMKLPKTYRVTLKLGIETTTGDITGSVTRTMPVSGDAEERLRRATCAFLGMRLQRPPAFSAVRVNGERAHRLARKGKTPPLEARPVFIRSIRVTSPVDEDGYVSMVVECHKGTYIRSLAFDIGRKVGCGATVSSLRRVALGSLAEAQSLSSRLLPHMDREALSRHLLPVERLLDHFTAYEIDQHVEEACWRGQAIKGCPGRRLLSWGILPTSEGVALVGERGVTFCEVVLSSGGASFYPKVNVPLEGEIAG | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 311
Sequence Mass (Da): 33831
|
A0A3A9FXV2 | MKLIVGGYAQGKRAYLETIVQKIADGGLADEKTLEEAQGIDKLHLLAARWMEQGKDPTVMALTLAEKNPEIIFVCDEIGCGIVPMERKERGWREAVGRMCCALAAQAQQVERVICGIPMVIKS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A1L9GUP7 | MDEQKQKQSASSSEAPVVGARTESVVAIKEIESLNGYYKKVVLEKTNAVPQKLTDLGGKVFKDRYSLKSKDGLQIEHTPEQMWRRVAKTIATAETTSEKQREWEDNFYWALTDFKFVPAGRILTGAGANTEVTFYNCYVLPYPEDSRGGIMKSVTIMMEIMARGGGVGVNLSSLRPRGSYVKGVNGSASGAVSFGALYSFVTGLIEQGGSRRGALMLMMNDDHPDIEEFITVKREMGKITNANLSVCVSDRFMEAVKKDADWDLVWNGEVRKTIKAAKLWDLVTESAHASGEPGCVFMERCNKESNTWYFENIICVNPCG... | Pathway: Genetic information processing; DNA replication.
Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
EC: 1.17.4.1
Catalytic... |
A0A7X9KZM4 | MIKILKRAKAAKISMAQLTSEQKNEILLNFAEKINKYSDKIIEANKKDIVIARQKNMSEALIDRLALNEKRIQGMIDAIHEIIAQDDPINKVIEQFPIKAGPIVSKVSVPLGVVLIIYESRPNVFVDSAALCIKSSNVSVLRGSSSAIYSNSCLNSIIKETLKELEIDENIVNFIEDTDRKLVDSLVKAREYIDVLIPRGGKGLKQYIYETATIPIIETGDGICHIFVDESAKSDMARDVLVNAKTQRPGTCNSCETVLFHKNLDINTIANITDALLNKNVEIRYQKDIIESLKSINYNNVDKLIEAQDSDFGFEFHDMI... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
... |
A0A2J0M541 | MRIEFYYLPKSINLDFLKKVIGIVLREEKKIDSEINVIFLSKRQIEKLNFNYRKKQESTDVLSFKADNQFSTEDRNYLGELVVCFPYIKDNAKQFEQSLKKELASVLIHGVLHLLGYNHEIRGKDSKIMMAKQEKYLLII | 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: 140
Sequence Mass (Da): 16577
|
A0A914JU85 | MRRSLQTLAKSYRSFSTAAPASLESIVHPDVSNLQLEYLKETCIAVDENDKVLGPISKASSHQIGTATLHRAFSVKGRCQRLLFRIVGRMRVVRIQIASRKNPSKKMHWEFDEQLKXXXXGTGKFCICLDKFLKNVLPATLHRAFSVLIFNSKKEMLLQKRSMSKITFPNCWTNACCSHPNCIPEESIEENALGVRRAAQRKLHHELGISKMFCDLSDFNLVGRFIYASDSDDYWCEKELDYVLILKNFAGRINLNPDEVSEAKFVDPQTLTFMMKSNSQSFSPWFRLLYEQGXXXIFVFFVRKKFAFFTL | Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
EC: ... |
A0A925R795 | AMAHNLQVFQPRRVREPSFIETIKQLSPDVIVVIAFGQILPKAFLEIPQYGCINVHASLLPKYRGAAPIQWCIINGEVVTGITTMFMDVGIDTGDMLLKTEIEIAQDETGGSLHDRLQELGGPLLLQTLDQLEQGSAVRQPQIHEHSIYAPMLDKKLGEIDWNKSAVEIERLIRGLAPWPSAYTYLDGKILKLWKAEVVSTTAEHSVGTLCDIQKNEGFTIQCGQEGLLIKELQLQGKNKMDGSAFLRGAKLNVGSKFGQPV | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A1M2Z3T2 | MAFVFYDTETTGTNWQFDQILQFAAVKTDTDLQVVDEFQTQSRLLPHVVPHPEAMKINGLTPAQITNPGLPSHYQMVRQIDAQLRGWGRTMFMGFNNLGLDENILRAAFYKTLHRPYLTVMDGNSRTDLLKLARAAHLLAPGTLRLNTSDYGTPLFSLGELARANGFNNPHAHNARADLDATLHVARILMNEAPGVWNDFMRFAQKSTVLQHIQDEQIFGLAEFYKGKAYTWLVTRIGTSGRDKNVHYAFDLQFDPADFAALTDEELVERLASMPRPLKKLKVNGCPVLFAVDDAPPGTEARLLDDDELERRVRRLGDDP... | Cofactor: Binds 2 Mg(2+) ions per monomer.
