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stringlengths 6
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A8HM70 | PPSLLLLLMSSMVESGAGTGWTVYPPLSSNIAHSGSSIDLAIFSLHLAGISSILGAINFITTVINMRPEGMTLDRMPLFVWAVVITAILLLLSLPVLAGAI | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 101
Sequence Mass (Da): 10559
Location Topology: Multi-pass membrane protein
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A0A6C2YSH0 | MGKPVQVLFDSMDSRDLIEIAILAVGIYAVLRFLRRTRGAGIVRGLGIVFCGFFLVAQLLIARFDLTELGKVLDYILATTVFGLLVIFQPELRRGLMLLGQYRGLQFLGVADELPSISKSLTDTALALSKDRVGGLIAVQREQSLQPYIETGERIDSELSIPLLRTIFHDQTPLHDGAVIVQRGRIIAAACQLPLGNPPVGLRTGMRHRAAIGLSDETDALLLIVSEESGRISLAMHGQLEIVPRDQLAKRLAEELDAPSAPAEAKRSYWNRILRAGRKSVTPVS | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 285
Sequence Mass (Da): 31213
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A0A429GJ62 | MNPLIAALVLGIVQGISEWLPISSKTQIMIVSSLLLKLDISEAYSLGLFLESGSLLAAIIYFYREIREIILGIMGRSKKGLRMLLYLVIVTLTTGLVGVPLYLFVEENIKGFIIGIPMILLGIALLFDSLIIKISNKGGDKLFESTGIKHWLIVGISQGIAALPGISRSGMTTSAMLFMGLCAEEAFRLSFLALIPASAGASALTLLMGRSTYSAIGRIGYLGALVAMLISTLVSLAVIKSILRFARRSKVYRITFVLGIIAIISGALSLLTGS | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
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): 29301
Location Topology: Multi-pass membrane protein
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A0A090LMR2 | MTIQYAQDIRNASIWSNVRVLLRWKGSVWKGVYKEFIVWALLFIAIYLLVRFGFNDEQKITFDRVSYAILKFQSFIPLTFMLGFYVTQVVMRWFLIIDNLSFIDSFSIYCTQYISGMDIRSQFMRRSILRYMATSQVLVYRDISPKVRKRFPEYSHIKDQGYLTEDECEKLSHQARNTLAPWWIPVSWAMKLIIDASKEGRLDNGHFGVQDCLGKIMAFKGSLQQLLIYDWFPIPLSYTQIVSIAVRSYFFFCLISRQKGMSNEFYDKKNKSLNLYVPIFTVLQFIIYMGWLKLAEELVNPLGNDDDDIDVDFVLNRNLSAGLGIVDKDLEFTPSIIGDVMYKKPYPKVLNTPEVNEFPYETLLKKGKIN | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 370
Sequence Mass (Da): 43382
Location Topology: Multi-pass membrane protein
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B4F857 | MVASAFTVDLDKPLVFQVGHLEEQYQEWVHQPIVCKEGPRFFENDILEFLTRTKWWAVPLIWLPIVCWCLSTSIKMGNTITDVAMMIGFGIFLWTLIEYVLHRFLFHIKTKSYWGNTAHYLLHGCHHKHPMDGLRLVFPPAAAAILCFPFWNMIKLFSTPSTTPGLFGGGLLGYVIYDCTHYYLHHGQPSSDPAKYLKKYHLNHHFRIQTKGFGITSTLWDHVFGTLPSTKTVDKSI | Catalytic Activity: a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+)
EC: 4.1.99.5
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 237
Sequence Mass (Da): 27342
Location Topology: Multi-pass membrane protein
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A0A090LV22 | MSYLSEIYTIPVVKRYVSTTLSMSNFIRINFKLISFFLPLIISFSSFGFWLKVNFFKEQPKLKFTKEYMISLDYNDKKIFWSSFQNYNELYKNNLVIPSLNFIEMDSNFDKIMDSIQIDMTFDNVTKNNNTIGRIFFGFLFETILDYRINWKFKTFVMGEYFLLKNGPINQINCFGDLYLESINEYIDMNDMNKNINITQNILNTTDISIDLFYKYIRDIKYSLEGRKFICNTMYNINSTSTNLSFSYKIPEQIIFYKTSIFELIKWGLIQYITFAILIRSFLNQFLKFLCINNCLDTWIDK | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: Cell projection
Sequence Length: 302
Sequence Mass (Da): 36192
Location Topology: Multi-pass membrane protein
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A9S3T7 | MARILRASCIFALVCVIAISLSVNQVDALDYNYYRKSCPQAESIIFREVQRYFKKDPTVAPGLLRLIFHDCFVRGCDASVLLSGRRSERASAINARLHGFQVIDAAKHYLEDACPRTVSCADILAYASRDAVVLTGGKGWRVIAGRRDGRISNKIEPEQNIPTAFASVNELVSTFAQQGLNTEDMVVLSGAHTIGVTHCNHISDRIYNPVDKTMPKDLLKSLQKSCPKASSPTSLVMDRKSVHKFDTEYFRNIRAGYGLMTSDQGLYREDFTRPIVDANLNQRAFVNRFAEAMFKLQFIQPLEAPDGEIRRRCQCRN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 317
Sequence Mass (Da): 35603
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A0A0N4UN75 | MMSHFQLLNENKCAPPVAVFFTCMDARIDPLNLTHTQAGDMYIVRNAGNMVPNSLTFGLCGQEILAETEPAALDLTLNRSKIKHAVVCGHSDCKAMKLLRNIYENPHEFDLSSPLHQWVRKRGYRSVDKLQERLKKGNSKIVFASNDNVFSFRALIDPENTLNIVDILSQINTLQQVENITSHGFLKDLIAKNQIHLHALWLDITNADIYLFSKKHERFIIIDEKTVNDLLKEVMDD | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 237
Sequence Mass (Da): 27044
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C0HFD0 | MEGQFQVGKEEVIQAWYMDDSEEDQRLPHHREPKEFIPLDKLSELGILSWRLNADDWENDENLKKIREARGYSYMDICDVCPEKLPNYEAKIKNFFEEHLHTDEEIRYCLEGSGYFDVRDQDDQWIRVAVKKGGMIVLPAGMYHRFTLDSDNYIKVSLTSFSVHTMSFVLFNSGNC | Cofactor: Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6.
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+)
Subcellular Location: Cytoplasm
Sequence Length: 176
Sequence Mass (Da): 20727
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A0A0N4URY9 | MKIALIGCAIWAHHIYTVGKNSCAYFAATIVIAVPIGAKVFTWLTTFMRKRSSFSGEKNSSN | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 62
Sequence Mass (Da): 6810
Location Topology: Multi-pass membrane protein
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A0A2K1KWE4 | MARGNKTKPVIEMTKWFDTNYHHIVPELSGETKFIYSSHKAVSEYKEAKELGIDTVPVLVGPVTYLLLSKGDKSAPKGFDTLSLLDAILPVYKEVITELKEAGASWIQLDEPKLVMDLEAAQFEAFKKAYAVLGELPGVKLLVKMYFTDLPSKAYQTLCELPIAGFGVDLVRYNVLVSTSCSLLHCAVDLKNETKLDVELKSWMAFAAQKLLEVVAIAKVVSGEKDEEFFSANAIALESRRNSPRVHNKAVKELAATLAGSELRRATSVSHRLEEQQKYLSLPILPTTTIGSFPQTPELRRVRREVKSRKISEEDYDKAIKAEIDSVVKLQEELDIDVLVHVEPERNDMVEYFGEQLNGFCFSANGWVQSYGSRCVKPSIIFGDVSRSMAMTVYWSTYAQSVTKRPMNGMLTGPVTILNWTFVRNDHPRSETCYQIALPIKDEVEDLEKANVTPEHADYLRWAVHGFRITTCGVKDTIQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGLRSAHLHDINSPRIPPTEEMADSARKMLAVLESKVLRINPDCGLKTRKYGEVVPALTNMVNAAKPLRAALAKLKSRR | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
EC: 2.1.1.14
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Length: 599
Sequence Mass (Da): 67285
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A0A090L467 | MKLVANFGTLLPSISLLEKYGVLHKLGFKLIEIPNPYTEEAEKLLLESQKYGMKHILINAPAGNNKGIAINASKSEMEESINIAVKYANILGVKKVHVMAGVIDDKNICKEIIHETYVRNLKIANKILEENNIECLIEPINNYTVPGYFLSSYQQALDIINMVDSENIKILYDLFHAQQIQGQLIQFAISNMSKIGHLQGAQVPSRGIFIKDGEINYPYVLSELGKINCNWMIGAECFLEADDIKKLINKNYDGIENFSFMNEWLTKCNLEL | Function: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
EC: 5.3.1.22
Catalytic Activity: 3-hydroxypyruvate = 2-hydroxy-3-oxopropanoate
Sequence Length: 272
Sequence Mass (Da): 30744
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B4FCJ7 | MPAGRSAPARGAAVAAMLLLTMLARLPCLEAQSSRRPTVLTVDMTGKGDYRTIQEAIDAIPAAANNSTSAAIVTINVNPGIYTEKVVVNKAGVSLVGRSATSTIVTWSGPWNQNHQSEFALYVQATDFVAKGLTFQNTLGSKDNGPAVAAKVDADKAAFYDCRFLSYQDTLLDATGRHYYRGCYIEGATDFIFGTGKAFFESCHLHSTSDAKGAFTAQRRSTESENAGFSFFRCESTGTGVATAILGRPWGPYARVVFALCNMSNTVAPEGWNNWDNTANEKTAFFGQFQCYGQGSGTQGRVTWAHNNLSPNEAAPFLTNAWVDGQDWLRPQ | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 332
Sequence Mass (Da): 35779
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A0A0V1LB36 | MSSAPEIEQSDILIRMGSILNSEMEPMKKRFRALFTLRNLGGHAAIDAICESFTSSSALLKHELAYCLGQMGDRYAKPMLEQVLKDENQEPIVRHEAAEALGAIADPSAISVLSLYKNSAIKEIAQTCELALQRIEWINSSPEVCLSNGDTTIEPVPPYPEHLRQLLSIENLEIILLDCTAKLWDRYQALFTLKHIGLESDGSALLRHEVAFVLGQLANPVAMDVLQRRLCKMDENCMVRHECAEALGAIGNLECRRILEQFLQDKERVVRESCEFLDSVHKGILYFHMH | Cofactor: Binds 2 Fe(2+) ions per subunit.
