ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A523MF25 | MNPRGQPAVSAARQPVSNPSESLILVDDDDREIGFCSKAECHEGNGRLHRAFSVFLFNEAGELLIQQRSEHKPLWPMYWANSCCSHPRESESVVDAGRRRVQEELHVECNLHFLYKFKYQAHFENLGAEHELCHVFTGVIEGVVSAHPEEIAATRFIGPDELTAEIAADPGRFTPWLKLEWERISADFLESILARIP | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isope... |
A0A9D0LNP3 | MGLAFHRIRKHTTRGDKLFDIDEFDIPEGACIILSGQNGAGKTTLLKILAGLEAPDNAEITFDGQRRTWKAARTRLRREVVYLHQQPYMFDHSVADNVAYGLSRQALPKTHIKERVARALAWSGLSHLAQRNARELSGGEQQRVALTRARVLSPRLLLLDEPLANMDISAREQTIQLIRRLKEDGTSTIITSHEPHISRLLGDQHRHLCKTGPCRYTIIKPFLFQRSVEQGVPPSGQTTEAPDPGNGTVMTPQDNDNTVTAVILAGGMARRMDGVDKGLIQLNGRPMIEYIIEALKPQVDHIVINANRNLEQYRRYGYPV... | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2E9VDV2 | MKLLIQRVSEASVTVESKTVASISKGVLILVGFDPLDSIEDINKLTKKLLSFKIFNDDRGRVGLSILEEKAEILIVPQVTLSVNTGKGNKPSFSQAAGPQKGLKLFNLFRDHIKDSYREAEAGIFGANMSVKLVNEGPITYWFES | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0A2E5US21 | MHQQVDKYAVIGNPIGHSKSPKIHRLFGEQLGHKISYGKLEATENTFFAVVEEFFRSGGKGINVTLPFKGLAYEFSDVLGSQAKNCGAVNTLSFSEDGRVYGESTDGIGLIRDLSNNNINIEGRSILLIGAGGTTKSILPSIIDMNPKNITLTNRTEKKAESLRDTFSHLFQIDSVSGENIDRNYDLVINTTSSQLSNTVPSVSAIAIKGAHSYDVNYSYQPTLFQNWSSENGSRSALQGWGMLVEQAAESFSIWRGVHPETVVVVNRLQSEVEN | 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... |
A0A938TQM3 | MTSSRLASTGRSLVLIGDVRDRCHELLPEEQLVLEGLSERRRAEFSTARVLAHQAMQRAGLRQAPVLRNTDRSPRWPDGLQGSLTHSRGLAAAAISTTLAGVGIDLEQQGRLAEAAATRILTAGESAVLGDLDGDFRWLATLAFSAKEAVYKSIYPAVGLYIGYREVTIALHPETASFTARYLGNNPANAVLEAGRGEWWCISDVVLTRFEIEPTPPATAPSSRSEGELACRQR | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provi... |
A0A946YHK1 | MKFLISITVAVLINLGLFLLMDSMVSRESARFVDLIEAQPIEFTRTNMDEETRTRDRRTPPPPKPREIQRPRANVQNIANRVSSLPTDVATYEVTSLLGEGGTSGVAIGRTLLEGSMESLDIMMADELIPLTMLPPQYPPSARMRRIEGWVDMLFTVNADGSVSDPVILDSEPDDIFNRAATDAALRWRFRPVTRDGEPVATLAQILINFSLQNGQ | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A962SB30 | MQATLTVKRLIDEMSSGLGLQWLAGAAAADHLLSRDEDPGGNRPNLIGPLNLISPNRIQVLGAAEVQSLEKYSLDPNAEAMRQLFQSDCNVIIMAEDQSPPPVFIRLAGEYQIALLRSPALSHDIINTLRHRLTRFLTKKIILHGVLMDVLGMGVLITGDSSVGKSELALELISRGHTLVADDAPEFRNIAPDTIEGKCPDLLRDFLEVRGLGVLNIRQMYGHASTRRRKILKFIVHLAAMDYDELANSIDRLDGRQLTRNILGVDILERTIPVAPGRNLAVLVEAAVRNYMLTANGYDAAADLSAKQRSVMEQN | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
A0A3M1X0P2 | MRLTRLYLPEELAPGKELPLPENARRHLIQVLRARPGQRLRLFNGRGGEYEAELVRAERREAIVRVHAFDPVDRESPLDLTLVQGIAKGPRMDLALQKATELGVRRIVPLVCARSSLPGKRLDRKHEHWLGVIASACEQSGRTRLPELFPPLTLDEYLNEPTPQRLFLHPETTPAVQAFGELEREARIDVVVGPEGGLSETERTQLLAAGA | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A974UM20 | MVTYTIDDAPTRNALSLALLADIDRVLATLADDPSVRLIVFTGARTVFSSGADRAELGDPATVERTTALLGSILTRIHESRVPIVARVNGAAFGAGLAIAAAADISIATTDAVFGLPEVRFGLVAGPAAAACLGRIGKAAGLDLLLTGRRFGAAEAARMHLVTGVVDRAALDAAVEGKVADVLLGDADAIAATRRLVHELSGPPLPELLAIARRAAESESQRYDGFVSRGLARGGVPDVDWRDVPARPRRARPGSELKPELRADLPQLGRSVVTIGTFDGVHRGHTEIIARTVASARRLGLASVLLTFDPHPVELTRPGA... | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.1.26
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 573
Sequence Mass (Da): 60606
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A0A850AI09 | MFGIGGMEVLVILIIALLLFGAKRLPELARSLGRSMNEFKYGLHSTLSELEKEVDRQKDSPETKKSNEPTIDKKNHEKS | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 79
Sequenc... |
A0A2E6IWL3 | MAARLIDTINITKMLPDDLLSVYQIEKDSYDFPWSEKIIEDCLFNNYDCFIAKNSRAVGYVIAKISSLDSHILNLTIDANYRGYGIGSSFVDLIIKECRLQGSHSIFLEARVTNSVARKLYQKYGFRSIGLRKNYYKNKSGREDAIVYRKNLIY | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17786
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A0A8T7I2W2 | MNPDVRNNYWVILASLTIALLLDILPLPGILEVYWPKWIVMVLLYWTIALPHRVGIFTAMMVGLFVDAIEGDVLGLNAMSLSIMTYFSSLLYQRIRLFPRWKQSLVIGMLTGIYMLVALGLKSLVMNYEKSFVYWVPMFFSGLFWPWLFILLRDIRRQFKVN | Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 162
Sequence Mass (Da): 18973
Location Topology: Multi-pass membrane protein
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A0A945VMS4 | MTAVALTVALVGNPNCGKTTLFNSLTGRHQRVGNWPGVTVEKKVGTFALADSTNKTVELVDLPGTYSLNATSDNLDEIIAQNFIGACEADLLINLLDASSLARGLYLTQSLLKTQQPMIVVVNMLDVAKDYGLELDLEKLSAELGCPVIGMVAAKGQGVDALKACITEIISSAPKPPVTDQAEAIEQTDIDIYGQIDALLLEATQHTAQPRSHTEVIDSIVMHRILAFPIFLGVMYLMFLISINLGSAFIDFFDLLGSALFVELPRQLLDAIGSPQWLTVFLADGVGGGVQLVGTFIPVIGALFLVLSVLEDSGYMARIA... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 706
Sequence Mass (Da): 75684
Location Topology: Multi-pass membrane protein
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A0A293N9W3 | MRLQIQVADDCDDAPSSDDLQEALQASLLALAQVLPTNLVAVLSEELCVRLCDEDESKQLNRNYRGQEKSTNVLSFGGMADKQTLAPLPSDALKQDLPELPLGDLAICWPVVQAEAQEQGKPVEHHLQHLFMHGVLHLLGFDHEMSEQAEAMERIECEALALLSIPNPYMSVAANA | 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: 176
Sequence Mass (Da): 19325
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A0A520T6Q6 | MGFTEEVNLILIGRLGKPVGLKGYINLIAHSDNPSGLSKYKEFFIDANGIQKLTLDKISKSGKKTLIKFDSINSMSEAEKLKNLDLFIDEDNLPDLPDGEFYWKDLIGKKVISLNNNFNGYVKEIMPTGANDVLVCEINDKEVLIPLIIGKFVIEISEHIIVDWDID | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A965TIX6 | GRLFTAKHAVEMAEMGVRCGASGFIAPATRPEGIAAIRAVVGDRTILSPGVGAQGGSAAAAISAGADYVIVGRSIYKSGDPRAVAKTLCDEIERCADL | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 98
Sequence Mass (Da): 9889
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A0A972R7T9 | MSDFSSPLWAWFIFIVTVGGIFWCFYLLMSQTKLLTKEEGNKIQVTGHKWDEDIEELNTPIPRWWMQMFIATNIFALVYLVLYPGSAIFDGVLGWSQVGQYNTEMKVAEKKYGAQYARYLQQDIAELATNNEALKTGGRLFSTYCTQCHGTDAGGGPSFPNLRDTHWLWGGKPEQISQTINAGRRGTMPAWGAVLGKSGVKDVTAYVLSLSGRKTAGDLKIGKQKFEQLCIGCHTAEGTGNIALGAPDLTDKSWLYGSSHRSIAKSISEGRNGNMPAFGNFLGKSKTHLLAAYVYSLSRTD | Cofactor: Binds 2 heme C groups per subunit.