EC: 3.1.11.1
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 468
Sequence Mass (Da): 52735
|
A0A2K3NHI5 | METSLRYGGDSKALKIHAKQKLQIDTNTFFQIRGELDTKSGQPNSLSALIRHYYPDLSATLGVGVRYDKQDSVGGARYAKNDKLRYTVRAKKTFPVTNDGLINFKVKGTCDVDQDFKERKSRGGAEFSWNIFNFQKDQDIRLRVGYEAFQQLLYGARLLGSLNLNKSLLFWECDMLLFSTKCCQIPAIEAL | Function: Voltage-dependent rectifying anion channel that facilitates the translocation between chloroplast and cytoplasm of phosphorylated carbohydrates such as triosephosphate, 3-phosphoglycerate and inorganic phosphate (Pi) depending of ATP to triosephosphate ratio in the plastidial intermembrane space; in high trio... |
A0A914JK07 | MLIPSYFFTYQLIHNRSLFNDKQVIKLQEIPGDMPAGQTPYSVTLFVHGALVEQVHPGDRVAVTGIYRMTPMRSNPVQRTLKATFRTTIDVLHFRKMNQDRLHDESDGSYMTEERIEQIKSLAANPDVVDILVHSVAPRIYGHEDVKKGVLCLLFGGTRKDADNQNKAKTRSEINILLCGDPGTAKSQMLQFVYHLVPRAQYTSGKGSSAVGLTASIARDPDTKGVVLQTGALVLADNGVCXXXXXXXXXLGAFLLFFLKISEN | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such tha... |
A0A2K3PRW4 | MLTQTVDPKCKDTDSQTWLSTALTNLETCKNGFYDLGVTNYVLPLLSNNVTKLLSNTLSLKKVPYKQPSYKGGFPTWVKPGDRKLLQTSSAASKANVVVAKDGSGKYTTVKAATDAAPSGSGRYVIYVKAGVYNEQVEIKAKNVMLVGDGIGKTIITGSKSVGGGTTTFRSATVAAVGDGFIAQDITFRNTAGAANHQAVAFRSGSDLSVFYKCSFEGYQDTLYVHSERQFYRECNIYGTVDFIFGNAAVVLQSCNIIARNPPQKTITLTAQGRTDPNQNTGIIIHNSQVTAASDLNPSSVKSYLGRPWQKYSRTVFMKT... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) ... |
A0A0M8K7B4 | MNDFFALGWEALGPFLLVCATALIVMLSDLWLEDDEREWLAYFSLAGLAGAFIMAVRQFLLVSNVQQPSLAFNDMIIWDRMSSGFHVLLVGVAFVAILLLPRYLADHDNLNRGELYALMLFSVAGMMLLASARDLIVIFLGIELLSFPLYILAGFARPRVDSEEAALKYFLLGAFASGFLLYGIALIYGAVGSTNLGVISTTFTVLGVGETLTNTLFLIGLALMLVGFGFKISLAPFHQWTPDVYQGAPTPITAFMVAATKAGGMVALMRVLYTALVPAADLWVPILAILAAVTMTWGNVAALVQSNIKRMLAYSSIAHA... | 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 ... |
A0A0N0RFK1 | MQGRTILITGGASGLGAATARRFVQEGAHVVLLDMNSTAGEAMVAELGDRARFAKTDVTSEADVQAAIALAQEAFGGVHGLVNCAGIAIAERVLGRENRIHDLERFAKVIAVNLTGTFNCIRLAAAAMAQNEPNEDGERGVIVNTASVAAFDGQIGQAAYSASKGGVVGMTLPIARDLAQYGIRVMTIAPGIMDTPMLAGLPEKARLSLSQQVPFPQRLGKPEEYAALVLHIFQNAYLNGEVXXXXFAWRHAKRAGKKPPPQPTRGSLTMKIGIVGTGAVGATAAYALVVRGIGREIVLVDINTKRAIAEAEDIFHAVPF... | Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
EC: 1.1.1.27
Subcellular Location: Cytoplasm
Sequence Length: 582
Sequence Mass (Da): 61246
|
A0A974ZKF4 | MQDSSSIPSATSAENDRQVSERVHHTLVETPLGQMHLAAREDALIGAWFTGQAHFPAKHHLGEKVEPSRHPILEQAARELEEYFAKERKSFEVPLAPDGTDFQLAVWDSLKDIPFGYTTTYGAISKIVGPGAPAQAVGQAVGHNKVSIFIPCHRVLSADGKLTGYAGGVERKQYLLDLEAPSAAEEGRLF | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A223B3V3 | MSTLKLNKKFIESIPMPMCIVDKKGKIVDFNAHIGEVFLYDDITGSDFFALTGVKLEDIIEESGEKGCKTIERSDKTFKVFTSEESCCEKNGDTDRSGDEDTDGNRDRDTDGSGDGNVDEGNVLVFFYDITRYEILKETYEDEKTCVALVRIDNYDELIAGTLPDMRMELSSRVDKTIRKWAADTHASIVKHKDDEYAMYFQQIYLKAMVDSKFSILDEVRQIETEVDFPISLSVGVGTAEDNMSDTEESARAALELALGRGGDQAVVRKHNQIDYYGGKLQTVEKTNKGKSRVIAHMLKQLIADADRILIMGHRNPDMD... | Cofactor: For phosphodiesterase activity, probably binds 2 Mn(2+) per subunit.