Pathway: Protein modification; eIF5A hypusination.
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
EC: 1.14.99.29
Catalytic Activity: [eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A + H2O
Sequence Length: 290
Sequence Mass (Da): 32647
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A0A429GK21 | MPKEQLSTKLKPDEIERLKKLLEDMNCISSGLSDHEIFRAKVRDSQIIVYKSGVVVYHQDVMPIISSSLLEDEAVEVGSDEAGKGEIEGPIVVAAVVLDGNARRELRTMGLMESKSIPKKRLFIMRNLIKSKCISLDLEVIEPEEFLSSWKRGNLNDLLVEWHKKAIIKVTKEVRVDRIIIDAFDRTKILSAVEPIAKEIGASLVVEERADENYPTVAAASILARATRDDLIKEGHTERKWRL | 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.
Sequence Length: 243
Sequence Mass (Da): 27428
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A0A183HIC5 | MCDFDVRVLGNKHRHTVQCVLMINMFNEKIYLFLWWWILLVIVSTIGSLIYWYCMCFSENQQYSFIAQYLRVYGLLDEQG | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 9711
Location Topology: Multi-pass membrane protein
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A0A1D6G8I9 | MQDDFDIGNVGANDTDLATDETAPQEPSDVGASGGPPRVRIERFPVCPESMREYIPCLDNEDDIKRLPSTERGERFERHCPAKDKGLSCLVPAPNGYKAPIPWPRSRDEVWFSNVPHTRLIDDKGGQNWITKVKDKFRFPGGGTQFIHGAINT | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 153
Sequence Mass (Da): 17078
Location Topology: Single-pass type II membrane protein
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A0A183K4G5 | MSSNKRFNLVTNFLREKFKNNHFIDVRHGGRHGYPRHAGDLGNIRVGHNSVMIFDLYVSLKGLEPYDGFIGRSLVIHANMDDLGRNADEGSRTTGNSGPRLACATIGYRAP | 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: 111
Sequence Mass (Da): 12358
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D8YJ42 | TLYFIXGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVESGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 216
Sequence Mass (Da): 23170
Location Topology: Multi-pass membrane protein
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A0A183HXN2 | MDKSSEQLKVNKWDGPSVRNTIDDAIRKVFNEKYDNWTERHTLADGRLIISTVAVAFAAFALIYDYYESFPKSKP | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 75
Sequence Mass (Da): 8673
Location Topology: Multi-pass membrane protein
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A0A962VM57 | MTSFSSPPVWLLTLIETVLNGVLRLQPDFMASVNTQLHDKIIQVQLPGPHWEFVLQPGAGGIRITAAAENPPDLTLRATPAALLKLAQGEWVSGPELEIHGDIQLARQLQLLVQEWDSDWEEWLARAFGDIPAYHISNMLRSGFNWGQETLNTVQSDLGEYLQYEAQTLPSPHAVQQFLQDVDELRDAVERLDARLMRVQHALNSVAR | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access their SCP2-bound polyprenyl substrates.
Subcellular Location: Cytoplasm
Sequence Length: 208
Sequence Mass (Da): 23378
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A0A089ZVL9 | MRAVILTAGEGTRMRPLTLTRPKTMLPVGGKPLLEYNIRALRDAGIKDITLIVGYQKEAVMDHFQDGHNLGVNINYVTQEERLGTAHAIGQVADLALETNDAIIVTNGDIILGNQLIKSLIDKYNKSQAQSILVLTEVDDPSSFGVVELEGDCINDVVEKPAPGEAPSNLINAGIYLFDPSIFQAIAQTDKSERGEYEITDSLKIQIKEGKKVLGLVSQDKWIDVGRPWEFLELNEHYLEASHEQIEGEIEEGVTIHGPVVLKKGSIIRSGTYIMGPVYIGENCDIGPNTFLRKHTSIGNDVNVGNAVEIKNSIIMDGTNVNHLSYVGDSIIGANCNIAAGTNIANLRFDDEGVKVTVKGKRVDSGRRKMGVIFADGVKTGINSSFNPGVTIGLNSSVGSGAIIYRDIPDNKIVIHHQKQEIKDKK | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
EC: 2.3.1.157
Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sequence Length: 426
Sequence Mass (Da): 46333
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A0A2S0L4Z3 | MMLYPAINELNKLTDSRYTLVVLTAKRARDIIDGKPVLTDVEAERPVSLATNEIAEGLITYKRSDEHDEEAPTFENFELDINCEAAVASEAAQEETSDEVQSDAEAEEPAVDETGLDA | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 118
Sequence Mass (Da): 12974
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A0A671DQK1 | MAQGLIEVERKFIPGPGTEERLQELGGILEHHVTFQDIYYDTPELSLMRADHWLRQRQNSGWELKCPGAAGVSGPHTKYVELTAEPAIVAQLCEVLGAGVLGAGGVAAVLGPLKLQEVASFVTKRRAWKLVLSRANEEEPLLRVDLDTADFGYAVGEVEAMVHEEAEVPAALEKINKLSSMLGVPAQEKVPAKLIVYLQRFRPQYYQRLLEVHSSREKPQGTKDADSSLG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
EC: 3.6.1.28
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 25324
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A0A1C6E120 | MEKLISIIEKTLVPVANKLSQNKYLSAISGGCMSTLGIIMVGAVFTILTNISWQPYTDLLASTGLDQLFTGVQNVTTNLLAVYMAFAVGYRGATVFENKKYTLTSGFLSLFAYMLLVPLDTTTLADSGISFFNISYLGTKGVFVALLAGLIVSRLLALITEKNIVIKLPDSVPEMVSESLSSLLAGVIITIVFLIFRALFAVTPYGNATDCIYTIIQTPLQSLTGNLPAFIIIILIAQLLWFFGIHGSMTVLPILFPIWLSYIGDNTAAMAAGKTIPHVLNIGLWDLANLGGSGATIGLVILMFFKAKSNQYKSFGKLTLPCGIFSVNEPVIFGLPVILNPIMLIPFIICPIVLVCLGYALIQFGIVTAPIGILGLGSMPPLISGIMQGSLSWGIYQLVAVVISIIIYYPFFKTIDNQALAKEKGEQGE | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular Location: Membrane
Sequence Length: 429
Sequence Mass (Da): 46163
Location Topology: Multi-pass membrane protein
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A0A7V0YIM6 | MSKRILITDPIEKNCIEILESNGFIVDYKPGIKEDEIISIIKDYVVLIVRSGTKVTKKIIDAASSLELIARAGAGVDNIDVNAATHRGIIVMNTPGGNTLSTAEHTMALLLSMCRNIPKANNELKQGIWDRKKYIGTELFGKRIGIIGLGKIGKEVAIRCKAFGMDVLGYDPILTQDAAQKIGVKLVSIDEIFETSDIITVHVPFSNETKNLIDRNALKKCKDGVKIINCARGGIVNEEALLEALNNKKVSAAALDVFENEPPQFPNELISHPNVVVTPHIGASTREAQEKVAVQIAQQIVDYYNNGNLIGAVNAYTLEKNITDEIKPFLELATTLGKFFSQISQENINTINLKYYGSVLDKYRQTLTAAFLIGFLSKKITGTVNYVNAQVLAEETGIKVSEAIEGEHITYKNLMTIESKIDSTKTLISGTIFGLKEIRIVQINEFSMDIHPTKFMLLYENVDKPGMLATVGSILAKNQINIAGLSLGRKQIGEKALTLMNLDSKLAYQTINEIKAIDGVGNIVFIEM | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
EC: 1.1.1.95
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Length: 528
Sequence Mass (Da): 57956
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A0A6U6BLM7 | MAHAHQCLRAESSHPHPPRACSSLRGNLAVREFHAGMADVRGWRWSTEHACRISSLYSTRDPAWRRNVISKPPEESEEVNYLRGVPQENIRNFSIIAHIDHGKSTLSDRLLQLTNTKLSEQRDQYMDKLQVERERGITVKAQSASLFYQQDGKDYLLNLIDTPGHVDFSYEVSRSLAACEGVILLIDASQGIEAQTLANHALATKNGLKIIPCMNKIDLPHADPDRVAAQVHAALGYAKEEILQVSGKTGVGVEELLRAVIERIPPPTGSLQNGLRALVFDTWYETFKGVVSLIRVMEGQIAHGEKFLMKSTDKTYEVHELGIMHPEATPVTRLQAGQVGYILCNMKSPAEARVGDTVCSDASVEALKGFQPPVPMVFAGIYPIDASDFDALNKAISKLLLNDTSVSIFKESSNALGLGFRCGFLGLLHMDVFRQRLEQEHNADIIITNPTVPFRVRLKKNPKEFVTISNPSDFPDQSQVIEFEEPVVKASLLMPTEVNR | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
EC: 3.6.5.n1
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 500
Sequence Mass (Da): 55567
Location Topology: Peripheral membrane protein
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A0A8D0DGM3 | MDNDSTEXKNPSAILLFSFLQNSSNXAFDSELNNLTRHLPLPEFRPCSYSGDLDELQADGNVFGQPQAERPADAWPDEILLQTIGAQLAEMGDALTAEIEAPFVNSLVDCFLERNMSREELVNRFSVAVRAAVQRIPSELEQEKVMLIIAMXLAKKVADAVPSLLERVFRTTVNFINENLLDVVNSLR | Function: Induces caspases and apoptosis. Counters the protective effect of BCL2.
Subcellular Location: Cytoplasm
Sequence Length: 188
Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.
