ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P59580 | MSFKNLVPVITIDGPSGVGKSSVCKVISKKLQWNVLESGWIYRVLAFIIFKNNVCFSSRNLNILFKNINLHDFIQRINFKNYVISQSLFTNISQEYIGNLASRLACIPYIRHFLLFQQRSFRKFPGLIANGRDMGTVVFPDAIIKFFLISDFKTRVARRCLEYEKKGINSCNYKKIFYDMKTRDQRDHNRKISPLIPAKNAILIDSTYMSLKQVSNVLLSYILKMQKFKL | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 26787
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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A9ADV5 | MKSTRPFHPTPVITIDGPTASGKGTVAALVAAHLGFHLLDSGALYRLAALASMRYDIAAEDVDALVKLIDDLHITFREGCAQLDGVDVSNDIRAEAVGNRASAIAVHGPVRTALVARQRAFRKTPGLVADGRDMGTVIFPDAMLKVFLTASAEARAARRHKQLMQKGFSANIDDLLRDLRERDARDSNRAAAPLKPAADAKLLDTSALSVDEAVDQVLQWYRALGQPA | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24459
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q8PV21 | MQITVSGLPGSGTSTLSKLLAECYDLELISSGEIFRRMARERGMSLAEFGALAERDPSIDLDIDKNQKAIIHSRENIILESRLAGHMAQGRSDVIKIWIKAPLLTRVKRIQRREKTISFDEELKKTVERERSETLRYKNYYGIDITDLSIYDIVIDSEKWNQYQTLDILRVAIDALVGPE | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 20587
Sequence Length: 180
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
B8EN73 | MIIAIDGPAASGKGTLARRLAAHFGLPHLDTGLLYRATARALLDHGHDLSDREAAISAARSLALTDFDEAGLRSRDMAEAASVVAAIPEVRAALVDMQRRFAGRPGGALLDGRDIGTVICPDADCKIFVTASDEARATRRALELRGRGEKVDYAAVLEDIRKRDLRDSSRAAAPLKPADDAVVLDTTKLDVEAAFKAALVIVESAHDSLRAGHPAF | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 22899
Sequence Length: 216
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q2NFY4 | MIITIGGLAGTGTSTTAKTLSQEINIPFISAGDVFRQMAVENNMTLLEFSEFAEGNDNIDKALDKRQAEIANNSENLIVEGRISAFFVNADYRIWLKAPDNVRAERISYREDKSLDTVKQEIAERTASERKRYMEIHDIDIDNLDIYDLIINTDTFNIESTVNIIKKCIENKK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 19626
Sequence Length: 173
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
A0B9U5 | MIITISGPPGSGTSTLARGLSEVLGVRWVNSGDLFRRIAAERGLSLKELGRLAEQGPEIDYLIDDAQRSLAKSGSGIFEGRLAGHMLDADLKIMLKTSLSVRASRIAKRENKSIEEALSEARAREECEARRYKMYYNIDINDLSIYDLIIDTGRWDERGTLSIALAAIRALK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 19012
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
A5IZG6 | MSNKINIAIDGPCGAGKSTVAKEVSKKLKYVFINSGSVYRAIALSAIQMGVDFEVENEVFKMLSEIEIDLDEHENIFLNGENVSETIRDDKVAKAASKVAQYPLIRHYVVDFIHKITKKSKGYIMDGRDTTFKLMPHAELKIFLTGTPEVRARRRALENKDKGFETNYDVVLAEVKARDYADQHRETDPLHITDDAIVIDSTDMNFEQVVDKIVSLAKERM | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25000