Subcellular Location: Cell membrane
Sequence Length: 616
Sequence Mass (Da): 68305
Location Topology: Multi-pass membrane protein
|
A0A2K3N0Q4 | MNTANAIKRRINSPREEIALNDCEQLMDLSMDRIWDSVFAMTKSNIDSDKDAHTWLSSVLTNHATCLDGLEGISLTLMENDIQEMISRARTSLAVFLAVFPQKGHDEFVDETLNGEFPSWVTSNGRSLLESSVGDIKANVVVATDGSGKFKTVAEGVASAPDNGKTTYVIYVKKGTYKENIEIGKKKTNVMLVGDGMDATIITGNLNFIDGTTTFKSATVGPEKHQAVALRVGADQSVINRCRIDAFQDTLYAHSNRQFYRDSVITGTIDFIFGNAAVVFQKCKLVARKPLSNQNNMFTAQGREDPAQNTGTSIQQCDLT... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) ... |
R6E3N9 | MKDENGREYSDYDIDKLIEEYSHINRNDEPEQVSQPPKEKKKFVVHIDESLIDSPQSVEPKPQSGGIYFSNYPKHHSTSRVQEPHAAEHKGNMKKNAAKHEHASHEDAVRKVKDGIEKVGGKAAVGFLAFILISTILLSYVGITCLGDMLAINRSDENVTVDIPADATYSQIIDILKDNKLIKRKGFCKMFTKFRGFDEGKYLSGQYYLNSKMGVEGMLKDIMAAPVTAESISLSFPEGLTATQILEKLEKNDVCNSAKVLTAMRTGKFNYDFLNDITDNKNRFLKLEGYLFPDTYDFYVDADPNYVITKFLDNFNSKWE... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 470
Sequence Mass (Da): 52662
Location Topology: Single-pass membrane protein
|
A0A841CAV4 | MKLAKFGGSSLASGEQIRKVFGIVKSDPLRKIVVVSAPGKRFESDIKVTDLLDAYYQDYKNGKNLVPIQTTLLDRFEEICDELELSELKQFLSEKVISLALLNLHNRFVYDKFLSTGEECSALIVSSYFKKNGLNAKFLSPKDAGILVSSDPCEAKLLPIAYNKIAGLVKYPEILIIPGFYGATLNGEVCTFSRGGSDITGAILAAGVKAEMYENFTDVDGIYSVNPNVVENPVIIEEVTYREMRELSFAGFSVLHEEALIPAARAGVPMLLKNTNHPELPGTQIVPNWTIDMPVVGIASSRGYVIIKITKYMLYRDISF... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to t... |
A0A4P2VLA6 | MPANEIGERLRVTFVGESHGRLVGAVMDGVPAGLELSEADLQPMLDLRRPSHGPHSTARAEPDRVEILTGVYRGRTTGAPILIAVPNEDVDSSYYEGPPIPRPGHADYTAWVKYGGYNDPRGGGRFSGRLTAAMVAAGAVSLKLLRLALGVEVIAYTLEIGGVRARDGLSIEELRNRYADPLRCPDPEASRLMSDAVERARRDGDSLGGIVEAIALGVPPGLGEPLVDTLDGDLAKAMFAIPAVKGIEFGAGFGASRLRGSEDNDEYRVLAWRVMKDITNTSCSEDNDEYRVREGRIVTATNNSGGILGGISNGMPIVLR... | Cofactor: Reduced FMN (FMNH(2)).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to... |
W9H796 | MSNETPAAQKITGQKIAAEKIAVVLFNLGGPDSREAVRPFLFNLFNDPAILRIPGLFRTPLAHFLAKRRAKPAGEIYEILGGKSPLLENTEAQAQALQAALGDLGQVRTFIAMRYWHPMSDETAQRVREFDPDRIVLLPLYPQFSTTTTASSEKVWFQSAKAAGIDKPTVTVCCYPTEPGFIKSAAKLIRAGIEDAGAAGHGKPRVLFSSHGLPKKVVKGGDPYQWQCERTAEAIVRELDIPGLDWVSCYQSRVGPLEWIGPSTDAEIERAGTDGVPLVVVPIAFVSEHSETLVEIEVEYRELAHEKGVPHFVRVPTVGV... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 385
Sequ... |
A0A8T4K6M6 | MAYFPFFADIQGKEAVVVGGGKIACRRILSLLPFGCRVRVIAPEIGPELKAVLDEEKASGRLLWENKEYEERDLDACGRPAFVLAASGNLAVNEAVVLNCRARGIAVNDASKKENCDFYFPGLARRGGLVAGVTASGTDHKKAAALAAAVRKLLEDDVWAEENSLKPGEKGSEPDGVQVEGRDA | 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: 184
Sequence Mass (Da): 19658
|
A0A9D1M0P8 | MKKLFTSESVTEGHPDKMCDLISDAILDAHLEQDENSRVACETVAGKGEIYITGEITSKAEVDIENLVRNVICQIGYDDAQTGMDYRTCKITINLSKQSPDIAQGVDKSIETKEGEDLESEGAGDQGIMFGFACDETEEFMPLPISLAHKLAKRLTEVRKKGMIQGLKPDGKVQVTVEYDDNKPVRIDTIVISTQHEENKNLEELKKELERKVIHEIVPANLLDEKTRYLINPTGRFVIGGPLGDSGLTGRKIIVDTYGGYSRHGGGAFSGKDATKVDRSASYMARFLAKNIVANHYAKKCEIQLSYAIGVARPVSIYID... | Cofactor: Binds 1 potassium ion per subunit.