Pathway: Energy metabolism; oxidative phosphorylation.
Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
Subcellular Location: Cell inner membrane
Sequence Length: 301
Sequence Mass (Da): 33266
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A0A973DLJ2 | EQLLIDAKFTAQAKQKVIIGGPMMGFSLHQINAPILKATNCIIVASDAELPDAPAEQNCIRCGDCEQVCPADLLPAQLVWYAKDQDHQKLKDHDLFDCIECGACAYVCPSSIPLVQYYRIAKSDIRKNEQEQRQADRAKERFELRNQRLERDKLERLERSKKAAEARQKSMSANSDGDVVAAALARIKAKKAAANSGDIQEVNPQDRVAAAIARAKAKKAQQAENQLTSSTDAESPAASDVDPQKARVAAAIARAKAKKAQQAESPASDVDPQKARVAAAIARAKAKRAQQQQVNDQPVVNTDSESPAQEVDPQKARVAA... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 343
Sequence Mass (Da): 37224
Location Topology: Peripheral membrane protein
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A0A7T5RMC6 | MFIQNIRFILLGLLFGILFLLFNYWQSDHIDQPLNINNENNVNMSFDNNYISSLNIDKNDLIDSYHTKSMQRDINDINIISVKTDLYNIKIDTYGGDIIFLELIKYPISGFKNTSGFILFDTSDLRYYVAQCGLLSEYGPDSIKFGKIKFSCEKNFFEMTEEKLYINLTYETVDNIKFIKRFCFKRDNYLIDVEYIVHNESSNCYYGYMYGRLKQTERIFHDNFLMMSARSYIGGAVYTPNKHYKKISFSDMKSSKNFEQQIFGGWIAMVEHYFLGAWIPSQNAEHIYCSEKYDENTYGLRFIDVNPLIVEPGHINSIKS... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A521RBN0 | MATTAIRIVAGLGNPGKDYSGTRHNAGFWFVDRLIAQAGGSFSRDARLQCDSARLRDATLDIRVIKPLTYMNESGRAVGQALNYFKLQPEELLVVHDEVDFPPGVIRLKRDGGHAGHNGLRSIIAHLGANNFTRLRIGVGHPGHKDRMLDAVLGRPSAEEQKLIDAAIARGLAEMPLILAGELEKAMTGLHSGEPTMDPGPDSAP | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 22059
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A0A2G6EWF9 | MTDTATTHHVRAFIALGANLGEPLAQLDSAVAALNQQPGVTCIAMSKVYLSKPHGPQDQPDFTNAVVKIRTVLSAEQLLDTLQAIEFKHGRKRQEHWGARTLDLDIILFGNQQINTPRLTIPHPRAFEREFVIRPLADLDADLVIANRGRVKDLLKRLPANTMETIRNVTTDYC | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A660L2S9 | MTVLLLALAGGLGAVSRFLLSSRLPVPFGTLAVNVSGAFVLGLIGENLVLGTGFAGAYTTFSTWMLETERLSKPAAALNIVGSLALGLAAAQLGITLRTAG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 101
Sequence Mass (Da): 10161
Location Topology: Multi-pass membrane protein
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A0A661END6 | MEKELSWLSFNGRVLQEAMDRKVPLIERLRFLGIFSNNLDEFFRVRVADVNRRIIIAREDPDADLTLKTEKKLLKNIQQKIDELQAQFDETYHHILIELARRNILLINETQLTEEQEKWVREYFHESLLPLLSTWLLDDQEELPQLEEKSIYLAVELDLENGQRLYSLIAIPTEKLGRFVPIPRRYSSGKKAFIILDNIIRHCLADVYNEVMNVARVSAYTIKVTRDAELEKDEAITGSLMENLSTSLKKRLAGTPVRFIYDREMPAAMIHFFAEQFGLGDKENLTAGGRYHNFKDFIKFPAVGRGHLVYERLKHVRSPQ... | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n)... |
A0A2E6PGN8 | MKSVPNTQLGTLVADWPIHMQRAIELSSSVWTATPNPRVGCVIAKHGAIIGEGWHAAPGQAHAEVVALDKAGESAKAATAFVSLEPCSHTGRTGPCCESLIASGIQQVVIAALDPNPAVAGSGVEQMERAGIEVYHLVDFEQKARSVNAGYFKRREEGLPFVRLKLAMSLDGRTALADGRSKWITGTAARGDVQRLRASASAVITGINTVLIDDPFLTVRSSDLSISDEERKLNAKLIERQPLRVIIDSQLQTPGTARILNSGGLVKVYTLNEDIIGKSSSGQCGNYSNR | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
EC: 1.1.1.193
Sequence Length: 290
Sequence Mass (Da): 3090... |
A0A3D0ZV93 | LLHSGRGGGLSDMFGGGLGSQAAGSTVIERNLDRITIILALVFSFTTLALALMMDE | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 56
Sequence Mass (Da): 5796
Location Topology: Multi-pass membrane protein
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A0A1Q7TU58 | MLLASTGLLFAFLVAFSMPIVFALGAAAILGLVLGGYSLEMLASSLIGASQNWILLAIPSFIFAGTVMERCGMSNALVDLARALVGWLRGGLGMSVIVVSYFFSDICGSKMAEVSALGSTLMPPLRRAGYRSADGASLIASGTAMGMLVPPAIFMIVIGEVTNVSVVALFLAGFIPAAVIGVCLCALVAIQAHLLGWPKDTRPSLLFLLRSLRAAAVPLVIPLVILGGFS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 230
Sequence Mass (Da): 23762
Location Topology: Multi-pass membrane protein
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A0A502CQC8 | MSSNLRQLVASMRMMLVLTLLLGVLYPAAVWGIGRVAFADQAGGSLVHRDGAVVGSTLLGQSFTDARFFQGRPSASEYAGGVSGGSNLAASDPDQVKTVKERAAAYAATNSGSAPADALTASSSGLDPQISPANARAQAHRVAAANGLSRAEVMKLVQANTQGRSLGFLGEPRVNVLELNLAVQDAAGR | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
A0A7C1TMK8 | MKRPQTDSRLLPDPSRRRFVQGLAAGGVLLGLGPVVRPALAGDETATRTGMAPFLSGTEFDLVIAETPVNFTGAPRMATTINGSIPGPILRWREGDTVTIRVTNRLPVSTSIHWHGIILPYEMDGVPGVSYPGIAPGETFVYRFKVRQSGTYWYHSHTGFQEQTGMYGAIIIDPADGDRIRADRDYVVQLSDWTDEDPLDVFAKLKKQSDYYNFNQLTVGDFFRDAATLGFAKAWEKRRKWNRMRMSPTDLADISAHTYTYLMNGTPPAGNWTALFRRGERVRLRFISSGTQSFFDVRIPGLKMTVVHVDGQDIEPVTVD... | Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.
Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite
EC: 1.7.2.1
Subcellular Location: Periplasm
Sequence Length: 440
Sequence Mass (Da): 48924
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A0A0X3P8V4 | MSWSQIVEILPATASWIILLTLNSIYFICICFQFASQTSWAIFIVHLIFAVFVICTFARTTFMNPGFLPAATEQEVEFDEAMGSPLYREFDVRGTVAKVKWCKTCLFYRIPRSTHCSICNKCVECFDHHCPWVNNCIGRRNYRYFFTFLLTVCLHMVAVFLVTLFYVLWSDQPLDTHTNIIAMVLMSLVGLVFIPVLSLTIFHITIISRGMTTNEQVTEKFRTVPNPYATTCLQHWLTLFCSPQYPTHMDPMSGKELLKKRRKLRNRYKDHFLLDVENVETSRALTSGKGTGVGADDPAFFALLATEAASTVRAAKLKET... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 513
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 56448
Location Topology: Multi-pass membrane protein
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A0A2D7RK30 | MAKTIGIFGGAFDPVHVGHTSLISDIQKIIDFEKIFIIPSGKPVLKNIHFVDGDKRIEMLDIAFKKNKGVHIDNREVLKKEVSYTFETLREFHKEYKTNQHFSFILGQDAFANFKSWKNWEELLNLCSLIVIKRPNYFFSSEYINDFKKNITSSLSNFLTGHGNIFFAENLMLDISSSDIRENVYKSEFKEINLDNEVLDYIKLNSLYKN | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A349X1S3 | MNCSLAASDMDYKGLIAQTIDELERISSSGAQHLDIVLIDNPALHSTIKLACFDMDSTLIKMEVIDELARYAGIGDQVSQITERAMRGELDFKESFTARLGLLNGLRAEVIEEIKQSLPVMEGAVLLMAGLKRRGVVTMIFSGGFDVFAQHLAKSLGMQSFHANTLEVHDGVLTGAVHPPVVDADLKRALLRRYSGELRLSAEQTLAVGDGANDLKMLGAAGLGVAYRAKPIVRQQAQVAISKNDLSSILYLL | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 253
Sequence Mass (Da): 27367
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A0A349X8U2 | MNQNPVWKYLALVFIVTFGLIYAIPNVYQAEPGVQVIGSRNTVVDQDVVARVSRALENSGVLVKAISFDGEAIRATVDSEEAQNTARDVLKSALGDNYAVALADVATTPSWLSSLGGKPMFLGLDLRGGVHFLMQVDMSAAKAKAMENYEADIRRILREERIRYSGLQTTEVGDVEMRFRTEEDVVNAGNKLRLEFPELGQFQRPIDTSFELQLRMSEQAFSELSRAALKKNMLSIRNRIDQLGVSEPIIQQQGLDRIVVQLPGVKDPTEAKSILGKTATLEVRLVDEKNALASSVRGNVPIGSKRFNFRDGTPILLENR... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 619
Sequence Mass (Da): 67356
Location... |
A0A351MCK4 | MTDLTQPGQDARHPWAARLRGAASFKRVFAGRRLHGRAFSVTWKASDQEGPRLGLIVSRKTSKSAVERNRLKRLIRESFRRHHPVIGKRDVVVTARREAVALPGRELLLELASLWCRLPS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A2E9EEP4 | MSEPKTVAIIMDGNRRWAKKNNLPISSGHRRGIESLIEIVKTAKKAKLERLIVYAFSTENWSRDTFEVNALMNLINFGVDVKLTEIKENGIKLDFIGNLADLPKNAQKGINKCIDETKHLSELTLTVALNYGAISDILEAVKTINENKIELNEENFLNATQIGNQEIDIFIRTGGDKRLSNFLLANIGYTELFFSDKLWPEFSNNDFIQILDEFKERQRRFGK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in ... |
A0A973DQC9 | PILLTLGFKFGEMNIFHRHVSSDGRGDVLFSLANMVKPGIFDIDNMEQFTTTGVSLFMTLPKKQSNIETFNLMLNASAKIAEEISGQVLDGNRSTLTNQLTKHYVERIRDVERNLLTANK | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 1... |
A0A3D5AYX8 | MDTPSLPRLRHAAFAIWARNMLVLRKLMGSSIVINFGEPLLYLLGLGYGLGLFIGGQLDMPYMTFLASGILAASAMNTASFEALFGVFTRMVPQKSYDAMLASPLEIQDILAGEIFYCATKSLIHGTGILVVATALGAVSSWSALWVLPILFLVGLTFAALALIMTSMASSYASFSYYTTLVMMPLMLMSGVFYPIAALPELMQKILYGLPLIHAVQLIRPLMAGLPVTDVALHLAVLAAYGVTGYWIAFRQIRKRLHV | Function: Part of the ABC transporter complex NodIJ involved in the export of the nodulation factors (Nod factors), the bacterial signal molecules that induce symbiosis and subsequent nodulation induction. Nod factors are LCO (lipo-chitin oligosaccharide), a modified beta-1,4-linked N-acetylglucosamine oligosaccharide.... |
A0A2E8NFN2 | MLILVVGIPLIGVIKAYMRKLMDNVDFDEGLENFLYRIAGVALWALVILTAADEFGINVTGLVVGLGFIGLAVAFAAQDTVENVIAGVFIIIDRPFREGERILLPKSLGGTYSKWGDVTYIGLRTTRVRS | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A2D8Y092 | MKNRLSKVITYVTLSILGSFLVLTNASSTNNPKVLIQTKMGHIEITLLPDKAPLTVQNFLGLVEQKHYNGLIFHRVIANFMIQGGGYTSELEYRDSGKRVKNESNNGLPNSRGTIAMARTSDPDSASAQFYINVKNNNHLDFRENVMGYTVFGFVTKGMQVVESIELVDTHIQRGMPAVPIQPIVIESIKRL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 192
Sequence Mass (Da): 21395
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A0A2D5T759 | MKIPYKKMHGTGNIILVIDQRLGNLLPPSSDILQLLGDENTGPGFDQLMWLGPSTSNNHLASYQIFNSDGTKAKQCGNGVRCVAKYLAEIEKNIKSFSLLSPSGLVAADIHEDGSVEVSMGIPSFEPNDIPFLAKEKKILYKLMINNEEIEFSALSLGNPHVVVTVNSINNADIDTIGPLIQNHNIFPDQANVGFMRIINRKHIELRVYERGAGETAACGTGACAAVISGQKRGLLDNEVSVQLLGGQVMVSCDGNKGPVWLKGDAIFVSDGVIEL | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A521RHJ5 | MNLLMDVGNTRIKAAITQVDGLHELKPFAYDLSNCESLLSHQIDGLEVPQKVLVANVGGEAVADRITACMARLWRREPKFVQVPREWGGLVNGYADIRQLGVDRWLGLLAAWMRYRQLVCVVSCGTAVTIDCATGDGRHLGGVIIPGLELMQRSLNQATKGINATRTSDPSCKLGLSTDVCVANGALYAVCSLIKNVLADLESRHGEQPSLVVTGGDAATVGECLSTPFASRPALVLEGLAIIAEQE | 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... |
A0A357KPW7 | FFAPNKGKFNVTDKGGMIDKDHFDWGSAGFIFFILVLNLVGLVFAYMRYFHWNTFETDTVILNFAWTIYNTIIVGAALSVAWEKRQRRKHARVERTIPAEIRTADGRRFKASTGDLSIGDLSLQFEGQANIQPHEFVDVFLFDKNKSTKFRARVATSNGSQLGLVFEELTASQLSKLVYFSHGREKGWTSWYLACEPAKPFRSFFEIIRFGVMGVFKALFKRSGSASKAQSDKSKYGVVGWVLAVLIVVAGSLLYPQFSKAEELQPKIYQIEKKKFSIGDLSNGKDIHLRGGNTDEDVWFSLPVDLLAKEAELVLGFSLS... | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 876