Sequence Length: 221
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
P63804 | MSRLSAAVVAIDGPAGTGKSSVSRRLARELGARFLDTGAMYRIVTLAVLRAGADPSDIAAVETIASTVQMSLGYDPDGDSCYLAGEDVSVEIRGDAVTRAVSAVSSVPAVRTRLVELQRTMAEGPGSIVVEGRDIGTVVFPDAPVKIFLTASAETRARRRNAQNVAAGLADDYDGVLADVRRRDHLDSTRAVSPLQAAGDAVIVDTSDMTEAEVVAHLLELVTRRSEAVR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24177
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q5XCU3 | MKAIKIAIDGPASSGKSTVAKIIAKNLGYTYLDTGAMYRSATYIALTHGYTDKEVALILEELEKNPISFKKAKDGSQLVFLGDEDVTLVIRQNDVTNNVSWVSALPEIREELVHQQRRIAQAGGIIMDGRDIGTVVLPDAELKIFLVASVEERAERRYKENLEKGIESDFETLKEEIAARDYKDSHRKVSPLKAAEDALIFDTTGVSIDGVVQFIQEKAEKIVDMS | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25047
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
C4LDM1 | MKIKATIDRIPGGLMLVPLLLGAILHTAAPGTAEYFGSFTKGIITGTLPILSVWFFCIGASIDLRATGTVLRKSGTLVLTKIAVAWVVALIAAQLLPEYGIEVGMLAGLSTLALVSAMDMTNGGLYASLMNQYGSKEESGAFVLMSVESGPLMTMVILGSAGLASFQPHHFVGAVLPFLIGFALGNLDHDLREFFSRATQTLIPFFGFALGNTINLGVILDTGLLGIAMGLLVIVVTGIPLIIADRLIGGGNGTAGLAASSTAGAAVANPVIIAQMNPAFAKIAPAATALVATCVIVTSILVPILTAMYAKRMGNPMPAQ... | Function: Catalyzes the proton-dependent uptake of 2-keto-3-deoxygluconate (KDG) into the cell.
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate(in) + H(+)(in) = 2-dehydro-3-deoxy-D-gluconate(out) + H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34460
Sequence Length: 335
Subcellular Loca... |
O87681 | MKPPSFDYVVADSVEHALRLLADGGDDAKIIAGGQSLVPLLNFRMSRPSLLVDINRVPGLANIRKSDQTIAIGALTRHAKLTTSKTISQNLPILSEAAAWIAHPQIRNRGTIGGSLAHADAAAELPVVLLALDAYVTAQSLQGERKIPLKELLVSHFVSSILPGELIVEVNVPQLPHGSGAAFDEFSRRHGDYAIGGAASIVTLDEQGKCSRARITVLGGGSTAIRCQEAENILIDSTLSSHDIAAAAHAAVQGLDPVPTVHGSAQYRAQVIRTMVERTLAKALHRARPTKESMDH | Cofactor: Binds 1 FAD per subunit.
Function: Molybdo-flavoprotein enzyme complex involved in nicotine degradation. The subunit gamma (large subunit) contains the substrate-binding sites, the subunit alpha (medium subunit) binds FAD and the subunit beta (small subunit) has a 2Fe-2S ferredoxin-type domain which binds 2 2... |
O87682 | MNAFRLTVEVNGVTHATDVEPRRLLADFLRDDLHLRGTRVGCEHGVCGSCTVLLDGQPVRSCTVLAVQANNSRIETVESLQKDGQLHPLQRSFSKCHALQCGFCTSGFLMTLKPLYDDEDVTLDATSAREAISGNICRCTGYQQIVEATVDAFHCRDHND | Cofactor: Binds 2 [2Fe-2S] clusters.