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequenti... |
A0A918PN13 | MGWRMKKIETKIERINMNATNVNYAIFGGGCFWCIEAVLQRINGVLTVESGYANGHAKEPNYRDVCKGDSGYAEVVKVGYDPEIISYEDLLLIFMTSHDPTSLNQQGADRGTQYRSGIYYENDAQKETAELVVKELTAHYSSTIVTEIEPLRNYFVAEEYHQNYYNQNSSAGYCRVVIEPKINKLRAMFSDKLKKTV | 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... |
A0A068VN07 | MVLQTIMMAQLILVVILAILFSRIVVASAAAFPISKPGCNSSCGDVEIPYPFGMTEGCYLDEPFQVICNTSFNPPKPFSQLSEMDVTRISLEGCCQTSIPKGTSEFSLSVGSFRNHSVVENFNPCSSVFVVEQGGFNFSMDLLRDIENVNKLPVALDWTIGNETCEIAQKNLDTYACQKNSKCINDPEPDSYPGYRCSCLEGYEGNPYIACQDIDECQDENLNTCTFKSLCKNEIGGHKCSCPNGYHGDGKISPCLPKRKNQQLLVTRIIAGIALVTAALLAFGSWLYFEFKRRKLIIEKQKFFQENGGLLLQQELIKQQ... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 599
Sequence Mass (Da): 66613
Location Topology: Single-pass type I membrane protein
|
T0LYE5 | MISLYIAIALIGILSAVVSGNNISAAVGTIVGSRIVSRHFGLTLGATGFSLGLIIEGRFLSNSLFLIMPEKSNLILIVLGVSIIMFIIATLARIPLSLIMAIVGTSIGIGLRTGYNYDSLYVIMIIALWIVAPILAILSSYFLNLNLSKIGVKNVWATARFYKLFLVTISFLTAFTLGANTFGLLASLERSSYLTIPTMIIAIFLGAAFMSSGVIRRISQDMYGMRYQNATVSLLVSSILVEGATFFALPLPSTQTLTSSVFGTGLSYKTKAMQIRPFLIIVIMWVVSPLLGMALGYLIA | Function: Potential transporter for phosphate.
Subcellular Location: Membrane
Sequence Length: 300
Sequence Mass (Da): 32259
Location Topology: Multi-pass membrane protein
|
A0A437A5I2 | MVLGKHFIGDIKSPVEKALKCLLEVNPTLGLIESHKVIYNRSGKTDKVLLISGGGSGHEPAHAGFVGDGMLDVAVAGDIFASPSAAQILVGLKAIEGSKGTLMIVKNYTGDKLNFGLAAQKARSEGQEISVVFVNEDASLDAKSLVGRRGLAGTVFVHKIAGAAASRGLELSEVTRIAQKVADNVTTVGVSLDKCSVPGRSGQEGLGAGELEYGMGIHNEPGVLRASLTDLSSVVSKVLSYLLSGSSPVAFDKNDSVAVLVNNLGGLSVLELNVIAEEVLKWLSNAPQQFKIARKFVGTFMTSLDGPGFSVTLLKADQEI... | Pathway: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 2/2.
Function: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Catalytic Activity: ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+)
Sequence Length: 536
Sequence M... |
A0A914FMB3 | MGVRGATSEQNPPLPPSLKAPQYGVSQPISMELPTASELELTKSLEFELKAKNVYESEQELEIRLEVLRRINALVKAWVKHVSVQKGLPLDQVERAGGKLFTFGSYRLGVYTRGADIDSLCVAPRHVERSDFFSSFFQMLKEDSNVTELHAVEEAFVPLIKFRYNGIELDILFARLALKEVGENQRLDDNGLLRNLDEKSIRSLNGCRVADEILKSIPNQKTFTIALRAVKLWAKNHSIYSNSLGFLGGISWAILVARTCQLYPNATPSTIIEKFFLVF | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 279
Sequence Mass (Da): 31389
|
A0A365U6L7 | MDGSALLILVVVLAFFAAQIATLFRILLRERRAPAARLAWIICVFALPGVGIVLYFLFGEVDFGRYKLEQLKAIEARLPRTVPGVAPVPPGVLPAGQAFARAAASNGFDPVAGNTAEIAQDSDDAIARLVADIDAAEAQVHLLFYIWLEDANGTRVLEAVRRAAARGVTCRVMVDALGSRKLAQSRAWAELSEAGVQTGLAFGFRVALLHMFFARVDIRNHRKIAVIDGRIAYVGSQNCADAAFLPKAKYAPWVDVMARMEGPVAWQMQRLFAEDWELHTGEDLSAMLDRAAGEMPDGKVTAVAMGTGPDDGFEAVPDTA... | Function: Could be a virulence factor.
Subcellular Location: Membrane
Sequence Length: 480
Sequence Mass (Da): 51997
Location Topology: Multi-pass membrane protein
|
A0A914FGT0 | MIKFGENIRDKDNGYFCRKSIESLPSSTEYLIISDCRRPTDLEYFKLKFSNVFVIEINADIKTRSERGFIHCPEIDDAESE | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3.