Sequence Mass (Da): 97539
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A0A916HKS4 | MTTVALFVLLFVFMFLGMPVAVALGLSSLLTILFFAQDSLASLSLKLFETSEHYTLLSIPFFILGGAFMTTGGVAKRMIRFANACIGHLRGGLAMASVMACMLFAAVSGSSPATVVAVGSIVIAGMVRAGYSQPFAAGVICNAGTLGILIPPSIVMVVYGAATETSVGKLFMAGVIPGILLGLLLMVAIYVRARMIDLPKQPRATLGEVLSSGRDSLWGLLLIVIILGGIYGGVFTPTEAAAVAAVYAFVIAVFVYRDIGMRRVPHVLVDAGKVTVMLMFIVANALLFAHVLTTERI | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 297
Sequence Mass (Da): 31157
Location Topology: Multi-pass membrane protein
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A0A964LLU2 | MAHARGRPGWSPHHGYPRLAAGSQHPPVAGVSPVQRRRHAGRLLHCDRPRLVTHHSPGQADLRCRDWHTHLRDPHLRQLCRRRRLCGTADECHRSPARALDPATSLWAGRVNSGSREEPLIRHRAAGPRNLAALAVVLLLAVILIGGSWQSTRQRIADNAARQIVAQISLVLPGTLYDNEPNKDTVLKDTGGGQPLPIYRARRNGSPVAAVLTVSAPDGYVGPIRLLVGIAADGRVLGVLITAHQETPGIGAAIATEPPTWLTGFTGRSLTDPPAARWNLRTDGGDFDAIAGATVSSRATVAGVSTAVHYFATHRDEIFS... | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 329
Sequence Mass (Da): 35300
Location Topology: Single-pass membrane protein
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A0A2H0KF43 | MTIAEATTKIAGGATLTESEALSVQSSILAGEAQTPTLVAFFEAFKDRKVSAFELRGFFRASLSAMTPLETGMDTLDTCGTGGDGSGSFNISTVSALLCATAGVPVAKHGNRAASSKCGSADVLEALGVKIELSPEQAKTMLEQTGFVFLFARSYHPAFKHAGEARKLFGKKTYFNFLGPLLNPAKASYRVHGLSDFSLAETLGDILIESGVRKAWLVHAEDGLDEVSPMSLTHGISFSTGGYSEPFNIDPKEHGLAIEDGGGLTGGDVKKNAEILISILQGKGTEAQNAVTILNTAAGLTVSGRSTTFADGVRFAKALI... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A946WY64 | MRKMKIQEMKLSGAFEITPTLNVDSRGFLARTYDQDTFNNAKIDRRWVQESWSHTENKFTVRGLHVQFSPYTETKLVSIINGKMMWVIVDVRKGSDTFGEWDSVLLSSEERNSLFVERGFAHGCLSLTDNCDLLLKSDCEFIEGKGTGILWNDPIIDIDWGEMHKKPIISERDDAYPSFNDFIMNYGGI | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Length: 189
Sequence Mass (Da): 21788
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A0A962UKW9 | GLDSLVLGEPQILGQVKSAFQTASDAGRCGKMLTRLFQHAFSTAKRVRTDTAIGDSPVSVAFAAVSLARQIFADLSQQTAMLIGAGETVELAARHLVQNGIGRIIVANRTIARAQELAEQFGAYAIGLTEIPSHLADADIVIASTASPVPILGKGTVESALKRRRHQPIFMVDIAVPRDIEAEVADLEDVYLYTVDDLEEVIQGNLRSRQEAAEQAKEIIQFQVDDFIAWMRSLDAVGLIQDYRRQAFEIRDEVLAKATRMIESGKPPEEALNFLAQALTNKLLHTPSTQLREAGSSGRHELLEAANALFQLGHGDTAKH | 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... |
A0A349EFI0 | MASSHSRPQETLSIVPSIIDRYLIREIGLTLLATLLALMAILLSHRLAGYLSKAAAGLLAKDSVLLLLLLQSVDMVIVLAPLAFLLSIMLTLGRLYRDHEMTALAAGGQGPLAVYRAVFLLATPLALLTLGAALFLLPVIMQWQFEALAKARKEAEVSMFTPGAFREIMQGQHVIYIGALDERELRNIFIQSREPDGDFSITTGARGRQETDEQGIRHIILEQGHRYRGVPGRGDYDLLSFERAIMRIDTRLTMETSRRETLPTAQLLNATEPLQIAELHMRLNSPLQMLLIALWAPLLARAQPREGRYGRIVAAILVYA... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 379
Sequence Mass (Da): 42039
Location Topology: Multi-pass membrane protein
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A0A661CP41 | MPPLEQNERVVAATQPSSLQNERVAVSNERAAAATQPPPIPNVMPNQTDEDEIDLRFYWHIFTKNKWKIFGLTLLIGLLATLIVFSLQPIYRSTAMLLIESDKTNIISLEDIYGMSSFRQEYYQTQLEILQSWSLTEKVVNKLKLISHSAFAPEQPQKGFFRWRSWLPSSWLPPEEPPTETDRHKGIVETVQAKLEISPVRNSQLVKISFESPDAQLAAKVSNTLADMYIESDLEGRLEMTKKANKWLTERLTGLRKKLEVAEKNLQAYMERQQLVNVAGVKSVAARQIEETASNLVQARQRLGEAESVYQQVKDLRGQS... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 806
Sequence Mass (Da): 90028
Location Topology: Multi-pass membrane protein
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A0A9C9FZM9 | MMQQISAIVAMSENYVIGVDGVLPWHYSGDLRRFKEVTLNSTIIMGRRTWQSIGCRKLPQRRNMVISGQSQAGVETFDSLVVALSCCDGLIWLIGGAALYHSGLPLCQRIDVTFVPGIIEHPSAVYFPELNTHDWQAGTRQPHPYEVDLSYCVYTRITQPTHGRRLV | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Sequence Length: 167
Sequence Mass (... |
Q605M9 | MLKSTAMVGSMTLISRLLGFVRDLIIARTFGADAATDAFFVAFRIPNFLRRLFAEGAFSQGLVPVLSELRVSSDAATVRQTIARMAGTLGLVAALLTCLGMAAAPVLTFLFAPGFQAQPFQFGLTVEMLRITFPYLFFVTLTAFAGGVLHTWGQFAVPAFTPALLNLAMIAAALWLAPLLDLPVEALAWGVFAAGLLQLAFQLPSLWGIRQISLPCPVWRDREVLRMFKLMGPAILGVSATQINLLLDTLVASFLVSGSVSWLYYSDRLVELPQGLLGVAIGTAILPHLAAGHLDHDRDGFSRTLDWALRWVVLLGLPAT... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 513
Sequence Mass (Da): 55061
Location... |
A0A8T7J6Z2 | MSAIQQTLSAYWRLTRMNRPIGIYLLLWPTLSALWLASDGRPSLHFVAVFVLGTTLMRAGGCAINDFADRHVDGQVARTRDRPLATGELRARNAVWTFVVLSLLALALALTLPSPAWPLLLPAALVAFLYPFTKRWIQQPQAVLGIAFGFGIPIAFAAAKGEVTGLGWFLFLMNFFWVLAYDTLYAMCDRPDDLKVGIKSTAVWLGDHDLWVVSVWHAVHMVGWIWIGLSENLGGLFWLGFLVAAGLVIRQMWRVRDREPQVCLWAFLNNHWVGFSLFLGVVGGTWI | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB,... |
A0A6P1M4B4 | MDTKYYVTTPIYYVNDKPHIGHAYTTILADVLANYHRLLGTPTYFLTGTDEHGQKVQQAAEKNGISAQEQCDQTVVRFQELWKRLEISNDDFIRTTEYRHKKIVQEVLQDLYDRDEIYRAEYEGWYCVGCERFFTEKDLVEGNCPECGRKVDAIVETNYFFRMSHYQQWLIEYIETHPEFIQPDFRANETLGFLKNNELQDLCISRPKSRLAWGIELPFDSDFVTYVWFDALLNYITAIGYKSDDDMFKKWWPVNHQLIGKDILTTHTVYWPTMLKAMGVELPKTVFAHGWWLTGRTKMSKSLGNVVNPMEMIDRYGVDA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