Sequence Mass (Da): 20972
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K7N160 | MTSEKLAGPNLNSLCGFEVIDKIKYLVKEECPITVSCVDILAMAARDVVELRGGPRWDALLGRKDALESSFSGANILIPAPNSSLEVLIDNFKQQGLDIEDLVTLSGSHTIGRARCLSFRQRIYNAKEEYHYGYDHYKRYTSFRRILRSICPVEGRDTKFAPLDFQTPKRFHNHYFINILEGKGLLGSDNVLISHDLDGKTTEQWMVGLIVEFCLYVWFPQHGRYSSLLCNI | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 232
Sequence Mass (Da): 26396
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A0A0G9GJB4 | MDTRPEISRTPPRNIEAEQAVLGAILLKDDAIVEAMEYVKEDDFYTRQHQLLFKTMVALNDNDKPIDVVSMQVELNRQNQLEAVGGIQYLAKLAAAVPTAADVGFYAKIVHDKATARRLIDTATKIASEGYEDADEITDMLDRAEQSILNVAEDNNQSEMQNIEEVVHEAANHTYELSKQQTRVTGLRTGYPQLDNMTTGLHEDELIILAARPAMGKTAFALNIAQNVAVRGDNQPTVAIFSLEMGAESLVNRMLCAEGGINANHLRTGNLDTDEWDALWVAMGSLAGTNVYIDDTAGIKVPEIRAKCRRLKKRTGNLSLIVIDYLQLIEGSNSENRQQEVSEISRQLKKLAKELSVPVIALSQLSRGVEQRQDKRPVMSDIRESGSIEQDADIVAFLYRDDYYTREQQEDGAPQAGSDQEAENSLSEVEVIIEKNRSGPRGTVKLLFNKAYNKFASVDFTPGQGPQ | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 467
Sequence Mass (Da): 51812
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A0A6U5HXT2 | MVFHIPGELFEWEGFKNLIDDIALTWLLGIKLVLVVGCRSLVDRQLQSMNIETKRHNGRRVTDRDTLDVVKTQAGYARFEIERLLGRALNHGGNRNDKSQKANVVSGNFYTSQPLGVLNGVDFEFSGKIRRIDIDKVHQAHKNSDVVVMTNLGVSPSGELFNMYSECIAAKVAGELQASKVFYLTTKKDVVFKDSINRVVHSLQASEAKDMLLCNNVSLSKQKVIIENESENLPIENEVLEKIGWSVLALENGVKRAHIVCPEDGSILEEIYTVNGSGLLISKDLYEGVRQATSNDTLKIYGLIQPLVDAGVLAKRTKRMIEDDINSYYVLTRDSHIVACGQLHFLGNRNAEICFIASSENSICRDKDVMLGYLERLCFEQGSETIFVLSTQTMQWFWEKGFYPTEFDTLPLSRQMIYDKERKSKVFIKRINDPKDLEEQEQLWNQ | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
EC: 2.3.1.1
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Length: 446
Sequence Mass (Da): 50640
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A0A949SHI4 | MLNKIKETTTFLQSQGIDAPEIGIVLGTGLGGLVKEIEVIKAIDYDKIPHFPVSTVESHHGKLIYGIVKGKKVLAMQGRFHYYEGYDMQQITFPIRVMKQIGVKNLLISNAAGAVNLAFKKSTLMLITDHINLFPSNPLIGKNYPELGPRFPDMSEPYSKKLNNLLKTIAKEKGILLHEGVYVPVTGPNLETRAEYRMIGKLGGDAAGMSTVPEVIVANHMGLPCCAISVLTDECDPDHLAPVSLEEILAAAAIAEPQLTTLYTELIGRL | Pathway: Purine metabolism; purine nucleoside salvage.
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
EC: 2.4.2.1
Sequence Length: 270
Sequence Mass (Da): 29463
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A0A5B8MH77 | MNGNMRARGTAQSNSYGSVQEGGGGEMGMDYGIDLEMAGARPGKAVASDLSKMNPLARCVIAMDKKVLGIFAAVFYCALFFLGLKTSGIAACVLFICAVMLCFSVWLARWVISRGEGTPQMIQVSNAIRDGAEGYFTTQYGTIGQMSFVLTFVIFGVYMFRRVTPEQQQAGMTRTVLAFLTSLSFLLGAFCSAVAGYVGMWVSVRANVRVAGAARRSASEALQVALRAGGFSAMIVVGMTVLGVCSLFSAFCVFFGVHNGYVPIDQIPLLLVGYGFGASFVALFAQLGGGIYTKAADVGADLVGKIEQNIPEDDPRNPAVIADLVGDNVGDCAARGADLFESIAAEIISAMILGGTMAKQSKLQNPIGFIMFPLVVHSLDLVVSAVGIMSVKGQASKTKSSYDIMKGGYSVSIFLAAIGFIITCRTLLYAESAPNAWMYFSACGFVGIACSYCFVFISQYYTDYKYAPVRKIADASATGHGTNIIAGVGVGMEATALPVIVISIAVTAAYWFGKMSGLEDDQGYPTGGLFGTAVACMGMLSTAAYVLTMDIFGPIADNAGGIVEMSDEPESVRAITDELDAVGNTTKATTKGYAIGSAALAAFLLFSAYMDEVSAFNGEKFDMVDIAIPEVWIGGLLGSMLVYLFSAWACAAVGNSAQDVVIEVRRQFQEKPGIMNYEEMPDYARCVSIVAASALKEMKKPGLLAVGAPIAVGVTFRFFGQLTGQTMLGAKVVAGMIMFATVSGILMALFLNTAGGAWDNAKKYVELGAHGGKGSEAHKASITGDTVGDPFKDTAGPSIHVLIKMLATITLVMAPLFLD | EC: 7.1.3.1
Subcellular Location: Membrane
Sequence Length: 819
Sequence Mass (Da): 86164
Location Topology: Multi-pass membrane protein
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A0A1V4H211 | MFDKSILSVYFVAGTQDCTHRSEPTPEQRLLAVLENALQAGITCYQFREKGDNALTCLDKIKKLALDCQALCCQYGVPFVINNDVHLCLDIGADGVHVGQTDMDIHDVARLCRGRAFVGLSHSSLDEIGVSVGHDLADYLAIGAVFDTRSKADAGRAVGVDMVGQVRAMIGNRPLVAIGGIDTTNASLVRANGADGVACVSVIARADDMGAVVGALKGT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 219
Sequence Mass (Da): 23049
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A0A859A7B5 | MTPAQRQQLFERLAQANPHPTTELIWHTPFQLLLAVLLSAQSTDVGVNRVTAPLFPTLQTPQDLLTLGLATFEEAIRTLGLYRTKSRHAIEMAKILVDQHEGQVPETQVELEALPGVGRKTANVVLNTLYGHPTIAVDTHVFRVANRTGLARGTTPLAVEQALLRAVPAPFLQHAHHWLILQGRHICLARAPRCGICPIQDLCDTGKIHV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
EC: 4.2.99.18
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 210
Sequence Mass (Da): 23159
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I7FV68 | WCWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 216
Sequence Mass (Da): 23273
Location Topology: Multi-pass membrane protein
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A0A814G6T3 | MQFLRRFSQIRYLSSIKTNVSPSTKQKELSEIQKLMRNYNNSHESIRTLALFEWMVNISDTKPDFPCYLQIIRACGEVNHFNFCQKVHDFIKNDRTLDQNEYYQLQTKLIYMYAKINRLDFAEQIFQSLTTNTNNQTKHISLFGTLFKSYNMNGQANKTIDVYENELLNNKTIELDAITATCVLNACSDCHRLNIGKHIHNEVIRLKLLDSSNVRLVTALMDMYCKCGSIDRARELFDQYLPELDCIAYSTMMKAYLAANQPNQVLDLFKQLQSTSISPDVSLYLHVISAGKELQQPEQAEFIHRTIRSLHRIYVPCRFQHAQDQSTLVVERALRSIRMDAYETSLIRNFCIIAHVDHGKSTLADRLLELTGTIPKSKENRQVLDKLEVERERGITVKAAAVSMFYPYQNQTYLLNLIDTPGHVDFSTEVARSLSACQSAILLVDAAQGIQAQTVANFLLACDSFMEVIAVINKIDLKEAKVERTIRQIESEFGLPAKNIIQVSAKHGTNCDKILEEIVKQLPSPNYSRTKPLRLFVFDSAFASNINSTVINVAVTDGIVRAGDKIASKLSGKNYTVLETGIFTYPDRVKTDALYAGHVGYIICDTKHVQDAVVGDTFHHQGVNVEPLQTFKVPKPMVFAGFFPFEEAQYNVFEQSIERLALNDTGVRIIPTSNPAFGKGMRIGFLGLLHMEIFNQRLQSEFAQQVITTFPGVAYQCRIVGKDNIKDYGSDLLTISDPLKWPDTNIIRETLEPIVFGQILTPTQFASLVKIICDERRGDLIEEYCIDEKRTLLKYKLPLAEIVYDFFDQLKQITSGYGTFDYEDGGYEKSNIVKMRICINQEEIDELSVLCHAKRAQVVGKEIVTKLKENIDRQQYAVKIEAKVHATVLARQNIPPYKKDVGAKLYGGDKTRLMKLLKRQEEGKERMRSIANIQVPRDAIIAVLKRK | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
EC: 3.6.5.n1
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 947
Sequence Mass (Da): 107912
Location Topology: Peripheral membrane protein
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A0A1F2P3Q4 | MRVEVFTVDDMPRINEGDDLTRLILERVRLEDNDILAIASSVVAKAEGRVRNLSEITPSAEAYRISRKLDEDPRFVEAVLEESCEILIESPFILVRRPDGHVCVNAGVDRSNIEEGKIILLPRDPSASAARIRSRIYESTGRRVSVIITDTNGRAFRVGQTGLAIGTSGISSTRDWVGLRDLFGNVLTITNEAIIDEIAGFANLMMGEGDGGTPAVVIRGLSLFEDVDAFHEIIRDEHEDMILRALRRVRFG | Cofactor: Monovalent cation. The ion could be potassium.