EC: 2.7.4.2
Subcellular Location: Cytoplasm
Sequence Length: 81
Sequence Mass (Da): 9486
|
E5E4Y6 | FGAWAGMLXTALSILIRAELGQPGALLGDDQIYNVIVTAHAFXMIFFMVMPIMLGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A941WU14 | MRCGLIGEKLGHSHSKTLHGLLADYRYDLIELAPEELGPFLKKGEFDGLNVTIPYKQAVIPYLRELSPAARAIGSVNTIVRRPDGTLFGDNTDAYGLGVITGRAGMAFAGTKTLILGSGGTSKTARHVVEAAGGEAVTVSRTGETNYENLERHADAAWLINATPVGMYPRAQAAPVDLARLTNLRGVADVIYNPLRTRLLQQARALGIPCEGGLTMLTYQAVRACERFTGRPVPAERAREAERALRRAVTGLALVGMPGAGKSTVGALAAARLGMPFVDLDGEIEKAAGMPIPRIFETEGEAGFRRRETEALRRVALVGG... | 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... |
H6MYY6 | MGAVGKGVGKGIGAGWGLLARGVGGVARAGSGRRGPSNRDTDLDDFHDDDLHNDDLHNGDFYDDDVEAAAEYDDPDLGAGPRGGRRAGDRRAQRDRASATGDVGGHTHRRDGVALGLLALAVLIAAGVWFGAAGPAGAFINALIRAIVGSLAVLIPVALVAAAIILMRRPPNPVRRGRYIGAALLIVLPLLGLIHLVAGSPTDLDGRSSAGGFLGFAVGTPLTAGATAWVSVPILLLCMAFGVLVISGRTVRDVLDAVRTYLGLTASVDDWDTDDELPWDADVDLADDPDSYHPDSYDPYDRDDFGSDDRFGGASARRGR... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
H6MW95 | MARAIIDLLPDEDIVYIGDTANGPYGPLTIPQIRKHALAIGDELAERGVKAIVIACNTASAACLRDARERYAPIPVIEVVLPAVRRAVVATKTGRIGVIGTEATIASQAYQDSFAAARDAEITAVACPRFVDFVERGITSGRQILGLAQGYLEPLQDAGVDTVVLGCTHYPLLSGVIALAMGDEVTLVSSAEETAKDLFAVLTRSDMLHPHTDRAAERVFQATGNPESFARLSTRFLGPTVGSVARI | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 247
Sequence Mass (Da): 26196
|
A0A0P7XU98 | MSGVAALGNFDGVHAGHCAVLGQARALAQSIGSEPVAAVFSPHPRRLFRPDDPPFRLMSDSQRERALLAAGAARVDTIRFDASLAAMTPEEFVRVVLVGQLALDGVVTGADFCFGKGRAGNAETLKALGAQHGLAVGIAPTLIADSLQDRGKFSSSAVRHALRDGDVETAANLLGRAWAIEGEVAHGDKRGRTLGFPTANIALGEYLRPRAGVYAVRAHLPGHPGLVKGVANIGKRPTVEGTEERLEVYFFDFSGDLYGKTLEVELLGFIREERRFDGLEALKAQIAADSASARALLDRDGAS | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 303
Sequence Mass (Da): 32033
|
A0A914FDY2 | XEKLRHFNELDHELCLRLNRSYEFSVRYMEQFISPVLEIIAKYITFAAASIFTVLGLLTIWDEDVLTFEHVITVMSACAGIIFVCRSFIANENLVFCPDFLMKQIVAXXXXLFREKLRHFNELDHELHLRLSRSYEFSVRYMEQFISPVLEIIAKYITFAAASIFTVLGLLTIWDEDVLTFEHVITVMSACAGIIFVCRSFIANENLVFCPDFLMKQIVANIHYAPESWLRDAHSSEVVSEFGKLFHMRAYAIALDVFSPIFNPFILYFVISPKAAGEIVQFFLEKNRYVPELGDVCSYALMDLKDGEKELSELNNDDDN... | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by di... |
A0A6I1FJV3 | MSENLWRNNVRKLDPYIPGQAAEEAKQQEKLTEVVRLATNENQLGPSPKAIEAMTKALQEVHFYPDLTSLELRTKLGELHGIDPENYVVANGADNIINLVIASYINPGDEVVYCTPTFSEYHKNTLLMGGVPVELPTTKDHKFDLEAILGAITEKTKIVIVCNPNNPTGTIVGEEELRAFFKRLPKHVVAVLDEAYGEFISVENYATGVEYIKEGLPVITIRTFSKLYGLAGMRVGYAMATEELIQPLQRVREPFACNRVAHAGALGALEDTEHKNKTLTENKREMKKLIKEFRALGYEVEESHTNFLFVDMKQDTSKIA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 370
Sequence Mass (Da): 41223
|
A0A3S3PQB0 | MCSARKLGSEANTGILMMNMGGPQDLNEVEPFLTRLFTDKDIIPLPMQSKLGPLIAKRRSPKIAAKYSQIGGGSPIKAWTEKQGQAMVKLLDEKSPQSAPHKFYIGFRYAQPLMEDTIEQMEREGVKKAIAFSQYPQYSCSTTGSSFNALAKHYLKRKGVSEMRWSFIDRWPVNKGLIDAFTDLTLKEIEKFPPTVKDDIVILFSAHSLPMSAVNRGDPYPTEVGATVLRVMETLNWRYPYRLVWQSKVGPVPWLSPQTDKALEGFVKNGHKNFLIVPISFVNEHIETLHELDIEYSDELAHKLKIENIRRVPAPNDHPS... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Mitochondrion inner membrane
Sequen... |
A0A7V6H545 | MKDILLILDYHSKYTEDIAKKLRLEGIACRILPGDVLPSEIQAISPLGIILAGGTGADFPLSIDGRLLHTGIPILALGNTAASVCLLLNGEIKDTTMLKKVENVSFLPSTLTEDLQTSQRMLHAINTLELSSELKPIAKWKDEIIGFKHQELNLFALGFQIESNDPDGNHILLRFAIDICGCSQWWDESAHIALMRSHIEKMVGDGTAVCAITGGLDSGVSAVLAHKVLGDRLRCIFVNTGLLREGEVEFVLKHYRDEENLSITLINAQNEFLEALNGIISAEEKQKAILNTMRRVLSDALEGIEYNAVIRGITCDEVLR... | Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
Function: Catalyzes the synthesis of GMP from XMP.