EC: 6.1.1.10
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Subcellu... |
A0A2E3QKQ0 | MIRXXKEMRKTRXRXGWVKRQNXDQYVQASRKEGLXSRAAFKLEQIXKKYKIXDSGCRVLDLGCAPGGWLKVXXKYVGXSGKIVGVDLLDXXPIKGVDFIXGDXRDPKIVEQIQERLGIRGLDLVISDMAPNISGVREADQANLLELVESVQEFALEKLKPNGSLLFKCFEGPGIEAMRARLKYRFGKIINVKPAASRKESKEFYILSQDPIGKSALRLQTRSQVEA | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subc... |
A0A833IRL8 | MQTDNRPLSPHVQVYKQGWTGTPSILHRITGAVTTAGSVLLIWWLVALASGPEAFATAQGFFGSIVGQVFLFALTWTLIYHTLAGIRHLFWDAVIGVEVDRAVFTAKLIVFGSIGITVLLWIIAYTVGGA | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 130
Sequence Mass (Da): 14070
Location Topology: Multi-pass membrane protein
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A0A349X767 | MSMIYISLEAPYEWVHAEGTRIEAFGEVPGLGDYPISGEETVVGVVPGEWVTSHLVTLPAKTRKQFNAAVPYALEELFAQDIEEVHFVCPKWQADSQITVYSVAKSKLQEWANLAKTYSIPATRIVPDYALLPQHDVAECSLAVSGDRALAQSKDGFGVTMDLDFVNLWLKETPLSAVIAVNNKDFAERLIKDNSERDIRHWSFGDRMAHWLEYSGQADIDLWTDQTRPRSRKSLFVEYWQAAALIGITITVLATSEIHTYLSLHREIKLITQESQELVKRLVPELDYVTEGQERTYAEKILSRQSQGASPSSLPRMLVA... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 397
Sequence Mass (Da): 44472
Location Topology: Single-pass membrane protei... |
A0A964LV54 | MFFIVFAEKIQLGEQWRPLVIVGFLGAMTTFSSFTIEALLLIEQGHYNTALLYIASSVVVCLLAAFAGMQATRLLF | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 76
Sequence Mass (Da): 8433
Location Topology: Multi-pass membrane protein
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A0A6N8ZJ49 | MRISRTARPTPPSSCTRSSDERRVRRRADDDPGIQDYHTPVLVREVLALLEPERGGLFVDGTVGGGGHARAILERAPGVHLVAVDRDPGALAEAERTLAPFGDRVRFLLSDFRHAARAPELDEGAVSGVLLDLGVSSRQLDHDRRGFAFRRGVPLDMRMDGSDARTASAADVLNSYDEGDLARVFRELGEHRGAHRLARRIVRRRRTRPFAVSDDLVGALRAAMGRSPAPRDKARVFQALRLEVNDELGALREGLDTLRDTMDAGGRMAVISYHSLEDREVKNRFREWSRDCTCPPALPVCVCAGRAAGETLVRRPVRPA... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 342
Seque... |
A0A349S696 | MDTTDISFIGCGNMATSIISGLISNGYPAHQLHVADTNPAQLAAIHQRHQGIQRYSDNTTAIIHSNTIILAIKPQQAQTVLSELASQWQPHQLCISVMAGIELDAITTWLDNPRLAAIRVMPNTPAMLNLGASGLYANAYSNEQQRQQAMTIMQTCGIAIWLAEEQDIDAVTALAGSGPAYFFFMMEAMIEAAVSLGLTTDIARQLCHQTAIGAATMAHQSRFDINTLRQQVTSPGGTTAHAIEVLQSNDFKQLITKAMQAAATRSKELAKR | 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... |
A0A2D9WUD6 | MAEETDKLLTEEELAAIEEMVATGDLGGEGYNVGVATGSYDLTRQDTSVGVNVTAIEQINDRLHRFMRIGLLEELRYNARLQPGRTEIIRYADYVASTSPPLAVNVTKIDPLRGECLIVIHSQVVFSCLDNWFGGSAQSLTSVAAGRIFTPTENAVINKIRGVIFNSLAEAWAPFMQVECSLSSSEISAVFANIAADDEMVIMNRFETQGDGEELGFVDVIYPYANLKQVRDVLSTRITTSGSDAESDARWSAGLLGSLEEVPIEGVVKAVELSISVDELSNMKVGDWFPIRPPEHAELSVNGFPVFNVEVGSRGNQVAI... | Function: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.... |
A0A938PYL2 | MSAWIEYFAVAAGVGYALLAVRRIRWAWVFGGVSSALLALLAARSSLPLQSALQTVYVGMAVYGFWQWSVSKKKDGLSDPITEGSRRGPVIRRWPLSAHGWALAGIALASLVLSPALAETTGASWPRLDAAVTCASLLATWMTARSVLENWLYWYAVNAASMFLYGVQGLSLVAGLYVVYFIIAVFGWREWLAQYRRQ | Function: Required for nicotinamide riboside transport across the inner membrane.
Subcellular Location: Membrane
Sequence Length: 198
Sequence Mass (Da): 21784
Location Topology: Multi-pass membrane protein
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A0A938Q3L3 | MIMKIVMMAIFFIAGSAHASIESWNMPPGVTEMSHAIYGLHMTVFWICVGIGCVVFTLMLWAIIFHRKSLGHNAVPFHESLVLEIIWTTVPIIILIAMAWPATQILIKIEDTRDSDLTIKIVGYQWFWGYEYPEYHVSYFSNLSDSDDQVKNKAPKDELYLKRVDQPLVVPVGKKIRLLTTAADVQHSFWVPDLGFKKDAIPGFINESWTKIDKPGVYYGRCAELCGYKHAYMPIELHAVSQEDFDAFIKKQQEQH | 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(... |
A0A2E1QN11 | MISNKNLKDLNSLKLEYSCKNYFELNNHQDLFELSKEIRKSSTRFWILGEGTNVVILKNLDGLVIKNNLLGISFQDNFVNCASGENWDNLVKRCLEQKLYGFENLSGIPGSVGAGPIQNIGAYGVEISSFIEYVEVFNLITGNFEVFDVNDCKFAYRNSIFKELPNHLITNIRFSLSTNFQPNLSYESIPQDSEISSAEELRNLILSIRNDRLVNPNQDPNVGSFFKNPIVSKSKLKELKNSFPEIKFYDVEHDLYKISAAWLIENIGMKGKQDKSCGVSKKHSLVLVNFSDKSESIINLSNKIKSMIKSRFDLELETEP... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 324
Sequence Mass (Da): 36905
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A0A9E1Y3T7 | MPNPSQTSHLRIIGGIWRGRKVSFKPSPGLRPTPDRVRETLFNWLQGKVSGRRSLELFAGSGILSLEALSRGAEASTLVDTAKTQTQHFQTICSAFQIEPAQCQVHVQDAFKLIQTKPVKPYHLIFVDPPFDTDRYLDIVPSLLKNDFLAPDGFVYLEAPSADVIAKVAQQGLTLYRQKRAGQVHYALLTR | Function: Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
EC: 2.1.1.171
Catalytic Activity: guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 191
Sequence Mass (Da): 21328
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A0A2E6LL43 | MRSGAAARRTRPSVGDRPAEANRAEALIAGAAALEVALTGAQADRLLGFAELLEQANRAFNLISRQDVPRLLARHLLDSLSAAPLLPAGTALDLGTGGGLPGVPLAIAREDIRFTLVDRSERKTRFVARAVRTLGLANVTVRCGDVAGLALAPCDAVVSRAVTAPDRLWALAEPKLAEGGIVVAMYRADGQGEAGSPTPPAGAEVRTRRRVDIPGLPRPHEILVLARAASAPTDETDARRN | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 241