Function: Molybdo-flavoprotein enzyme complex involved in nicotine degradation. The subunit gamma (large subunit) contains the substrate-binding sites, the subunit alpha (medium subunit) binds FAD and the subunit beta (small subunit) has a 2Fe-2S ferredoxin-type domain which binds 2... |
Q933N0 | MMAKAKALIPDNGRAGADEGNRQAWIGQEVLRREDRRLLTGTATFAGDLGVPGQLHMRIVRSTQAHARIVSIDATEAEKTPGVRMVITSEHTRHLGSVLLEELGYHEIYENIEDFSHPVLAVDKVLYVGQPVVAVLAVDPYLAEDAAELVSIEYEPLPVLLDPEEALTGKVELFPGRGNEGARIKKAYGDIDRAFAEAEHVIRHKYVTNRHSGVPMEPRAVVVQPDPARDTLFIWGTVHVHDNRRIIAKMLNLPEVNVRMKHVEIGGSFGVKGGVFPENVVAAWAARTLGVPIKWTEDRVEHMTSTSHAREMVHKLELAL... | Cofactor: Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) per subunit.
Function: Molybdo-flavoprotein enzyme complex involved in nicotine degradation. The subunit gamma (large subunit) contains the substrate-binding sites, the subunit alpha (medium subunit) binds FAD and the subunit beta (small subunit) has a 2... |
Q9X900 | MSPVLAGVLQLLALTAALALAHVPLGNYLARVYSSPKHLRIEKWIYKSIGADPDTEMRWPAYLRGVLAFSLAGVLFLYLLQRLQGVLPGSLGFASIDPDQAFNTAASFVANTNWQSYYGEQAMGHVVQTAGLAVQNFVSAAVGIAVAVALVRGFARSRTGELGNFWADLVRGVVRVLVPIAAVGAVILVACGVIQNFSGIHEVGQFMGGTQEWNGGAVASQEVIKELGTNGGGYFNANSAHPFENPTPFTNLFEIFLILLIPVALTRTFGIMTGSVRQGYAILGTMAAIWAGFVALMMWTEFAHHGPALQAAGGAMEGKE... | 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 binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramemb... |
P57685 | MNLIEYEAYFWAKFFVAERAVSGVIIILIYLIIASVLAYILSFHIAKIYLDEKTVFSKITGRIISFFERMIGESPDHGMTFKEYFINLLLFNFFAGLISFLVIMFQKYLPFSYDTVGMSPSLDFNTVVSFLTNTNLQHYSNPMRLSYFSQTFVITGLMFLSAGTGFAASMAFVRGIRTDTGNIGNFYHDFLVSIFDLILPLTVILTVILILAGIPETMQRYITVNAFLTNKVYNIPLGPVATLEAIKNIGTNGGGFYGANAAYPFENPDWFTNLVEFVSFVIIPLASLISLGIVFGDRKFGRMLYWVVMFFFIFDALFAF... | 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 binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramemb... |
B4E5Q9 | MKSLIRPLVVLFVILTAVTGLAYPAVMTVFGQAVFPSQANGSLIEQDGKVVGSALIGQPFDAPKYFWGRLSATAPMPYNAAGSGGSNFGPLNPSLPDQVKARIAALRDAGTDLSKPVPVDLVTASASGLDPEITPAAAAYQVERVAKARHLAPDAVAQLVAANTTGRQFGVLGEPRVNVLKLNLALDAAQAAH | 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... |
Q2SZS2 | MKSLFRPLIVVFVVLAAVTGLAYPAVMTVFGQAVFPSQANGSLIEKDGKVVGSALIGQQFDAPQYFWGRLSATSPMPYNAAGSGGSNLGPLNPSLKDQVKGRLDALKAAGTDLSQPVPVDLVTASASGLDPEISPAAADYQVARVARARKMPEADVRRLVADNTAGRQFGVLGEPRVNVLKLNLALDAAQTAQ | 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... |