EC: 6.3.5.2
Sequence Length: 483
Sequence Mass (Da): 53549
|
A0A1D8PHJ3 | MFAQSALRPARTLPSRILTRRNFQVSARKFDINTIVYGTAKEGPYENLPFKIKNRKFVPFAVWYWGVLGFFFAFPFLTSWWQLKKSGAFNKTE | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1D8PMZ8 | MVAPALIYSNHELSTAIDSTHAFEGPEKLLEIWFYESKELSPINLRDIKFDTWIEILNLVHCEVLSKVSSNLCDAFLLSESSLFVFPHKIILKTCGTTTTLACLDLLFETVNKELLQNEGLKATFQSKNIYQIFYSRRSFMFPDRQIHVHGNWQEEVKLLNQYFNNGKSYIVGNNTNWHLYVGGNGKTKNPVASTTTTTTPVVNDCTLEIIMTQLSLEASQQFYTTRKPGDTAIDSNHDLGHDLGQEILKQTGLNELFKFKKQPTMPGLSSSPIKEIHDGFAFTPCGFSSNSINESDYYTIHVTPEPGWSYASFETNMIG... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Seq... |
A0A1G2BXX4 | MASEYLIILLIVLGITIWLEKTCHLQLFNTKKERVIITLVLFLIGVAWDTFAIYRGHWLFLPEKNLGITIGLMPLEEYLFMLIQPYFIITIYKLVESKLKIKK | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 103
Sequence Mass (Da): 12144
Location Topology: Multi-pass membrane protein
|
A0A2M7US72 | MKHASFIKKAYAFSSKACGCVLAVCITVYQKTISPDHSMFLRPFYPHGCCKFYPSCSEYTRQAVVKHGVFKGTRLFFGRLRKCHPWAEGGIDLIP | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 95
Sequence Mass (Da): 10767
Location Topology: Peripheral membrane protein
|
I0IAL2 | MSEARRLFAEAVAWGGLDADALERLLRDDLAVDLEPAGVDVTAACFPGIAGPAEVALVAREPGRLAGLDLVAPLLEAPEAAGVACAFHRRDGDAVAAGETLAVFTGPRPAVLTIERTLLNLVGHLAGVATAAATLVDAVRAAGSDAAVLDTRKTLPGLRKLQKYAHRRGGGTAHRTGLGDAVLVKDNHLAGVPLGELAATLAAAASAARSRFPGLRFVEVEVDTLDQLREVLKAPVDFVLLDNFDAGWLAEAVAMRDAAAPGVRLEASGGVTLETVGSLAVPGIDRVSVGAITHSARSLDLGFDDAG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 307
Sequence Mass (Da): 31415
|
A0A443QQ93 | MYNKKLTILCYAINATGHINALLGIAFALRRRNHRVVFITAKSREGTFLKIGFKEETYEENPIDNRTIESNINSSSEEFKKPAIEQVQWVVNTFERGVERIKFMEKRMREIVSKVKPDVIVIDDIIPHPCFIHSNAPLVYTNSISPLFAIDDERLPPGFFGLPLNERSEWESSRKIFDALKEKVWNKMNNWLEENGIQKLAKFRVQHRSSNLNIYMYPKPLMEDFLRLCPLGEEWMGLDHSIRESVEKFNLPENFKRENERLIYLSMGSLVSIIAELMSHLTQILSKCKHKIIVVTGKSHQEYNLAENMWGEPFLPQLEI... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 431
Sequence Mass (Da): 49973
Location Topology: Single-pass membrane protein
|
A0A1Z4RX01 | MSLAVEYRPIRFDQIVGQSVAVNIAVASLNQPQIHTTYILVGSSGSGKTTLARIIARAINCKQRDGFEPCNQCDSCQAHLRNQHLDINEIDGADRNGVDDVREIIEQCKLNTVISKYRVYIIDEAHQMSKPAQNALLKILEEPPRNTIFLLCTTEEDKLLETIRSRARILRFNTVNRDLVIGYLNSVAHNEKIPLTEEEANIIYDYNKGSIRQCLQTLGTISPQVTVADLCPQISLHEIQNLFLAFEMRDYLTINNIVQRIIEQGFYPKQLLISLVDTAINMMTMPNIKSEFIFNLNRVLEVILPAVNRLGTSSNAVTNC... | 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: 408
Seq... |
A0A7V6LAV0 | MNILRKVFIKFYSSYMRIKALLIHILLSLDLITKACFYDADIVLIPSILKLEGHKNYGMAFSMFSNNPAYVTVFAVILTAFLIFVFIRYSNENNMLAYGIILMLAGSIGNLIDRLVHGYVVDFICPLFVDFAVFNIADSLITIGAAMSCIYILLNLEKGKWKST | 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-, ... |
A0A2T4JTB7 | MGRLTTHVLDTARGLPAAGVRIALYRLSEAGREPVGETVTNADGRTDAPMLAGEALVAGVYELVFFAGDYLRASGQAEAGPLFLDEIPIRFGVADAAAHYHVPLLLSPFAYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 117
Sequence Mass (Da): 12380
|
A0A914IV91 | MSADSEILDAPTKTVSSATDFYFIAENGSRLKISYPFRPYLYLGAIPGTEFQVASYLNKKYPIAHVEKENLDSXXXXQHMICHITCVFVLMRKSVGLWYKISGCDPSKQKPKITRNLDLIDAPNPVVCAFDIETTKLPLKFPDSSIDQIMMISYMIDGRGYLIINGEIISEDIDEFAYTPRPEYKGEFKVFNEKDEKQVLKKFFAHLLKVKPHVMVTYNGDFFDWPFVEARAEFHGLKMYDEVGFYKDSQDEYKHINSIHMDAFRWVQRDS | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 271