Sequence Mass (Da): 25... |
A0A348UQE5 | MSAPRFALGLVGLGTMGGALAERLLEQEFALVACSYDEPERARFARRHGFERTVSDAAALARELSAPRVVLIMVTAGSAVDRVIADLQPHLLPGDVIIDGGNAHFRDTARRADALRSAGIGFIGAGISGGESGARHGAALMIGATPDEFERCRPVFDALAARVRGRPCVSHVGPAPAGHFVKTVHNGIEYALMQVIADIWRTLQDTLGRDRETQRALFARWAAGPGAGYLVSITRDILGVNDDLGRGHLLDQVRDRAGQKGTGRWAMEAALELAVPMPLLAAALTERMISASPFRRPPEPDLPVSAFGNTSLLQERGVAS... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
EC: 1.1.1.44
Catalytic Acti... |
A0A0R2KI41 | MNMLYFFIAIILIVVGIYLALMYFQHTYKKVLIEQQKQVTAVLENSLEGTFADLNKLNLTGDSLTELEKLEKSYRYLMNRQLPEISEFILALHKKLTQFKVFGFKRELSILNRDLEGAQSTYADIKQRLDLIIEDTKAQQAVVAELKDKYQDIRKQLLAKNESYGPALDELENRLTQLEYDFDQYVEITLSGDYVKAQQPMQQLEEQTAQMEVALTIIPELQHKLVSVFPIQLAELKAGVEQLTSEYYGFTQDLLATIADIETKCQVNHEQIKTLDVEQAQELNQQIVIDIDGVYDAVEKEYVARQVVESNEKQLNEFIE... | Function: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
Subcellular Location: Cell membrane
Sequence Length: 573
Sequence Mas... |
A0A0R2NRI6 | MNLKISALEFVEEAKNGNISVEDFIAKTLERIDSVEDKLHAFLSINDEALDQARQLDKKIKSGEDVGDCFGMPISIKDNMCIKNSKTTCASKMLENFIAPYDATVISKLKKQDAIFIGKANMDEFAISAFECVASLGSDTGGSVRNPASFCSTVGYKPTYGLISRYGLISYANSIEQIGPLTRTVKDSAFMLNLIAGIDPNDNTTVNNNNEDYLANIDAGIEGKRIGIITEMIGDGIDPEVLTATKEAISKLEGLGAICEEVSLEMVKYSVAAYYTISTTEAGSNLARYDNLRYGYDFPVEGYEFNAYISKARRNFGPEV... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: AT... |
A0A3B8WUG4 | MKRPMNRTLLTSVLGMLLVSGCSGFSDRMVERANDTGGWISEQLSGTGKAKDAAELVEFTPQFKPVRIWRKSLGDSVGRGFPKPVPAMVNQQITVIDDHRRGVVSWDYSTRKKLWSSRFEERIAGGIGGDENRIYLATRDAKLLALSAESGELLWQQQMPSEVLAPPVSNNRVVVVATSDGKLIGLNADDGQQRWLTEREVPALSLRGSSTPLIVGDMVVKGFADGRLVALELDTGFDLWDAPVAIAKGRSELDRMVDADATPVADGGVIYTSAYQGRVVAIGQNSGEVLWSRSISSFSGIAVDLFNIYLTDDQDTVWAL... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 411
Sequence Mass (Da): 44935
Location Topology: Lipid-anchor
|
A0A6L8EP22 | MGWQAFPGEWHLSAAVLLLALVFDCMLGEPPDVLHPVVWMGKLIALLERLFPMGGNATSLLAGAGIALFVPALFGLAAWLAVQGLRELGTIPYLLGGALLLKTTFSVKGLGQAAQVTRRFLVAGNLNAARRSLGRLVSRDTQKLDEPLVAAAAIESVGENTTDSYIAPWLAFALLGLPGAFAYRAVNTLDSMIGYHGKYEYSGKAAAKLDDLVNLVPARLSALLLLAAGLFAGLSQRVAEPLEAVSVRRGWKIMRRDHGLTESPNAGWTMSAMSGLIGVALEKPGHYLIGNGLRRPGAADIGRAVRLAYLTAALGVLTTL... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 328
Sequence Mass (Da): 34679
Location Topology: Multi-pass membrane protein
|
A0A520TQ43 | MNFTKKTFLFSIAILIASCSSVSSDRTNDATAISASASGAYSDSGITSNNVLYFSYDKSDINSEGRTKIRTLAKLINDNNLSVRVEGHCDERGTREYNLALGEQRAKTVAELLIINGVSSDKIQTVSYGEEKPVAAGSNERSWSQNRRALVKTF | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 154
Sequence Mass (Da): 16798
Location Topology: Lipid-anchor
|
A0A923THV3 | MSDQQELKPINSNFADDAPRNDEPTVLSIEELNLSIKQLLEGQFNIVWARGEISNFKAHTSGHLYFSLKDSKSQISAVMFRGFGSRLKFKPTDGTEVIVRGRVSVYEPRGNYQILCEMMEPVGAGALQRAFEQLKEKLKKEGLFESARKRPIPTMPKHVAVVTSPTGAAIRDIINILSRRAPWLQVTVVPTVVQGGTAAEKICEALGKALRLPDVDVIIVGRGGGSIEDMWCFNDEKLARAIVASPVPIISAVGHEIDFTIADFVADLRAPTPSAAAELVARSSNELTNRLQQLKKLLGLSLQKNFKLWEQRLQILTKGL... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A963F2J8 | MLLDIGNTNLKWCLFYEGRFDTIHSVSHRDRSFSDVADECWSGIAPPTDIIVSNVAGHAMHGALQQWVQDNWNLEPYFVEAHDCAFGVKNGYRTPGQLGVDRWLTLIAVHNRLNQSACIVDCGTAVTIDVLQADGLHKGGLILPGFNLMRESLLDRTHIPRVSVALESPLLGTDTETAVASASLHATAALIERVMDYMSVQLNGPIVLVMTGSDAPRMRTLLKVESQVIPDLVISGLALIARERTP | 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... |
A0A661EE22 | MKYLFFKQWRLIITNKGFFIAGTGTDVGKTYIGCVLSAFLYQQGITVAPFKPIESNCLIIDNKLHANDANMYFKAIDKSITDAIIAPYRFKQICSTARAAKLNQKKITLFDIVEHININKIFRNNSILIVEGAGGMLSPLCYDGFNIDLAKKLGLPIILVASNKLGVINDILLNLKLFDSYDLDCQYIILNDTDNDTVANDDMNNLNELKEYTKIKIVQNDYNSHSFLQQIKIPS | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A2E9NWS9 | MRLISQISIYAGLLGSSLLAITGAFLTYEVVARYFFTKPTIWAAELSQLCLIWGCLLAMAWVLTLRHHITVNALTSLLP | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 79
Sequence Mass (Da): 8768
Location Topology: Multi-pass membrane protein
|
A0A2E3DC12 | MTIIKRLSCLVKSLEDSALVLAFFLMLLLTLMQIVLRNFFDVGLMWAESLLKIMVLWVALLGAMIATREGQHIKIDLFDRFLSESRFSFLSKVVSFFSAYVCGLAAYSCSELVYYEYMDGTKAFSEVPVWLCQIIMPIAFFVMGLRFLRNVWKS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 154
Sequence Mass (Da): 17742
Location Topology: Multi-pass membrane protein
|
A0A6L7JMW9 | MRIAMVVAEASGDNIAANLICTMKAQNPDVEVSGICGPSMIQQGARAIYKLDDIASLGVEGLFSRLHKILKIRRNYVNSLLENPPDVFVGIDAPDFNLKIEERLRKAGIPTLQYVAPTVWAWRGYRIHKLKRAVSQLLTIYPFEGEMIDRAGIPYKYIGHPLADQIAARNTASGREKYELNEDDRVVALLPGSRTNEVKRLAAIFLQTATELLKSEPNLKFIAPFTSDSTHTMFENIRRTMNIELPVQVVVNDSLGVIEASDIVIAASGTAALESALCGKPVVVSYRVSLMTYWMVKMLSRTRHYSMLNHFDGGPTIPEF... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2... |