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
EC: 6.3.2.31
Catalytic Activity: GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate
Sequence Length: 252
Sequence Mass (Da): 27931
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A0A1C6D6D4 | MNISQLLEAVKDPSSTLSMGEKLLAGVSVAVLSMAVVFIVLVVIALIITILQRDGSKKVKEDNIELIKQKEDEIKDVNNNEDLGELVSVITAAIAATTGNSTNNIVVRKIQRSNNTKTSWERMAKNTTK | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 129
Sequence Mass (Da): 14037
Location Topology: Single-pass membrane protein
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M2Y6R4 | MISTRAFVSYATWGRKQLVFDKSCKSFSCSNCDNRRSRLLHSNSLSHRRQASLHLCATQQPSKLLERVKFDSNGLVPVVAQQYDTQEVLMLAWMDRQALLVTLKEGRACYYSRSRKSLWRKGETSGQVQWLKDIYIDCDGDSVLIKVDQKGVACHTGRRSCFFL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Length: 164
Sequence Mass (Da): 18847
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A0A315S1D5 | MNREHISYSTPQLLADAVAARTLLLANDILCRPDRERVDIALTGGTDGTAILRALAGSPLLDVPDWSKVHLWWGDERFVAANSAERNAVGASDALLDMLLETKRIARNQIHEMPADRRSQEELAAATDQDNAVALAAAAADYQDELEKELGENGHLDIAMFGLGPDGHFASLFPNMPQVGINDPDVLVTGVTNSPKMPPLRLSLTVPMIVRTDYVWVCGSREGKAEAMGLTFHAQNNPALPASYADAVQQVLWITDEAAGRDC | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Length: 263
Sequence Mass (Da): 28464
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K7LKQ2 | MSSKGLLRGASLTANAVWHRSSFFPKVTVSVHRKLVKFRSFSLTTTCSSLLPPDLPRLAKTAQISLTPNEVEEIAPKIQQVIEWFGQLQGVDLESVEPSIRAETENNLRDNDPETFDHRDALIASVPSYEEPYIKVPRVLSMD | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
EC: 6.3.5.-
Subcellular Location: Mitochondrion
Sequence Length: 143
Sequence Mass (Da): 16035
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I1NBN0 | MTLNYQRFGSYHNKMDSDNYSKEKEGMVLNIAIMVVSMIAIAMVTVSVVAHIDGSKQDAGKNVKTLLSVCTKTEEPEICFRVLKHVGETATVLNYVKAAINATLTELLFVIRPKPRLERSLTLLQQESYKDCLELLSLGKEELESLYLMANFYVDLSELNLDDLLNSLSAVISYQHACTDELIRINSYGVLGYSLQVPILLTRIALAIVDNFSERPNSREPRRLEEFARWFSERERKMIESNQGDNGGEQWPINVVVAQDGSGHFSTIADSLNACPKNKTIACVIYVKRGKYEERVVIPKGVKVFMYGDGPAHTIVSGTNTRDPRIVTTSFRAATFVVMGKGFICKDMGFTAPADITGAPALLVLSDHAAFFNCKIDGNEGTLYAVAQRQFYRDCEILGSVDIIKGDSATVIQNSQIILKPRNSSDLVLRRNVMSAQSRLDKYQTTGLVIQNCTITAQKESMNTLNATTYLGSPYSEYSRTIIMESFLGDVIHPKGWCKWSDNYGIETATFWEFDNRGPGARTDKRVKWNGYSTIFERNQMVSYTVGRFLQADQWLLNRGIPYESGFVVLK | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Subcellular Location: Secreted
Sequence Length: 571
Sequence Mass (Da): 64044
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I1K551 | MNSPIHAPSPPSSSSSCSYNRPPPCLAHASRNFKFPLLLPQAIRTSQKMYRCSGGHVEGSTNTNPLKNYVVGRSTSGWFETQPLVSEQLLNRRLLPVEALVTPTVQDFSDTPLIGDDKIGVLLLNLGGPETLEDVQPFLFNLFADPDIIRLPRLFSFLQKPLAQFVSVLRAPKSKEGYASIGGGSPLRRITDAQAEELRKSLWSKNVPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLESIFRDDEYLVNMQHTVIPSWYQREGYIKAMTNLIEKELRGFDCPEEVMIFFSAHGVPLAYVEEAGDPYKAEMEECVDLIMEELEKRKITNAYTLAYQSRVGPVEWLKPYTDETIIELGEKGVKSLLAVPISFVSEHIETLEEIDVEYKELALNSGIEKWGRVPALGTEPTFISDLADAVIESLPYVGAMAVSNLEARQSLVPLGSVEELLAAYDSQRRELPPPVIVWEWGWTKSAETWNGRAAMLAVLLLLFLEVTTGEGFLHQWGILPLFR | 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: Plastid
Sequence Length: 531
Sequence Mass (Da): 59533
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K7N7I8 | MMTSLFSTFDPTTNMLQINWIIMITPMIILPKWFWIKKSRWNKMMKLMEKKLTMEFKNMTHHKEMMIMSISVFMFIMLMNMMGLFPYIFTATSHLSISMSIALPMWLMMNIYGWTKFTNSMFKHLLPKGTPMMISPMMILIETSGNIIRPVSLSVRLTANMIAGHLLMTLLGNTASMEKTMMILPLQMMLTAFELAISIIQAYVLSTLITLYSSEIP | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Subcellular Location: Membrane
Sequence Length: 217
Sequence Mass (Da): 25169
Location Topology: Multi-pass membrane protein
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A0A0B7GU66 | MFNSINGVLTEKSSESICIETHGIEWSVAVSAKSLDSFGMVGATVRVFTWLYHREDQMRLFGFPTREERALFLDLIKVDGIGPKQALRILSGITAENLETALEEGDVHLLQTIPGVGKKTAQKMVLALKGQLSNIHEIGKSASIPQSEFEDIIQALVQMGYDRKAATEQVEAAASALRSKGANPQENENELFRSAIVALSTGK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 203
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 22146
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K7KY67 | MGTIPCITLLLGGNLTQGLKSSNVKPLTLISIIIAPLFLLPYVLVMQYAMPPAMNISTMAQLFEVGNEEHSVILLWTYSAAAIALTAWLTFLLWLFLKKSKELVEDEFSTESLDCCSQCWSC | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 122
Sequence Mass (Da): 13519
Location Topology: Multi-pass membrane protein
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A9PB08 | MELCPCVKNILLLDFEGKRVASKYFCDDWPTNGAKEAFEKAVFNKTQKTNARSEVEVTMLENNIVVYKFVQDLHFFVTGGEEENEVILATVLQGFFDAVGLLLRFLQCHFLPCSSIHFYAVSTYCHPFCYLISYPF | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Location: Cytoplasm
Sequence Length: 136
Sequence Mass (Da): 15643
Location Topology: Peripheral membrane protein
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A0A086XW11 | MQDATPILPKSHIPVALQDVIHRMATVAASLQTRIARDGLDEVLDELRGQNAGGDGQKALDLIADEAFREALTGSAVRFYASEERDEAEEINPEGAYALAIDPLDGSSNIGVNVSIGTIFAIYPAGVTAEESFLRRGRDLVAAGYVIYGPQCCLVATMGEGVQKYLLDPESGRFRLIRTSIELAPKSWEFAINASNYRHWSRPIRAYIDDCVAGTEGPRTRDFNMRWVASLVAETHRILSRGGVFLYPGDSRKGYERGRLRYLYECAPIAFIVEQAGGAATDGIDLILDHAPRSIHERTPFVFGCAQNVARVSSYHDLPDNETSALFGSRGLFRS | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
EC: 3.1.3.11
Subcellular Location: Cytoplasm
Sequence Length: 335
Sequence Mass (Da): 36742
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S4RDF6 | VVHREFAKERERVENRRAFLKLRRQQQIERELNGYMEWICKAEEVMLAEEDRNAEDKSAFDGEEITSGNPPPNSRPPLSSRWLNVTVLRRATLKKSRTDLIQAEEGLNERFSDITSTGSPFARASIVSVKQETSSYFQRKEKRMRFFIRRMVKSHTFYWTVLCLVGLNTLCVAIVHYDQPVLLTDLLTYAEFVFLGLFLSEMLLKMYGLGTRSYFHSSFNCFDFGVIIGSIFEIIWATIQPGTSFGIRVLRALRLLRIFKVTKYWASLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFEECTPPTNFDTFPAAIMTVFQILTGEDWNVVMYDAIKSQGGINRGTIFCIYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKEEAYQFEPATEQRTPGQLPHDLHVSPVAGRNQPIQDAQGKGGKPRSVWEQRTNELRRINLRASSEALYSELDPEERRRFASSLHIRPDMKSHLDRPLTVSPPSCDGRRVSDVARAAGVAGIPFLPEAGRGGDGGAVAIAIAAFGDRGAADSGGGKQRKQPKEQALEEDREQRAPRRPNDLRPGMEGEDEDLARGRRQRHRAHSTYETDEQEEGKGRCRDDPASKEARQRRNAQTREATKTEQIREGRGERGGVRAPSPGIFGISEKKLSPGEHMKFNTMALTYAVGSKAGHMEDLKSSDKTDVNSKLPNQKINKMDPSVRIPVMITGPSGESADAPGDRNNADNTGNQITRQQEHKDDKITRVVICALVRSDIGALASLKKPDDVAEEEKDEKGDNDDDDDKRHKPILPYSSMFIFSSTNPLRRLCHYIVTLRYFEMCILLVIAMSSIALAAEDPVEADSPWNKILRNFDYVFTGVFTFELFIKMIDLGLVFHPGAYFRDLWNILDFIVVSGALMAYVFS | Function: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This alpha-1B subunit gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group. They are involved in pain signaling. Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.