B0SYJ5 | MLSHLRPAIVSAGLFTVLLGLAYPLAVTGVAQAAFPAQANGSLVKDAKGTVVGSTLIAQAFAKPEYLHPRPSAAGAGYDASASSGSNMGPLNDTLIKREKTDADALRAENPGVVIPADAVTTSGSGLDPEISPANARFQAPRVAKARGLRLAQVQAVIDGQAQGPLLGFIGQPRVNVLTVNRTLDARFPAHGQKGG | 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... |
Q9A7X6 | MLSHLRPALVSMGLFTVLLGLAYPLAVTGVAQAAFPNQANGSLIRDADGKVVGSALIGQVFAKPEYFHGRPSAAGAGYDASASSGSNMGPLNETLIARLKTDAAALRAENPGVAIPADAVTTSGSGLDPDISPANARFQAPRVAGARGVPEKDVTALIDAQVQQPLLGFIGQPRVNVLALNRALDARYPPLASQKDG | 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... |
P9WGL3 | MTLLFADLCAIFTPYRWMIEHVTTKRGQLRIYLGAAPGVGKTYAMLGEAHRRLERGTDVVAAVVETHGRNKTAKLLEGIEMIPPRYVEYRGARFPELDVEAVLRRHPQVVLVDELAHTNTPGSKNPKRWQDVQEILDAGITVISTVNIQHLEGLNDVVEQITGIEQKEKIPDEIVRAADQVELVDITPEALRRRLAHGNVYAAERVDAALSNYFRTGNLTALREIALLWLADQVDAALEKYRADKKITATWEARERVVVAVTGGPESETLVRRASRIASKSSAELMVVHVIRGDGLAGVSAPQLGRVRELATSLGATMHT... | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of KdpE in response to... |
O34971 | MLVGARVLLGAPRGVGKTFTMLEEAKPLRDEGVDVVVAVVETHGRAGTAAALVGLEVVPRLTVEHRGVVLTEMDVAGVIVRRAPQLALVDELAHTNASRQRTEKRWQDVEAILDAGIDVMSTVNIQHIESLTDVVHKITGAPQRETIPDEVLRAAREIEVIDVTPVAAGALASGLVYPAERIDAALSNYFRLGNLTGLRELALLWLADEVDSALKNYRAEQGIDSTWETRERVVVALTGGPEGDSHPPGATHCRPCGRGELLAVHVTGQDGFAPPTRGLWRQRSLVESLGGSYHQVIGDDIALVEFARAANATQLVIGVS... | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals (By similarity).
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho... |
Q2FWH7 | MSNTESLNIGKKRGSLTIYIGYSPGVGKTFEMLSNAIELFQSNVDIKIGYIEPHQRDETNALAEQLPKITTNFTKHGSHHFQYLDVDRIIEESPTIVLIDELAHTNISRDRHEKRYMDIEEILNHGIDVHTTLNIQHIESLSSQIELMTGVHVKERVPDYFIMSADVLEVVDISPEQLIKRLKAGKVYKKDRLDVAFSNFFTYAHLSELRTLTLRTVADLMSDKEKVRHNHKTSLKPHIAVAISGSIYNEAVIKEAFHIAQKEHAKFTAIYIDVFEKNRQYKDSQKQVHQHLMLAKSLGAKVKVVYSQTVALGLDEWCKN... | Function: Member of the two-component regulatory system KdpD/KdpE that regulates the transcription of a series of virulence factors through sensing external K(+) concentrations . Regulates also capsular polysaccharide production . May function as a membrane-associated protein kinase that phosphorylates KdpE in response... |
P21866 | MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSAVPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATTAPDPLVKFSDVTVDLAARVIHRGEEEVHLTPIEFRLLAVLLNNAGKVLTQRQLLNQVWGPNAVEHSHYLRIYMGHLRQKLEQDPARPRHFITETGIGYRFML | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon.
PTM: Phosphorylated by KdpD.