A0A6P2BAU6 | MPFGTRILAGGGVRFQLFAPAAHAVTLALDGVGDLYMDDTGDGWYACDAPAAGPGSRYRFLIDGSLAVPDPASRQQPLGHAGPSEVIDPNQFTWTDQAWRGRPWEDAVIHEVHVGSFTPEGDFDGIRRRLDHLLDLGVTALELMPVAEGPGRWSWGYDGVLPFAPRHGYGGSQALRQLVDAAHARGLMVLLDVVYNHFGPEGNFLPNYAPAFLSRRHQTPWGAAINFDDVDSAPVRTFFVHNALYWLEEYHLDGLRLDAVHAIIDESEQHILLDIAEAVHQGPGTDREVHLILENDANEARYLRREAGGSVRHFSAQWND... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
EC: 3.2.1.141
Subcellular Location: Cytoplasm
Sequence Length: 593
Sequence Mass (Da): 65534
|
A0A7C2JW17 | MSADETFVEHGAHLMLAAGERAEKPTPNWFDPAEWRRAGAVAIETSGRGEVLIVAHGDETWVLRHYRRGGLVARVIDDHYVWLGPERTRAFREWRLLRSLRAAGLPVPNPVAAHVYRTGVIYTADIITSYLRDTRKLSWFIAQGTLPAGCWRRIGAMIRGFHDHGVDHPDLTAHNVLLDDAGNAFLVDFDNALIKPPGDWQRAGVERFNRSLRKVALETGTDFDAEAWAEVEAGYAAAGSARLGLE | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + A... |
A0A2E7GHZ6 | MEHFENDHFAKFLSRFEIEGITQSLAHQINQDYAGETVALIGVLKGSFVFLSDLIRRLNVDAQVDFVRMTRNKTQSDPENGTISTIKDLTLEIKDKHVIIVEEIIDSGRILKFLYDRIRSASPRSVEVLTLLDKGKKRLVDVPVKYVGKSIDDQFLVGYGLDLEEQWRNLSDIFYLRYPN | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 180
Sequence Mass (Da): 20765
|
A0A8T6K6K0 | MKGRALLLCAVLVLGGLLGLFMARDPGYLVLAYDGAVLETSLWFGLLLLVAAYVSLRLLLFVLGRLLRGKGLFTAWRARAAQRQTNRGLLLLEEGDWPQAKRLLVNAAGDVAAPAINYLNAARAAHELGAFEERDELLSQAKQQDSKAAPAVGLAGADLRMAAGQWREALAWLRELQVLAPKHPRVLERLWRCHEALEDWQALVELAPAMRKADAADAEALNAMERQAWCRRLATADGLKVWEKRPKALKDDPDLALAATLGGQAAGDAAGAESLLREVLGRSWRDDLVNLYGRIKSPAPDHQLAT | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 306
Sequence Mass (Da): 33400
Location Topology: Multi-pass membrane protein
|
A0A2E6PDT9 | MQMDEGLDTGAILYQQPIAITDSDTRQSLEDNLAHAGKEALLHTLDNLEPLMAGAIQQDNQGSTYAEKLKKTEALINWKSPASTISRTIRAGIGRFPAYTFLDGARLRIIEATPKANRFEHPPGTIAELDRNGFVVACSNSSLHVNLVQLPGKNVANVAQVLNARPSLFAAGKSFTNSEAQS | 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... |
A0A8T7J5R3 | MKKRLYLGVMSGTSLDGIDIALIEINQSQINYVSGEFFPYQTELRQLIEQTCHDDKVSLQSLGELQVRLSLSYADAINSFLAINQLNPSIIEAIGCHGQTVYHQPNSDFPFSLQLVDPSLLAAKTNIPAVTDFRSMDIVLGGQGAPLIPAFHQALLGNGRSNNNKALLNIGGMANVTLFEQDQVFGFDTGPGNVLIDLWVQKYFDLPYDADGKIAREGTVDEELLDVLLSEPYFSEPFPKSTGREYFNLTWLEDRIPATTNESNVVSTLTALTAKTVAEALLNSSKQGELILFGGGSHNKTLLTMLKQYLPNWHFSPSNN... | Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the... |
A0A3D0SQM0 | MSKVMKFTKIVATLGPSSRNADTIERLLREGVDVIRLNFSHGGHEDHALSVQLVREAARKLNRHVAILQDLQGPKIRLGQLEGDFLEVAAGETLVLTTDELIGGVHEGLKKIAIDHRSLHEEIQPGDRVLIDDGLFEVTVERIEGHEIFSRVINGGRLKSRKGVNLPNIKLNISAMTDKDRGDLQFAYDQSLDYVALSFVRDAHDIKELIDVMLTTYGRKIPVIAKIEKPEALQHIEGIIAVADAIMVARGDLGVEISPQDVPLMQKSLIRQCNIAGKPVITATQMLESM | 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: 290
Sequence Mass (Da): 32067
|
A0A3D1EII5 | MSLTIGVLAGEVSGDLLGASLMDALHKRAEAYGGISFVGVGGEQMCRRGLTSLAELEDLSVQGFIDPLLRLPQLLGLQRRLLRRFVDIKIDAFVGIDFNVFNFMLEKRLKRAGVLTAHYVSPSVYAWRKNRVYTVAASADLLFCLYPFEPKQYLQTSVKAIYVGHPLTNSIAADAGNQAEREAARRDLGLSLEQPVLALLPGSRASELKYMLPTFLEAARQFNQKMAQAAQIVIPCVNDQRLQEVTASQSQYPDLWIHPYRGNASRGLQASDVALVKSGTGTLEAALLQRPLVMSYKTGSLNYQLARRLIELDQFALPNI... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2... |
A0A967SIB5 | MTDPAGLSAADRAHLERAKELARLGWGRVHPNPMVGCVLVRDGRVVGEGHHEVFGGPHAEIVALERALSEAEGATAYVSLEPCNHHGKTPPCSQALIEAGVRRVVYGAADPGEHSGGGARTLREAGVGVLGPVWSPATARAENAAFLHVTRHQTPFLALKLAMTLDARVAAAAGEETRITGVEAEREVHRLRSGFDAVMVGEGTALVDDPRLTVXARVPPWWTIRASRFASCRRDGRRRGASSSPPGPTSPPTRRSSRTPRRRRSTSSPVSTPRRRPSSAWSTRVPTSTPLPIATGGWTWTRSSASPGSSGSAPCSA | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
EC: 1.1.1.193
Sequence Length: 317
Sequence Mass (Da): 3358... |
A0A2E5VB02 | MLLLLTDIGARIRAKVVEKNVLVLSNNITLDKALDEPPVFSSRNNSLFRSLSYGIFRWHYRLEWQIDQLITKNLKPKDKKLKSLLRLGLFQLQFTRIPHHAAVSETVNAAEVLGISKTKGLVNAVLRRFLRERKKIDSYLCNDAQAYTAHPNWMVDLIKKDWPENWQAIINENNLQAPMWIRVNQRKVKIDDYLNLLEKNSLDYEYILENNLLRLKKPIPAKLLPKYEDGWVSIQDGAAQLAFNYLDIKPGDRVLDACAAPGGKSAHILEACKDIKELVSVDINNIRLDTMRDNLDRLGLKPNIICGDSCNPSEWWDGNL... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 436
Sequence Mass (Da): 50068... |
A0A534C126 | MTSPKLLEGEVSARGRRIAIIAARFNDFIVASLLKGALGAWVERGGAASELAVVRVPGAFELPVAARRLAASGRYDALVALGCVIRGDTPHFEYVAGECARGLQLASLETGVPIAFGVLTVDSVEQALERAATTAGNKGGAAMESALEMAGLMARL | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This ... |
A0A2E6ABC9 | MPVQKKYSSLISELREKLKDCNTAHDIANIKSEYLGKNGYITNEFSKLRNAQESEKKKLGKELNILKSQAHDIILNTNIINNKTEERFVDVTLPGKNAFVGSRHPISITISEITKILESHGFTPVTGIEVENEYYNFEALNIPESHPSRDMHDTFYVLEDKLLRTHTSSVQIHTMLNQSAPLKIMTPGKVYRCDSDPTHSPMFHQIEGLYIDKGINFCHLKGTLIAFIDEYFGKKMEIRFRPSYFPFTEPSAEIDIRFKGKWLEVLGCGMVHHNVLENVNINPKQFSGFAFGLGIERLAMLKYGITDLRMFFENDISFLS... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 326
Sequence Mass (Da): 37448
|