Sequence Mass (Da): 31413
|
A0A074YHB6 | MSGTPVSYASHPPHGHPENQGPTTQNADRASTASHPPSTKPDPTTTAPHPKLNPHGAKGSIPSSSSSGPAELSDLKVRLRNALRQYPDFPSKGILFEDIMPIFSSPQLHADLVKALELEVRSKFDKTPDVIVGLESRGFLFGPSLALRLNAGFVPVRKQGKLPGKLETEGYEKEYGTDFFQIQSDAIKKGQTVLVVDDIMATGGSAMAAGNLVSKIGGDIMGYLFLMELEFLHGRDKLNAPVVTLLSGQDAESREKELPLGQTKESAEDVKSVQDAGGAGASKQP | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4.2.7
Subcellular Location: Cytoplasm
Sequence Length: 285
Sequence Mass (Da): 30364
|
A0A267TGZ3 | MSEIIVGLDIGSKQVSVVAGRLDNMGKLEILGLGKGDTTGQVSKGVVLNVNKTIDAVRNAIMQVEQQANIDIRGVIASVAGPNIAGIKHKAMITRNTSGEEVTVTDVDQVASDAERTFISQGNSIVHTLPQEYVVDSSTGIQEPVGISGLKLQGDFLMITSPTLALDKTKRCIERAKEKMEIEGGLVFSPLAASLAVLSEQEKKSGVALVDIGSGTTEIAIFYKNIVRYISVLPYAGDIITADVEQGCNVSNEHAEVLKVRFGNALASQVPFEETISIPGINGRKPKVVSVKNLSIIIEERLKEIAALVVAEISRSGFGN... | 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: 454
Sequence Mass (Da): 48890
Location Topology: Peripheral membrane protein
|
A0A267T313 | MIHQTMPSIKVISLSYKTADVAVRGQLQFSEEEVQTFLANFQAHEDVKSLMLLSTCNRTELYFESETTSAKDMIEQMLTFKNVWIGGHLLKVIETTQESAQYMMEVATGLHSMVLGDKQIIQQVKSAYLQSQSMGLISGAFERLFQQVFRSFKRISNETAFLKGSQSTSYLAVEHARRLVGKQAKVLLLGAGEIAKDVVKYLVSQGFENVVIANRTLEKAQALAKSRDSYFYLPFSEIPQYFSDFDVVISSIGVKDLIQDTFFRKSTFPKVLVDLAVPASISISEETKQSVQLINIDTLVEKIQVNKTESQAAVNEVQTI... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A2D3R8B3 | MNFQKNLLKKIIIPKKYSGNRIDVTLSCIFPNYSRSKLNYFLRKGEITLNNSNLKPSYKVLGGENVFINLNNTKNINNIYPENIPLNIIYEDNEILIINKPNNLVVHPGAGNKKHTLLNALLYYNKDLQLLPRFGLLNRLDKNTTGLIIIAKKIESYFHLLNQMKNHNIKKYYLTLVHGTLSSNGIINTFYGRNPNNRLKMSVLNNGKIATTSFSVQKKYHYLTLVKVKLITGRTHQIRVHMSYINHPIIGDQLYGKKICFSKKINYKLINILTNFKRQALHAYKLSFIHPNTKKIIKFISPLPKDFKSILIELEKDIIL... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 321
Sequence Mass (Da): 37223
|
A0A914FU79 | MVCFGWSIGCAPKVYWDIHFIYLTQAAFYVHSIYATLYMDIWRKDSKLMCIHHFVALALIGLSYGSGHVLEGAFVVFLHDNTDMMLELTKLCVYLKKRENGDYYPLLNFLGGIAFVSFAIMWFVFRLYWYPLKLLYMTLYGGVYLGPQDSPFYLYLGFMLVILLFMNIYWFNFIARMVFRVCQTGEEPEDNREWDTTAVSGIPREKLQKLAMEGKLAAATSEVVKKKAD | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Membrane
Sequence Length: 229
Sequence Mass (Da): 26639
Location Topology: Multi-pass membrane protein
|
A0A3N0ZSV8 | MKKLIKNLSIVELQDFFYEYSQPKYRAEQVFKELYLNRVSDFSAMTTIPKDFREILDTNFHINSITEYQTQKSADGTIKFLFQLRDGQKIESVLIPDERRKSFDKLKMTETEKLRMTETDKLRMTETVKLRMTETDKLRMTETDKLRMTETDKLKMTETNKLRMTLCVSSQVGCTLNCTFCATGKLGFKRNLETAEIIDQMLFAEKVAGVKLSNIVFMGMGEPTYNLANVIKAIKIISSPNNQLLSPKRITVSTVGVVKKIRELADSGLKVKLAVSLHATNDLIRQQLMPYAERVTLKAIGDAIEYYYRKTKLDITYEYI... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-... |
A0A651FS60 | MSTTPVPPPSAGAPLERDQEVLSNEPEPSPAAQKVTLDLDDAPFLEDIEEETPKDDHNEVQDLVSSGEEEDRPSKVSPKLLIGIGITVILVLAGLTFWLTRSPPAEPVTLTEPDTFQEVQPAPMAEPEPEEFTINLAPFWVAFAEDDGIAFLSLRLILVLHDPSLYLETQRKNIILRDAVYYFLNNRPLPQIKHADAAENLKTDLKAVMNQHLSRPLTDILIEEYMVR | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 228
Sequence Mass (Da): 25468
Location Topology: Single-pass membrane protein
|