Sequence Mass (Da): 25362
Sequence Length: 225
Subcellular Location: Cytoplasm
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P9WGN0 | MTLVLVIDDEPQILRALRINLTVRGYQVITASTGAGALRAAAEHPPDVVILDLGLPDMSGIDVLGGLRGWLTAPVIVLSARTDSSDKVQALDAGADDYVTKPFGMDEFLARLRAAVRRNTAAAELEQPVIETDSFTVDLAGKKVIKDGAEVHLTPTEWGMLEMLARNRGKLVGRGELLKEVWGPAYATETHYLRVYLAQLRRKLEDDPSHPKHLLTESGMGYRFEA | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. Upon phosphorylation by KdpD, functions as a transcription regulator by direct binding to promoter regions of target genes to positively regulate their expression.
PTM: Phosphorylated by KdpD.
Sequence Mass (... |
P36937 | MSAGVITGVLLVFLLLGYLVYALINAEAF | 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 may be involved in stabilization of the complex .
Location Topology: Single-pass membrane protein
Sequence Mass... |
B0R9L8 | MLIGEAVLAVVTVAVVAYLTYVMMYPTRF | 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 may be involved in stabilization of the complex (By similarity). The Kdp system is essential for growth under K(... |
Q1NEI6 | MSVFAGRYAGRCAIVTGGASGLGKQVAARIIAEGGAVALWDLNGDALAATQAEIDATHVVALDVSDHAAVAAAAKDSAAALGKVDILICSAGITGATVPVWEFPVDSFQRVIDINLNGLFYCNREVVPFMLENGYGRIVNLASVAGKEGNPNASAYSASKAGVIGFTKSLGKELAGKGVIANALTPATFESPILDQLPQSQVDYMRSKIPMGRLGLVEESAAMVCFMASEECSFTTASTFDTSGGRTTF | Function: Catalyzes the NAD(+)-dependent dehydrogenation of 2-dehydro-3-deoxy-L-rhamnonate to form 2,4-didehydro-3-deoxy-L-rhamnonate. Does not show any detectable activity in the presence of NADP(+).
Catalytic Activity: 2-dehydro-3-deoxy-L-rhamnonate + NAD(+) = 2,4-didehydro-3-deoxy-L-rhamnonate + H(+) + NADH
Sequence... |
P0DOW0 | MKTLTWTAKETMSILSAPAPVPEPGWIALRVAGVGICGSELSGYLGHNELRKPPLVMGHEFSGVVEEVGHGVTNVKIGDLVTANPLVTCGRCIHCLRGERQRCESRRIIGIDFPGAYAERVLVPSNQCYAVKDAIDGALVEPLACAVRAVGLARIKVGDTAVVIGAGIIGLMTVRLLGLSGAKRIAVVDPNDERLKISQLWGATEMAPNLGALLTDNHPQSFDCVIDAVGLSTTRRDSLNALIRGGRAVWIGLHEALTHLDGNQIVRDELEVRGSFCYTDDEFIRAVSLINSQKFLPVDRQWLDVRSLEEGPAAFKELVN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent dehydrogenation of 2-dehydro-3-deoxy-L-rhamnonate to 2,4-didehydro-3-deoxy-L-rhamnonate. Also has weak dehydrogenase activity on butane-2,3-diol. Does not show any detectable activity in the presence of NADP(+).