A0A3A3A8R3 | MVSFWPWKGEDNSPASFEKSLSALSTKITETTTRLDNNRQTARRVKAIWTLYAIFAYTLYTIAVALLVGWENYGLKEIPALVGGPVIIYAVRAGTGKCFDYWIARTQRHLEALQKERAETIEKLKIATKYNSTQQLLEKYGGETSKPTRSKSEKQKSDSKRKPSQQQQQPVARTGISPPPTANIPRASPNQPPLRRRISLPISPRLTVLNLNRSSHPNLPPPSPHSLPRMLPVSRRMRFPALRSEDETQPKNRIALICKNCRLVNGQAPPGIKTLEGLGKWRCGGCGSMNGEESETTKVLADLRSRSAEEARKPEEGDNL... | Function: Plays a role in determining ER morphology.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 386
Domain: The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence Mass (Da): 43012
Location Topology: Multi-pass membrane protei... |
A0A520U802 | MSNYVIGDLQGCYEEFKELLNKISFDPEKDRLWLCGDLINRGPDSLGCLSFLYSIKESCHIVLGNHDLHLLAVAHGSRDLGKTDTFSDILESPDLDILLDWVKELPFHYIKEVKTDQGNIEFIMTHAGIPPMWSKADLIKNSNELSQVLKGEESRRFLKNMYGNKPNLLTDCRNKEERLRLNVNYLTRMRYIYPNGALDLKYKGVVKEAPKNLMPWFNLNPKIIDRNTHLLFGHWAALNGMTGVPKITALDTGCVWGNKLTAMRLEDYRIFSCDKLN | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
EC: 3.6.1.41
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Length: 277
Sequence Mass (Da): 31825
|
A0A521RGI7 | MKMEGIVEYLDMGGYAFYVWTSFGLCMGLMIAHLILPRRRERRILGEIRNRMRREAGRA | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 59
Sequence Mass (Da): 6992
Location Topology: Single-pass membrane protein
|
A0A9D0IG52 | MDAGYTGRVRALYSFLLYLMLPWVLLRLWLKGRRVPGYRQHWKERFGYVDVDVRQPVVWLHAVSVGEVRAAAPLVRALLEQYPERQVLVTTSTPTGRETAQGLFGDDIDCRYLPYDLPAFVHRFLDAVQPVLALVLETEIWPVLYALLEKKRIPLLLLNARLSEKSLRGYLRLRPLMQPALRAIRHIAARNEQDAQRFRRLGVRAAQLSVMGDLKFELQLPADFGRQVEALRKRLGPDRAVWVAGSTHRGEETQLLAAHRRVLADWPGALLVIAPRHPERAAEVAALCAGSGLASRFSSAMSTSGDGFQVLIIDRLGVLL... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A534HKM1 | MRSGSRESQRSRGCSMPAPASARRRSPRSASHARRHAQRGGRQAGLRHPGLRPVARGAHRRRYSRRGRRRHRGRGPQQQVDLQHPRADQRPHGQARQGRRGRRCARPSPGAVRLLRPRARGAATRGCHPDAQHRRRARGVRLHQPGERQAVRVPRAGRRAPLPLSGRAHRRARPCGPQQARRPRRARHAWGAGGGARRHLHGGRQDRRRLRGHHPHAPPRPHGGCLQGDRRLTAPRHPRHGGRGRAPLRDLHRSGRRHHHAHHRSGAHPHHAQRARLRQARRGGVRARRRHPRRLWGRCDPRVSRYPHRTERRHPVGERS... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = ... |
A0A0V0X075 | MLNMIWPLTTATLLLGAITPFSLGEVFTSMANIDMLLQMGEDVSRIIDNYVEEDERRLEQLKKLSAEYKSHKVQVHGQESTDSVIVNPVESFAIVKQLADNWRYVEQLMKTNSAEKLIQNFTHHTHNSVVRPPSEEDVIGMAVGLMRIQDVYKLDTHDMAEGKIRGVLDGRKLTAYDCLEIARVAYNKQDFYHTLLWATEAWDRVQKEDEPTIDEATVLEYIAFAMFKQGNIEWAIHYTTLIKQVDPNHPRASGNLKYYQDLLDPEGKPRKIDPKKLPPPTNRRPDDLSIPERDVYEGLCRSEYPIPDKDRAKLYCYYKR... | Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
EC: 1.14.11.2
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 592
Sequence Mass (Da): 67821
|
A0A525CQQ7 | MKIGMKLVQVIAGALMFAGTLSTVLISQPVVAADKPIDSIVAVVNDGVILASELRAEMEKTIQNLRNSRTRIPPRNILQSQVLEHLIMKNLQLDVARRTRVNIDDQQVNQAVQHIAQKNGLSISQLKNEIEQQGVDYLEFRQGIKEQMTLDVLRRRYVDQRVHVTEKEIANYVANQKSIGENAQEYKTAYILIEIPEAASSEQIEKAREKADMVMQKLREGADFTEMAVSYSDGGNALAGGVLEARKANQLPTMFAELVPDMKAGEYSGIIKSNGGYYIVKLLEVTQGAAEMVVQTKLRHILIKTTEFLNANQAQQKLEQ... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A351CZ46 | MNIRQLSILILIGTAFLVSCSPSKNSIIPELEPAERPKFDKTQSIVRNWSVSLGAGFDSAHVGLTPRLAGENIYAASPEGRVVAVNAETGKRAWTVNLRESVSGGVGAGIGLIFLGTYDGNVYALDASTGATRWTVPVTSVVTAPPMASDGRVVVRTADGRLTGLNVENGAEVWSIVREVPSLSLLGDAEPLLEGGVAIVGFPNGKLLAAGLEEGRVLWEIPVAYPRGRNELERLVDVDAPTSLVRGVLFSASYSGAIIALNVEERATIWNSEVATHHAFAIDTQYLYAVDRDSRVVALDLLTGQTVWTNEQLLYRELSA... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 386
Sequence Mass (Da): 41365
Location Topology: Lipid-anchor
|
A0A8T7I2S2 | MAKRSMYKNAVELGGFALLSIGLIAVFHLLTKDQIAAEMQAKLARTLGELIEPTEYNNDVYHDCIAIDSNGVLTLKGKTLFYRMEMDQKPVAAMFTVTAPDGYSGAIDLIMAIRFDESIAGVRVIQHNETPGLGDKIEPRKSDWIKQFEGLNFSLVPQENWKVKKDGGSFDGFTGATITPRAVLKAIEKGLSYFVTHKQEIFTTPTNCGGDNSNDN | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 216
Sequence Mass (Da): 23812
Location Topology: Single-pass membrane protein
|
A0A351CXI9 | MTFSSLDEKYMARAVELSQCGEGDTHPNPCVGCIIVSGDEVVGEGYHSRAGEDHAEVLALAQADDKARGATMYINLEPCCHQGRTPPCTDSIARAGIVRVVCAMEDPNPMVSGGGFDVLRTAGVDVEFGLLESEARWINRGFITRMLSGRPWVALKIGATLDGRTATESGESQWITGKEAREDVHKQRARYSAIMTGSGTVEADDPQMTVRLVATEKQPLRVVLDTSLRIVADAQIVGDDGNILILTGSTDVEKRIALESKGAEIVSVDVNDDCGIDLQAVLEELGLREHNDVFVECGGKLAGALLEHGLVDELIVYYAP... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A8H6YWK5 | MSFSKVLCIVAATTGLHVSTTSPNPPPLHSEKSIAPTGFEFMLASYPLRIALTCIYWGVAMAEIFVIMGLVSPSVWAEKILHAFALGGNPAKVIISATPTLTIGACLILCGAVIRLACYHELGRLFTFETGIFKNHKLVTSGPYSIVRHPSYLGAMVAYVGLMLYYASAGSWVMECAIKGSTTGRVFGGLYALLMFLVVTGLTCRIPKEDEALRNEFGKEWEDWAAGRYALLPFVY | Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Membrane
Sequence Length: 236
Sequence Mass (Da): 25642
Location Topology: Multi-pass membrane protein
|
A0A9D0W074 | MRVLVTGGDGQLGTELCLLLRERADEAIAPDLEELDFLRADTIAAQIDRHRPDWVINCAAYTQVDKAEEEEDKAFRINRDGAREVARAARAAGAGLAHISTDFIFGGERCRPYREDDAANPLGVYG | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NAD... |
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