Subcellular Location: Membrane
Sequence Length: 913
Sequence Mass (Da): 103070
Location Topology: Multi-pass membrane protein
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A9PDB6 | MFDDQDLGFFPNFLGIFIFVLVIAYHYVMADPKYEGN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 37
Sequence Mass (Da): 4348
Location Topology: Single-pass type III membrane protein
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A0A0B7GYF4 | MYKLGILGIGNMGSAILGGILKSKILNADEIIIYNRTYSKIEKYKQQGVHIGDCERTVIEHSENVFVAVTPQVLDSLTDVIKNSMNGEKLIISVVAGKNLLTLKNIFGAKNRYIRVMSNTPATIGEGMSAIIIDESANEKDKTFVNQILHSIGKVVELSEDKLDIFGSFAGTIPAYLYMFAEAIADGAVACGFPREGIYEIISQSILGSAKLQLETKKHPGELKDQVTTPGGMTIAGVAALEEAGLRNALIKAVKDAMAKKLGADMVAFGHSHVKMLETIDGIIVLNPGSTTIPKDGSKSAAIIEDGKARLLEF | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 314
Sequence Mass (Da): 33666
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A0A0N7JDE5 | MPEDRVEGRALIVGDNIDTDTIIPARYLHSTDPRELASHVFEDAPEIRRRLDALEKPVVIVAGRGFGYGSSREHAVLALKAAGVVAVVAESFHRIFYRNALNNGLVVLEAPGLRGRVRDGDYVEIDLSTGEIRVGGETVARARPMPGMLLELLRAGGLKEKLRELARAATPGHGSAGAPG | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
EC: 4.2.1.33
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Length: 180
Sequence Mass (Da): 19322
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A0A088STQ1 | MKNWFFTLSLGALMGVAGSAQAVNWWDIGNLKTSPAQTLKESRELFKQQHPDLPFDKYALGAYAFSPELYSQYQEAMQFNPGDLTLSTGKELWEKPFKNGKTYASCYPNGGKGVAAHYPMYDNKTHQVETIATSINACRVANGEEPLKYGSADMIALQTYLTSLSNGMPVAVKVEGPGATKAFQEGKAYYFMKRGQLGFSCASCHMAYDGKYLRDQIISPLQGETAHFPTYRAAWSAVNTLQKRIQGCNKNVGAQPQPLESTDYRNVEYFMAYLSNGIKINVPGYRP | Cofactor: Binds 2 heme groups per subunit.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
EC: 2.8.5.2
Subcellular Location: Periplasm
Sequence Length: 287
Sequence Mass (Da): 31879
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A0A6G1SJY3 | MAAFAELGVMPEIVQALEKMDWLLPTEIQAEAIPLILGGGDILMASETGTGKTGAFCVPIVQVVYEQIHMSPDQKSADKPAGPAKQSAPDVTALSIDDRDPGLVLSSDMSTAKSKSGQWQGCRANKGIRRSRGAKNSIAYYEVYFLEPGLARVGWSFANARLELGTDRDGWGYGGTAKKSNNKQFLDYGETFGEKWDSIGCLLNLESGDISFTKNRHNLGVAFKIPLDKLERQTLYPTICVKNACCQVLFGHSADYYCNKPDWCVWLNEMGKNLELNPTNRASNTSLNARAAGPLAIILEPSRELAKQTYDCLETFSSGLDIVTELLVGGSNDKKQAGDKTHIVVCTPGRLSEAVSKNQLPLSNVHFFILDEADGLLQQGLENLIRSIASKLPMMFGSGRRMQTICCSATLHNFQVKKLAQDLMYFPTWIDLKGEDSVPDTVHHVVFRVDPLKDTTYTELNGLFCTDGVHANDNVTDALFAGSKRTPAKPEALSEAIKLMKFYYTLRAIENLKMDQGIIFCRTKLDCDNLYDFMQNMNKKTRTDKYACVRLHSSLSQQERTDNLEYFKRGKTKFLICTDVAARGIDVRGVPFVIQVTLPDEKANYVHRIGRVGRADRMGLAVSLVGTVPEKVWYHGCRRRECHDTRLTEAGGCCKWFDELAMLADIEEHLKCSIQEIDRDFKLQVDEFDGKVVYGAKRLEQSSTYEGHVEQLKTIVSHLTELESRAQKNFISLYL | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 735
Domain: The helicase domain is involved in the stimulation of RELA transcriptional activity.
Sequence Mass (Da): 82001
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I1MUY1 | MHSSLQAYSEQDSPPSPGKGSRSNSRKSTGNVDDVRSNGWLDAMKASSPPRKKLIKGSSNQVASIDDDFEDYCSWMLEYPSALDSFEEIIDLAMDKKIAMFLDYDGTLSPIVDDPNCAFMSESMRSTVRSVAKHFPTAIISGRSRDKVFDLVKLTELYYAGSHGMDIIGPVSETLSKNHPNCVKSNDHPGKETTLFQPAREFLSMIDEIFRILVEITKDIQGAKVENHKFCVSVHYRNVEENNWTTIGQRVHDVLKDYPLLRSTHGRKVLEVRPVIDWNKGKAVEFLLESLGLADRNDVLPIYIGDDKTDEDAFKMLRESNRGYGILVSSVRKESNAFYSLRDPNEVMKFLQLLVNWKNQER | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 362
Sequence Mass (Da): 41039
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A0A5A5U3T7 | MLIKGKIVRIVSMQKQRLDLIEMFVVSLGGGIGGSLRYLLSFLPIVGQWPLMTILINWLGTLLLAILGSYLSHRSSRLKRWQAFLGTGILGGFTTFSTMLLQTAQLTQSNIVMAGLYLVMTVVGGVLMIILGQYIGHVLCGERL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 144
Sequence Mass (Da): 15811
Location Topology: Multi-pass membrane protein
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A0A0G4J2J6 | MALLLRRCVRRATVAVAMSGGVDSAVAAVLLKRKGHDVVAIHMTNWSHEEEGINPCEGRRDEDIARAVCDKLKIEFRQISFDREFWQLVFEDFLNGLRIGKTPNPDVLCNFHIKFSLFLRHCLDVQKCDLLATGHYAKFKHGHLLRGADHNIDQTYFLAQVPKCCFERVLFPVGDMTKAEVRRIAQEEGLPNATKPSSTGLCFVGERDFSKFIRQYVKPDPGRFLDVDDQPLDVPYHDGQMFLTIGQRARIGGLPEAVYVSFKRGKDVRVVPGRNHPDLYRESFTIEKPNWIAMSAKHKASSKQGLECLLSIRYRSALGRCRVKEDLMGFTVEMIDLHRAVTPGQYAVFYDGDRVLGSGEIVALGPSLHKLGKPVPVASPDDFLGELIITGDTPEDDRRREQLLSHPF | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
EC: 2.8.1.14
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Length: 408
Sequence Mass (Da): 46059
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I1LY75 | MYRTAAKRLLCGARYYYNGNVGLRFRPPQIFIPSSRFSTSETQPLPIPHATDRTIPVVVTTETENPNSSDSSASSSPSSSSTADDATKPRAKYEDQHTRVLQASLSYVLKLGWTEAALVAGARDVGLSPSIVGSFPRKEAALVEYFMDGCLQRLADKIDSDESLQNLTPSDCISKLIRFRLEMQAPYISTWPQALSIQAQPVNVPTSFKQRAVLVDEIWHAAGDNASDIDWYAKRTILGGIYSTTEIYMLTDTSPDFRDTWAFLDARVKDAFDLKKTIQEAQYLAEAVSTGLGNSFQGFVGKVFQR | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Location: Mitochondrion
Sequence Length: 306
Sequence Mass (Da): 33902
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A0A354FC56 | MGGFLLMLVICYLIGSIPCGYLIGKKNNVDIRRYGSGNIGATNAFRVLGTQVGLLVLFCDALKGFLPVLIVNNIYGPYWGVAAGFAALIGHNWSIFLGFRGGRGVATGAGILIALMPGVVVIAFVVWIIVVLISGYVSLGSIIAALAVPIIALFLHIPWVYFIFAIPAPILVVIRHLPNIRRLKMGTENRISFWK | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 195
Sequence Mass (Da): 21040
Location Topology: Multi-pass membrane protein
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A0A089ZC59 | MKGHSDNNPPEKVWISIYPADNLFFAVGVSPRNQKIVKIFLPQTSREKIQEQVTREFPHFQLTEKYQPLLKKIVKIYKGDCLDFDRDMLDLSTEKSKNKAGPVPNDFDLKVLGIVAEIPRGEVRTYKEVAESLGGRAWRAVGSAMARNPFPLVIPCHRVVRSDLNLGNYGGGVEMKRELLKKEGVKIKGLRVVRP | 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 irreversibly inactivated.