T0N0Y6 | MWIGIDDTDSRNAGCTTYIAFRIVSTFADRIISLPRLVRLNPNLKYKTRGNGALSIRIGNRTEETKTVIGKSDGKKISLGLQNNEMEPDFPKTYDNSMIEQVVGIVEEYYEKNQTNTNPGIVFSNKKFDTDIYRNALERDIPVDYIEEILKKTDSIYRKIGSGRGIIGAVSSIAWDRNRTTYELLNYKYPRGGYVDDMVKTIIGKIAESYDSTFNNMEMKEGKVCLFPKDRTPVIYGIRGLVFDDLIQIQEEINSRFPDFDRNYMIFATNQGTDDHILRLESGMELRELSSYEITGYVNELPLRKEGGHLFFGIKYGVTD... | Function: ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
Catalytic Activity: agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H... |
Q7TV33 | MPLLPKNETSNSQAPRNFALVFLLVDFVLMLVVFSRMFDGQDGGLQLVERVSWIPFIGLEWSLGADGLSAPLVVLSGLITLLAVAASWKVQSKTRLYFALLLVQASAQGLVFLSQDFLLFFLAWELELVPVYLLIAIWGGSRRLYAATKFILYTALASLLILISGLALALSGGEFTLNLTELANRSPEGSLGLLCYLGFLVGFGVKLPMFPLHTWLPDAHGEANAPVSMLLAGVLLKMGGYALLRFNVQMLPDAHLQLAPALIVIGIVNIIYGAFNAFAQDNVKRRIACSSVSHMGFVLLGIGAIDALGISGAMLQMISH... | Function: NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hyd... |
A0A101FKR7 | MGEVLHLLQAEDRGEDEGQVTSAFQEPFSGDRNEDFDEDEFKGTSISLEAAEDSPRLDLFLARELGISRSYAKSLVIEGRVRTQKEEARLKPSSKVRAGASFAISLPPPRELELEPEPVAFGVIYEDDDIAVVDKPAGLVVAPAPGHWRGTLLHGLLYRFPSMRVINGTERPGIVHRLDAGTSGLMVVAKNLHAQSFLMESFRQRKVKKEYIALVKGSLPRKEGSVDAPIGRDPRNRLRMAVVPRGKPAITHYEVLWLRQGCSLTICRPVTGRTHQIRVHMSHLGCPIVGDVLYSPKSGEYLGRPFLHAWRLAFLHPTRG... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 344
Sequence Mass (Da): 38478
|
W9H1A8 | MSEQSQNNEMTFQQTLKNPINCTGIGLHSGSKVSMCLKPSDVNTGIVFVRTDQPADRATVRADWDRVTDTRLCTLISNDAGVTIGTIEHLMAALRGCGIDNAVIELNGPEVPIMDGSSAPFVFLIECAGIQQQDKPRRFIKILKQVTVGDGTKFATLTPSPVTGFSFEIDFASAAIARQEGYVKLGNGAFKAELARARTFGFLQEVDQMRKLGLARGGSLDNAIVINGDKVLNEGGLRFTDEFVRHKILDSIGDLYLAGAPIIGHFHGCRSGHALNNQLLRALFADETAWTYVDADEIGAFPADWMAVEKVAAVA | 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... |
U2RVP2 | MAVVRTERGLDRLVNFSDATVAIAITLLILPLVDQADDAASDIGAWIRDNYWELIAFAVSFLVIARFWMTHHRIFEWVVSYDVRIIWLNFLWLLSIVIMPFTTNVLAAGKSGQSAVYALYIGNMLLVSVSMQFIAIVLRRTPELVRDDAKDEMDASRGWLADILLLLALVLAVLFPHIGIWWLFVLFLQGPLSALVKAVRRRPGATS | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 207
Sequence Mass (Da): 23342
Location Topology: Multi-pass membrane protein
|
A0A449A4I9 | MAIFNLENIQKRILNKKYKYIDLVRMLKIPKNQNFDFSKFLKSAVEKNKLFLTKDDEYFYLEKLGETVGKIKINNKGFGFVDDEDKSYFVPKKFLNNALNNDVVQISIFKEDSNDEKYMAIVDKVITRSDNFYYGYIVKNDVYFDFVSIDKKINGKFKWDKQYSLEENDVVKIKVIEATKYFYRISLVEKLGKIQDKFMDMKIAINSSEVPHSFSEKIRNYASTLPEEVSINDLKERIDLRHETIVTIDGKSTKDFDDAISIKKTQNNTFILGVHIADVSYYVNDEDIIDIEAKKRGTSIYLPHTVIPMLPFELSNGICS... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 689
Sequence Mass (Da): 804... |
A0A7D6W348 | MMSLTLALFMLLMYLIISKMVNTYQNTSKLSPFECGFEPMSNMRAPFSVKFFMLIILFVIFDVELALLFPLSFMNFFQISLKLILTLLVILIILLVGVFLEWHNGALDWKLY | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
I0IB92 | MLASRRSPLARVQTEAVAAALREAWPGLEPAFLWQRSTGDRVLDRPLADVGGKGLFVKELDAAVCSGAAAAAVHSLKDVPTRLAPGLVIAATPRRAPVEDVLLCGAGAAGFSALPAGATLGTSSPRRAAQALRANPRLRVVLLRGNVGSRRAAVGLGEPGDGSPTRCDATVLARAGLERLGVSVEAPGHAVLPPEESLPAAGQGAVAVVCREDDAATRERLAPLDDPPTAAAVAAERALVHRLGADCHSPVAVLAAPEAAPGSPGRWRLRARVLSTDGRRCLAAERTCDAGRLMAAAEDAAAELLGAGAAALLAEAASA | 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: 319
Sequence Mass (Da): 32264
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.