EC: 2.1.1.63
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Length: 195
Sequence Mass (Da): 22098
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A0A2A2JR04 | MDPREAAQYGNLPRLKELLDSGEITANWTDSDECSLLHWAAINNRFQVAELLIRHKCNVNAVGGVLRSTPLHWSARQGHVMMVALLVRNGAIVDKRDVEGFSALHCAAQSGATPVVAYLIAKGQPVDCLDEGRMTPAMWAAFKCTTADPLQILITLGADVNKSDSSYMNTPLHWATVAGNLTAMKTLIRANCDLTSVNRDNESALDIAVRKADVAAIRLLEKEARKRGLINATFLQKITERPVNNCIALNNHRSFILYLMTVVFATLIFDFAILSFWFDIYGSLSWEILKSCDQWLLFTFIVSAVSAVWCFCMLAVQIYQILLEITTNERLNAHRYAHIQVGDNKFDIRSPYS | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 353
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 39453
Location Topology: Multi-pass membrane protein
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A0A1M6N1X6 | MRILGLDVGSKTIGVACSDALLITAQGVETIRRQSDEADFARLRELIKEKEVHRIVVGKPRHMNGDYSENMKKIEEFVERFQQTVPDIDIVYWDERLTTVMAQNVLKEGNVRREKRKKFVDKMAAILILQNYLDAQSH | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 138
Sequence Mass (Da): 15958
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A0A0G4IS24 | MAKAAQAAKKAFDLVFLGNSVLRRTSLPVDVGAITKPETKELMAGMRKVLASTEYGIGLAAPQVGHNVRMLLYLNIVENDLTEEGTERDSLDHFPPPIMMINPVITDRSVEMVNEWEQCLSVPEFTGLVPRHASVSVDYYDEDGVARSVNMKGQDARTVQHEIDHLDGVLFIDRVDLKTNLFVTKEYERILAENPREIVQHEYPDIDFSDVGLSSSAPEGVDFTSDTQRDN | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 231
Sequence Mass (Da): 25778
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D3PP66 | MVVSIANTERATWRDYFWLTKPRVISLLLFTTLAAMFIAAGGWPGLGLFLVVFVGGYMAAGSANVFNMVIDRDIDGRMKRTAQRPTVTHKISSRDATLFATVLMLLSFVLLWWGANLTTALLAMAGLGWYVLVYTLYMKRRFWSNIVIGGAAGAFPPLVGWAAVTGELSLFAWYLFLIIFFWTPVHFWALSLMIKDDYAAVGVPMLPVVRGERETAYQIGLYAILTTVITLVPVLMGELRWVYLLAALLLNGWLLLYSWRLYQTLERNWTLTLYKYSMLYLALLFVAMAIDRALWM | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Cell membrane
Sequence Length: 296
Sequence Mass (Da): 33590
Location Topology: Multi-pass membrane protein
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A0A0E0L068 | MEKATTSGGGGGGTQPPRGVGLPLVEVQAAASLRRSEVLYVVKELLGFVLYMHHQIPAVLQNLENEFASLKEEMTEMALPPAEMKPSDQRKHNTRKREVRRRIEKQEKLMNGLSSVFSALQKALDEVPSIEGVLLILGGSLVRPLFVYDITISHGRFDAGSANEHGASKLAQSVSRKVVPLQMCIKCNIAGIQIDNQQITSILDASIARPTSSPGHGAASSPGHGANPLGLCNSPIPICGSSARGGGPPPEAGRPGSAMSALFNFNSFLTVVLLVICTCTYIKIQFPAILNDRTGFRGFFWKAARIGERLSPWVALGCFAMGISTIFF | Function: Involved in the early part of the secretory pathway.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 328
Sequence Mass (Da): 35153
Location Topology: Single-pass type I membrane protein
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I7JWU7 | MRVAIVAESYFPAVNGVSNTVARTVDYLSGRGHDVLLIAPGDEQPGDAANPRVTVRRLPATHVPPVRSLPVGIPLPRLTTWLKDFRPDVVHLASPFVLGAAGAAAAHRLNLPLVAVFQTDVPGFAARYGLAALEKPAWWLTRTIHQGCAVNLAPSTRSLEQLKEQGVPGLARWGRGVDAETFRPERRSNKLRRSWGAGESDVVVGYVGRLAPEKAVHRLSRLCRTPGVRVVVVGKGPERETLEAALPGAVFTGQLRGEKLGEAFASFDVFVHPGEFETFCQTVQEAHASGVPAIAPNRGGPVDLIDDGVDGFLLPVEGFADALPAKVAELTSPERRDSYRKASLAAVEGRDWGSLMAALEEHYATAIQRGPRPRPGALGGLESGPVGRAGLDKEPREVRRMFDGVGGHYDLANTVLSFGQDRRWRRRNTKRLGAAKGELVLDLAAGTGVSTVELAKNGAYAVSCDFSLGMLKAGRGRDVPMVAGDGLNLPFPDETFDAVTISYGLRNLNDPRAGLEEMARVTKPGGRLTVNEFSTPTVPVAGAVYKEYLMRLLPVVARAVATNPEAYVYLAESIRQWPDQEELAALINRSGWADCGWQNLTFGVVAIHSATKPE | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 614
Sequence Mass (Da): 65999
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A0A1C6D4J2 | MRFVIGGADSGKRDFVRENYGIDEILMADYDSVLTAKAVYGFHIFIKKLMADGKDIVAVIDEISEENHDITIISTEIGYGVVPMDKGDREWRETVGRTCCYIAKKADEVVRVVCGVGNRIK | 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 = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 121
Sequence Mass (Da): 13522
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A0A914WI56 | MTLPQRIRNFIQTRVFTSAVEYFFLSSYTEFFRAKYGDDFPSIPDLMRETQLYFINADPFFEYARPTQHNIIYMGGITMEKPEPMNEEWTKLLENAPGEGIVVFSLGSVARTEYMPMEKKEALVKAFAKFPQFTFFFRIDGDVPTLPKNVRHIGWMPQKELLGWCQFCFTTDQLNFSYPVA | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 181
Sequence Mass (Da): 21241
Location Topology: Single-pass membrane protein
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A0A967Q8G2 | PGMTEGLRILARVKEVHALPVVSDVHDISQVDPAAEVLDIIQIPAFLSRQTDLLVAAGRTGRIVNVKKGQFMAPLDMKNAVGKVESTGNSDIVLTERGASFGYNNLVTDMRSLVIMRELGCPVVFDATHSVQLPGGAGTASAGQRQFVGDLSRAAAAVGIDGLFWEVHENPDEALCDGPNSLYLADVSQMLEKIMAIDKLVKGY | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
EC: 2.5.1.55
Subcellular Location: Cytoplasm
Sequence Length: 204
Sequence Mass (Da): 21771
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A0A3D8IS64 | MLRIALLGIIFCGMSVFGAEGDTQAPTPQTPQDNAQSAQSPLPQVAQNTPQATQPAQPQEAQQPLKKGERDPNISFPPNASIPKTTRDIAPTYPDNFKLEKFQAVPTLNAAIDLAKQGKMKQALKLFKQSCNEGNPAGCFGSGLMHMYGQGTINNQEKAVAYFFEACAGGDSVACTNLAIAYDEGTGVKVDKEKALQYFLVGCEGGDSAGCNNAGWMYANGVGTPKNYYQALNSYNKSCNLGSELGCYNLGLMSNTYNVYGIDKDRLGAIDMNYIACSQGDMVGCANLGYLYATGDAGTPVNYFNAARYFDMACLGGVMSACNNMGVLYDNGRGVLQDKLRAMELFAYACQNGFETACQNYRISNSNSAGIRMFGR | Function: Hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
EC: 3.5.2.6
Subcellular Location: Secreted
Sequence Length: 376
Sequence Mass (Da): 40323
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A0A0W0R6D5 | MKSEIKGNKPQSLFDLAFPAVLLDKKATIIDCNECFLKLVAFPKNKIIASNLRDVFQHKNIAFPLTNLTDAAEFETTIPLGQDKLQANYKWTLTKVKNSKEEMFTLLGVNSEMVSSLENKDTITQSIIDQLPHHYIFWKDKNSVYLGCNHNLATAIGLQSSDEIVGKTDYDLPTTKEQSDTYREDDRWVIETGNPKLNIEETQTLSDGQTRILSTNKTPLRNKAGEIYGVLAIYSDITRQKELEQSLEEAKNKAEAASLAKTEFIANMSHDIRTPLSGVVGMSELLEEIAINEQQKEYAQSINQCAEQLLSLLNGILDVVSADNVNENDIHIENFELKNCLQSLIDLERPSTSLKGLFLNLDIDKRTPVFLFSDRTKIHRILLNLLGNAIKFTKEGGVTIQVDCMKKEKEFTTLRFSVKDTGIGIAQDKLKKVFQRFYRVEASYKGVYTGHGLGLHIAQVYAKLLGSKINVESEEGKGTTFYFDLKCKIGGNPNRDRKEAENLDVKVQNKKTKITNETTSTNAPTILLVEDNAIALKMAEIFALRAGFQLSTAIDGTTALTLVKKNNFSLIVTDIGLPDISGLQLTQLIREWEMQENKKSIPIIGLTAHVGDEAKEECIQAGMNDVFSKPVNLEMMQTIKQYLHPEESSDKNSSDVPLLGADLPNTEKELFAIEQYPLIDMKSGIQNSGNEELLKQMLLLMGNQELPKDVEALKNSYKTKDWNAVEKIAHKMKGGAIYIGTIRMKFACQFLERYIKAGNVTLREPLYEQLLKVVEETVAAINATASPIIS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 790
Sequence Mass (Da): 88480
Location Topology: Multi-pass membrane protein
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A0A3N7FHY5 | MMVDIHINIVVNNNNSQSGDSHMSTMRRLNLTSPLRIVINGSSRMAISSPPQPPLHQPHNCDWSFDFYFPPLNIIASVLRLAWTAEVMRHVINLTVSEVLFVPAIEELIIITRGLILLEGEDEFMFACAHCCLGIMESTFRHGNDWAFVLIAAHGKGFGQASQDARQLFERQGMEPIVDSDITQLNLLPHRSMRWFYLRYCCGCLDCQRTSNLNCHSLAPVFFNWIPHGLSWHCPDNSFFSSVTVAIIDCLNKTIKDNQSRIKPSVPTTRVNS | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 273
Sequence Mass (Da): 30914
Location Topology: Multi-pass membrane protein
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A0A174GM91 | MGVTKESFGFLEDKREAFLYTIENQNGFAVKVTDFGVNIVSLLVKNKEGNIKDVALGYDTLEEYFENGIMFGATVGRNVNRISNARFEIDGKEYHVAKNRGKHNIHSDKEHGFHKVLWDSEIIDDHAVKFTYVSPDGEQGFPGTLVTNIIYTVTETNGLIVSYHAVSDKKTLINLTNHNYFNLGGHESGTIENTKVRIYADEFTPINEDTIPTGEIRKVEHTPMDFREWKKIKNDLYAEDEQLEKGKGYDHNFVIRNKDCGFRKMAEALDEEQGIKMEVYSDLPGLQFYTGNTMKSTKGKGGVIYGKGCGFCMEPHYFPNSINTKEFDAPVFDAGEVYQTVTMYQFVTKED | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 351
Sequence Mass (Da): 39872
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A0A0W0R4C8 | MTITSDQLKKLSDLAYLAVDDTLINQLSSDVQAIVAFVNVLQNVNTSEVAPLLHPLDLTQPLRDDVVTEVNQLQALEKIAPRFEKNYFLVPKVIDKSK | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 98
Sequence Mass (Da): 10963
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A0A173ZCB4 | MFEKIKCFILDMDGTIYLGNELFPFTKDFLKKVEDTGREYYFFTNNSSKSQQAYIEKLGKLGIQIKKDQMMTSSHVIVKYLKEHYEGKSIYVLGTQSLIQEFQYFDMNLTEEDPDIVVLGFDTTLTYEKLSKACHYIRNGCIYFGINPDWNCPMEGGAFIPDCGSIAKLIEASTGRFPEFFGKPSKHTLDYIIQETGYEPDEIAIVGDRLYTDIAVADQSDVMSILVLSGESTREDVKTSDVKPNVILEDLSEITKML | Cofactor: Divalent metal ions. Mg(2+) is the most effective.
Function: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro.
EC: 3.1.3.-
Sequence Length: 258
Sequence Mass (Da): 29412
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B9IHH6 | MNPNLGSSSSTAASPARGEGRGGGGENGGMDKGYKPKRLYQVWRGSNRFFCGGRLIFGPDVASIFLSMLLIAAPAIGFCIKVYNKILDKGTKNPARWYPVFFVGSILTVLDLLFLFLTSSRDPGIVRRNTKPPESDETGDVTPSMEWVNGRTPYLRLPRTKDVMVNGHAVKVKYCDTCLLYRPPRASHCSICNNCVQRFDHHCPWVGQCIGIRNYRFFFMFISTATILCLFVFGFSWVFILDGKSNVWEAISHDVLADFLIVYCFIAVWFVGGLTAFHSYLISTNQTTYENFRYRYDKKENPYNRGVIRNIREIFFSKIPPSMNKFRSFVDEDEYMAVGSLTLNLGDNLVSSKEKIDIEMGAKVAGASNYSLPEILRDLDYDDDSDDNLKMEEDGRPGMDPFSHGELDLKGSVQTSIVGDGSIESVQGPDAFDGVRESARSSRESVQISIAGDGAGEPAQSSIADNGVIESLQSSIAEDGVLIKKSTVEDGTNLAKGTNNNHNCHQTTAPDLQV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 514
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 56878
Location Topology: Multi-pass membrane protein
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A0A246KFQ3 | MPLADNKAALSSPAPTERRDFIHVAAGAMAVGAVGMALWPLINSMNPAADTLALSSVEVDYGKVQLGQQIVVKWRGKPVFIRHRTPKEIAEAVADDHAALRDPATDASRHKPGKAEWLILIGVCTHLGCIPTFGTGDYGGWFCPCHGSHYDTAGRIRKGPAPKNLYLLDYAFLNETRVRLG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
EC: 7.1.1.8
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
Subcellular Location: Membrane
Sequence Length: 181
Sequence Mass (Da): 19556
Location Topology: Single-pass membrane protein
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D3PNW9 | MTLRGIGLHSGEPSTVRFHPAEGPVRFWVGGLELRPLASSVVDTARCTVLGEHNLRLMTVEHLLAALFIRGIWEGLVIEVTGPEIPILDGSAQEWLAALEDFPAQGPQALPLSGAIRVEEGRSSVLAQPAEQFALTATILFPHPRIGYQQVQCPPTPLAALAPARTFGFLHEVEALRARGLIQGASLENALVFSEHGPVNTPRMLYEPVYHKALDFLGDLYLAGRPYRGQFVAHRASHRLHVELAKLLQS | 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.
EC: 3.5.1.108
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Sequence Length: 250
Sequence Mass (Da): 27302
|
A0A0W0R2W6 | MTSLFQVGTVIGFLQGVFDSTFSMEELTKKGNFGLGTVNAVDGELVILDGVCYRINAEGKAEILPAQMCTPFALVTPFVSNKTFTLKNINSFEKLENVLEKDHMATPNIFYAIRIDGNFTSIQFRSEKCQTKTYRPLAETLPTLQTFFNLKNSKGTLVGFYCPKYSQGLCIPQFHFHYLDDKKETGGHVFELEMEEGEVSIIPLRRFEMEAFKSDDFDKMDLDLGILSSVTKVEKKIS | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 238
Sequence Mass (Da): 26855
|
A0A962UY11 | MIHRVLLSLLLLGCLGSGLGLVYTEQYSRNLLDKRSDLQRQQNELELEWQQLRLEQSAITAKAIVHDVARSQLQMVEPEPTDVIYIKP | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 88
Sequence Mass (Da): 10115
Location Topology: Single-pass type II membrane protein
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A0A0R3UHM7 | MHLDGSRHAVELHLHVDGSFRPSTMFQIAKHRGLLLPAKSSEEFSNFLKIHERGNLPELLSKFDCITPIVAGDEEAISQCMTDFLEDCVKKSHLCYVEARLAPHLLVGGGCSVEQVVKTVLEAMLSAATRFNIESRLILTMLRHQPQYASEVISLAKAFQPHGVCAIDLAGDDTPCDGTNTDLAVKEAFREAYLSGVHRTVHAGVDGPSASVREAIYDMFAERIGHGYHVIDDPALYMDVLEKNIHFEMCPLSGWLSGSVPESWRSHPIIQFFGDQGNVSINTDDPTLTGQWRQQEIAMCLTDLGLTSTQIERANINAAQAAFLADVEKEELLGHIAKALGFRTIRD | EC: 3.5.4.4
Subcellular Location: Cell junction
Sequence Length: 347
Sequence Mass (Da): 38293
Location Topology: Peripheral membrane protein
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A0A068X2C1 | MLKKFFLFFVSIGIIYLVVHRLSSENVESQTFFANVRSHNLRTFVPSRLPKNINYSKHTHPLILFVAASDNQISEDARLVISVVQSLRLAAHPLNLVPFFSQVHRLIRAKLFQMVIFGNFLIYFSPPAVVKLALDDYCNANRVVFIAFFQNAHTLRGTPGNDDFAVVDPSYPLLLRRFAPSSSPKGFFLSRESDVLYVARGGQADERDLMDQLPPCRDWQRNYSRCFPLRRDGYPQLLSDVTASVRHFVHLLPDFISVLNRSCVSEESIREEYQKWRRSWAALVPRNSGDADAFQTVAFTQVPLGQGTQLERRSCAFTECSINGTVGCDSEAIYQSLVLKDMGKFDGIERLLFAYRPLQHWSTSLLLNDAIHHFFEDSAVLEYDLGLLRYVHIDIDDVFVASRGDRMTPADVENLVETQNRWRRHFMPGFTFHMGFSGMFFLLGNPQEQLGDEALIQYRHQFKWFCHTYSHLQPHLLSPSELLQQFKLNKQFAEEKDLPIVDGYAVAPHHSGVYPVIPHLYTAWKEVWNINVTTTEGYPKLFPPHSRRGFHYQGVQVLPRQVCGVYTSTMLLNSYPGGVERLDGMAFGGDLFDTLLFRPVNLYMTHYGNYAQDRLALYVFERVFAFLRGWTRLKVQWAPIWRLMEYHLAFNPTERASAPTSMPVHSDPCVNPRHEAIWFPAACISSERRLPAAIIVGPQKTGTTALLAFMAMHPNLQPNRFLSHSPYEEVQFFSNSTIYSKGVAFYNDQFYSPVTGINFEKSATYFDSSLAVVRMAALLPKAKIIVLLRDPMLRAHSWYQHQRAHKVPVALNFTFTEVLNASSLDEAMAIATAAASSSFNAKHLAAQLYQLHLKCVEPSVYATHFRHWLHHYRANRILLVDVERLESDPAEVLRDVQEFLNVSTFIDYSKLLVWSERKGYYCARGGPYPKARQLLKRNGLSRDQWCLSESKGRSYNHSLPSATNRSTPFAESNRQLASLILQYPFWRPSRSHSATDLLPRWLRDL | Pathway: Glycan metabolism; heparan sulfate biosynthesis.
EC: 2.8.2.8
Subcellular Location: Membrane
Sequence Length: 1005
Sequence Mass (Da): 115376
Location Topology: Single-pass type II membrane protein
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Q9SDY6 | MKNMKLCSVMLCLSLAFLLGATAEQCGTQAGGALCPNRLCCSKFGWCGDTDSYCGEGCQSQCKSATPSTPTPTTPSSGGDISRLISSSLFDQMLKYRNDGRCSGHGFYRYDAFIAAAGSFNGFGTTGDDNTRKKEIAAFLAQTSHETTGGWASAPDGPYAWGYCFINEQNQATYCDGGNWPCAAGKKYYGRGPIQLTHNYNYGQAGKALGLDLINNPDLVATDATVSFKTALWFWMTAQGNKPSSHDVITGRWTPSSADSSAGRAPGYGVITNIINGGLECGHGQDNRVQDRIGFYRRYCQMMGISPGDNLDCNNQRPFA | Function: Defense against chitin-containing fungal pathogens.
EC: 3.2.1.14
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Length: 320
Sequence Mass (Da): 34341
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A0A816FDU2 | MLMTSGQPFKYKGSIDCITHAIRNEGVTSSLLKGTGANIGRGIEGAGVLVGFDKLVQLYTGTKFDTNTSGSG | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 72
Sequence Mass (Da): 7468
Location Topology: Multi-pass membrane protein
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I1LS07 | MGVLQSTLLYLILVHSCKIVAYKDQEWKKATATYANDTEGSLITEGACGYGDLHRASYGKHSAGLSTILFNRGSTCGACYEIRCVDHILWCVMGSPSVVVTVTDFCAPNYGLSVDYGGWCNFPREHFEMSRAAFAEIAKNKADIVPVQYRRVKCARSGGMRFTMCGSSHFYQVLISNVGLDGEVFAVKVKGSRTGWIPMARNWGQNWHCNFNFQNQPLSFEVTSSSGKTLTSYNVAPTNWMFGQTFEGKQFEHE | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 254
Sequence Mass (Da): 28276
Location Topology: Peripheral membrane protein
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I1JIY9 | MVSSSAVLADIILKEKLHNLGILGCIMCIAGSIIIVIHAPKEQPITSVLEIWNMATQPAFLAYVGSVIVLVFILVFHFAPRCGHTNVLVFTGICSLMGSLSVMSVKALGTSLKLTFEGKNQLIYPETWFFMLVVAICVIMQMNYLNKALDTFNTAIVSPIYYVMFTTLTILASVIMFKDWDGQSGGTIVSEICGFIIVLSGTIMLHATKDFERSSSFRGSDPLSPTLSARLFTGNGDSLLKQDEENGSPESNMRSRRQELY | Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Location: Cell membrane
Sequence Length: 261
Sequence Mass (Da): 28652
Location Topology: Multi-pass membrane protein
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A0A2S5T740 | MSAPPSVATGPARRWWHAVPAGMRGVLRVVSVGLAAGAALLASATMLAGICYAVAYPHLPDLGELTDYRPRLPMRVYAADGVLLGEYGEERRHFLSLDEIPQVMQDALLSVEDARFHQHGGIDFLRVLGASLHNLVAPLSQGASTITMQLARNFYLPTEKTFTRKLYEAMLALKIESQLGKRQILETYMNQIYLGQRAYGFAAASEIYFGKPLQDVTLAEAALLAGLPQSPSRLDPLVNPQRAKARQLVVLERMYRNGIITREQRDAAGAEPLHYRAREQLPPYARPLAETARRIVVRQYGSEAYTRGLNVHLTVTSSEQEAAYRAVREAVLAHERGRPYRGPEGEVRLPDDPEAVDERVAEALRAHPDRGELLAAVVLEAQPGRLQVMLRDGTTVTLGGPGLALAPHAATSTPLRRGAIVRVWQSQAGAWQLTQLPRVEAALVALDPRDGAVRAWVGGFAPRPGAEERVAQGGREAGTSLAPFIYAAALEQGHTASTVVEWRPGAPEVAGQGEGTVPEARNDVAPLVLRQALAAAQPETTRRLVEALGPDQVQAWLRRFGFDPASPPDGASMTAGTEAITPLQLASAHAVLANGGYRVRPVLVRRLTDADGRVLKETLPRLPGDSARVIDARNAFVITRLLHEASRMNFGGRAGRWLHRPDVQGHAGSTRDGGDAWFAGFQPGVVAVAWVGDEPPRPHGERDAHGKPSLPIWLDYMRFALRDTPVMRPAVPDGVVNIDGQWYYREYTPDSGIRSLDPAPPAGPSLPADSLPSGE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
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: 775
Sequence Mass (Da): 84023
Location Topology: Single-pass type II membrane protein
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A0A5K3EQ37 | MTDTKLSQCRPPKRPFRKNIAAEGDSVIVAYGKSDTQLIQLVRGAVTQNKFGALKHDEIIGKPYGSRIVVPRGHVCILGLDPVIWTQTLPHRTQIIYPTDSSMIVGQLDLVPGFRVLEAGTGSGALTHALAQAVWPTGRVRTFDFHRERVERASAEFAQHGLEEVVTVKYRDVLTDGFPAIGLEHNPDGCHAIMIDLPEPWGVLPGIVNCFQSLGGRVCIFSPCIEQVQRSCENLRTAGFTDIEVVECVSRSYDVVHTVLHVPNLGQKDATELFNGTYVHKKSRTANDGNEGTKGAGCDRHLFPPPTKYVTSTTQPCEMSKGHAPGRHQDGSWEAFPRPKDTGHTGYLTFASLIPRHPQSIGSSGDVPMETEADNDGTVLGDVVE | Function: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Catalytic Activity: adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.220
Subcellular Location: Nucleus
Sequence Length: 385
Sequence Mass (Da): 42037
|
A0A0R0GDI8 | MAEKEMEYRVELFNKMTQTCFNKCVDNRYKESELNMGENSCIDHCASKYWHVTNLIGLLLGSGRPPM | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 67
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 7806
Location Topology: Peripheral membrane protein
|
K7K150 | MESSDEMHSKIITMKQSFFDEGFLIPTQFQELELLQDRDNMNFVRDVFCLFFTDMTRQFSEIEQILREEIDGQPREDMNRLLQRLKGSVLSIGALKILNGVNKMIQLFEEGNLERIMAAFEQVKMESVNLRAKVEPYFQLLESQAESFTESQAPK | Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Location: Cytoplasm
Sequence Length: 155
Domain: Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence Mass (Da): 18155
|
I1L7V1 | MGSELIFRGHEAQPVDDSYSPKPHKPWFTVTRPIHYMLREQRLVFVLVGVIIATLFFTLVPSSSSSSVPYESLPISYFERESKIPAYHHRVAAAVHSVGKVPLGIKRKGLRIVVTGGAGFVGSHLVDRLIARGDSVIVVDNFFTGRKENVMHHFGNPRFELIRHDVVEPLLLEVDQIYHLACPASPVHYKFNPVKTIKTNVVGTLNMLGLAKRVGARFLLTSTSEVYGDPLQHPQKETYWGNVNPIGVRSCYDEGKRTAETLTMDYHRGAGVEVRIARIFNTYGPRMCLDDGRVVSNFVAQALRKEPLTVYGDGKQTRSFQYVSDLVEGLIRLMEGEHVGPFNLGNPGEFTMLELAKVVQETIDPDARIEYRPNTEDDPHKRKPDISRAKDQLGWEPKVDLRKGLPLMVSDFRQRIFGDQKEKASVA | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step 1/1.
Function: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
EC: 4.1.1.35
Sequence Length: 427
Sequence Mass (Da): 48057
|
A0A0R0IR07 | MSMVVKSTTKDSVKCAVVDGGELKSRMPKVVHELKNYLKSCGVDIHVIIKIESANSIPNLHSIISASHGTMVARGDLGAELPIEEVPLLQEEIINLCCNMGKVVIVATYMLESMIVHPTPTRAELSDITIVVREGSDGIMLSGETTHGKFPLKAMQVMHTVTLRTEATIPGGKMPPNIGQVLKNHMSEMFTYTMQP | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 196
Sequence Mass (Da): 21338
|
A0A1E7YTS3 | MSESERERSVFFVSDRTGLTASSYGKSLLAQFRGIRFTTRAVPFVDCLERAQAAAREIEECQARTGQRAIVFSTLVDEAAQRVIVRTGAFVLNLFEAFIGPLEEELAQPSVHTLGRAFRPPGEGVHQRWLDAMEFALAHDDGIHPEHYSDADLILVGVSRSGKTPTALFLAMNFSLKVGNYPLTDADLEHDDLPAPLVAWRDKLVALTIEPETLHTIREKRRASPHYAALSVCRREVRAAERIFRKARIPVFDSTNTSVEELASSILKYHQELAATDARG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
EC: 2.7.11.33
Catalytic Activity: [pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+)
Sequence Length: 280
Sequence Mass (Da): 31203
|
I1JYR7 | MDLMSVECVSSSDGMDEDEIHANHHHSEFSSTKPRNGGTSNINSVGPNGIAPATSVHELLECPVCTNSMYPPIHQCHNGHTLCSTCKTRVHNRCPTCRQELGDIRCLALEKVAESLELPCKYYSLGCPEIFPYYSKLKHETVCNFRPYSCPYAGSECSVVGDIPFLVAHLRDDHKVDMHTGCTFNHRYVKSNPREVENATWMLTLSSLAWPLYTWHSFVLWVMKMRLGIIAIA | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 233
Sequence Mass (Da): 26204
|
A0A6V2JBD9 | MLRINPLTHHLHPHHLPRGNTKWHCSHRPASQVVETSSKEADRVTMLGLWVNLVDEEILQRTYEENEDEFNTPEFATALANMEALREELRNAATTKLRHLLPLSDEQAKDEERAEEWQQWHDMLNPYVEAGDTWLTAPWMVTEFFVYRRFMEAIGYFDPSNEATFMWDPFVKAKRAGLDTSYASAENLMEKVEALPNTKEGVELAAAFALWGNKMDLSIWPADAANSDVDVFSNVLAAAADNLLHDDFIILANHCETLREKKGGVVDIIVDNAGFELVTDLALADHLVASGVAREIRFQLKSHPTFVSDALEKDLMETIETYAALDESTYPFAKKAGQRWKSYIDNKSWTCHENSFWVQGAAMWEMPDKLSKDLNANCDLAFVKGDANYRRLLGDRYWDYTSPFQDVVGAYFPCPVCALRTLKAEVGCGMDKEQVERASSLDDNWLVNGRFGVVHFGTGV | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism.
EC: 3.1.3.-
Catalytic Activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate
Sequence Length: 460
Domain: Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence Mass (Da): 52194
|
A0A2X0RC82 | MKRIVVALGGNAIEAGDNSAAAQEKQVKKTMKVVAKMIENGDQVAIVHGNGPQVGNLLLQQYKGSSKDNLAMPLDTVVSMTQGSIGYWMQKALDDQFKHTNYPHQAVALITQIIVNANDPTFKNPTKPIGPFYTFNEMQR | Pathway: Metabolic intermediate metabolism; carbamoyl phosphate degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.
EC: 2.7.2.2
Catalytic Activity: ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O
Sequence Length: 140
Sequence Mass (Da): 15330
|
A0A0R3U8S6 | MALSAATPAIRGYLLDTDCRWDIVSASVDDRTEEERGLKVISPVPANCIALTSLN | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 55
Sequence Mass (Da): 5920
|
A0A5P9L9H5 | RTSSKTWGKEAWKKIVVCIVSDGRGKINPRTRAVLAGLGVYQDGIAKQQVNGKDVTAHIYEYTTQIGMEVKGTQVLLKPRPGMPVQLLFCLKEKNQKKINSHRWFFQAFGRVLDPNICVLLDAGTKPGRQSIYQLWRAFDLEPM | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
EC: 2.4.1.16
Subcellular Location: Cell membrane
Sequence Length: 144
Sequence Mass (Da): 16317
Location Topology: Multi-pass membrane protein
|
A0A0R0IZZ7 | MQKFRLYETRSKFYMIGRDKNRTFWRVLKIDRLEPSELNIFEDSTLYSDIECCDLLRRIHEGNKSTGGLKFVTTCYGIIGFIKFLEPYYMLLITKRRKIGTICGHTIYAITKSEMVPIPHAIERSKMAYSKDENRYKKLLCSVDLTKDFFFSYSYNVMLSLQRNLSDHNTTGQSLYETLFVWNEFLTRGIRNNLQNTSWTVALVYGFFKQVKLSISDNEFNLTIIARRSRHYAGTRYLKRGVNEKGRVANDVETEQIVFTDARGGRPMQISSVVQIRGSIPLFWSQEASRLNIKPDIILSRKDSNFEATRLHFENLVKRYGNPIIILNLIKTREKKPRETILRAEFANAVRSLNKNLKGENRLRFLHWDLHRHSRCSKATNVLGQLGKVAAYALKLTGIFYCPVTSNVRLDGFSHYSYTENNNVTDHCITEQASINKDNVDKETEIINCYCSSDENKDYSVKPQMLQSGVLRTNCIDCLDRTNVAQYAYGLAALGCQLQALGFVETPYIDLDNPLAKELMEIYESMGDTLAFQYGGSAAHNKIFSERRGQWKAAAQSQEFIRTLQRYYNNTYLDGDKQKAINLLLGHFQPQQGNPALWELDSDQHYTVKKHGLYVADDSVRSTIKRSLSDGNILSESDTTIRNLNVTNDQNSSEKPDKRFLSGSTPDIYTCGSDICHCRQIYVNGQNCESDHICYDEHGDACDCSNFLDVDWLSSSGNSCEEELLERSTSISSENIANELITTETSASESGSSIKGRQSGEELNKDSKYSESFERWITQGEMLFI | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate
Subcellular Location: Vacuole membrane
Sequence Length: 785
Sequence Mass (Da): 89927
Location Topology: Peripheral membrane protein
|
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