Catalytic Activity: 2-de... |
Q9AV97 | MAATSLLYNQLKAAEPFFLLAGPNVIESEEHILRMAKHIKDISTKVGLPLVFKSSFDKANRTSSKSFRGPGMAEGLKILEKVKVAYDLPIVTDVHESSQCEAVGKVADIIQIPAFLCRQTDLLVAAAQTGKIINIKKGQFCAPSVMENSAEKIRLAGNPNVMVCERGTMFGYNDLIVDPRNFEWMREANCPVVADITHSLQQPAGKKLDGGGVASGGLRELIPCIARTAVAVGVDGIFMEVHDDPLSAPVDGPTQWPLRHLEELLEELIAIARVTKGKQRLQIDLTPYRD | Function: Catalyzes the stereospecific condensation of D-arabinose 5-phosphate and phosphoenolpyruvate to form 3-deoxy-D-manno-octulosonate 8-phosphate (KDO-8-phosphate) and inorganic phosphate. Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO) which is an indispensable component of rhamnogalacturonan ... |
Q88MG0 | MTQKIIRVGNIEIANDKPFVLFGGMNVLESRDLAMKVCEEYVRVTEKLGIPYVFKASFDKANRSSVTSYRGPGMEEGLKIFEEIKRTFNVPVITDVHEPYQAEPVAKVCDIIQLPAFLSRQTDLVVAMAKTGVVINIKKAQFLAPQEMKHILAKCEEAGNDQLILCERGSSFGYNNLVVDMLGFGIMKQFEYPVFFDVTHALQMPGGRADSAGGRRAQVTDLAKAGMSQGLAGLFLEAHPDPDNAKCDGPCALRLDKLEPFLVQLKQLDDLVKSFPTVETA | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 31034
Sequence Length: 281
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: s... |
B0BZZ8 | MIRTQVTDTLAIGEGCPLTLLSGPCVIESEDFTLKMASGIARICEKLGISYVFKSSFDKANRTSISSFRGHPMEEGLRILQRVKDEVGVPVVTDIHESHQAAPVAEVADILQIPAFLCRQTDLLMAAAATGRTINVKKGQFLAPWDMKNVVSKLEAGGAKKILLTERGTSFGYNALVVDFRSLPQMRSFGYPVVFDATHSVQMPGGQGSSSGGQREYAPYLARAAAAIGVDALFMEVHENPDQAPSDGPNMIPLHQLEDVLRPILEVHKIMNSTPVLA | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 30077
Sequence Length: 278
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: s... |
Q8EAR9 | MSNKIIKLGSIEIANDKPFVLFGGMNVLESRDLAMSIAETYAEVTQKLGIPYVFKASFDKANRSSVNSYRGPGMEEGLKIFEEIKKTFNLPLITDVHETYQCAPVAEVVDIIQLPAFLARQTDLVVAMAKTGAIINVKKPQFLAPHEMRHIITKFNEAGNDEIILCERGSCFGYNNLVVDMLGMDEMKQSGYPVIFDATHALQRPGGRADSAGGRRAQATELARSGMALGLAGLFIEAHPDPDNAKCDGPCALPLHQLENYLKQMKAIDDLVKSFEPIDTSK | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 30951
Sequence Length: 282
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: s... |
B3QTV9 | MKAVIVIPARLKSTRLPEKMLVDLDGKPLVVRTYEQAKKSRLASDVLLAVDSKRLLDIAESFGCKAVLTPENLQSGTDRIAFAAKSIDADVVINVQGDEPLIPPEMIDSAILPFIENAALPCATLIQPIVSDVPEILQNPNVVKVVTDKNGYALYFSRSPIPYQRNSDAQPKIFRHIGLYAFRKPALETFTTLPPSMLEETERLEQLRLLENGIRIKCVITNLDSQAVDTADDLAKVKAILAKKLK | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27172
Sequence Length: 246
Pathway: Nucleotide-suga... |
Q8KBF7 | MNAVIVIPARLSSSRLKEKMLADLEGEPLIVRTWQQATKSRLASRVVVATDSERIFAVLREAGAEVVMTSPDLTCGTDRIAEAAEQVGGDVFVNLQGDEPLIDPATIDLAIAPFFGEGPLPDCTTLVFPLKPDERQIIDDPHVVKAVLDTRGNALYFSRSPIPYRRETLPDTKYYRHIGLYAFRADVLKAFVALPPSMLERAESLEQLRLLENGYRIRCIETTTDTPGVNTEEELEEVRRLFRERFGA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27730
Sequence Length: 248
Pathway: Nucleotide-suga... |
Q7NSS6 | MNGFTVVIPARMASSRLPGKPLADIAGKPMVVRVAEQAAKSRAARVVVATDHADILAACAAHGVEAVLTREDHASGTDRLAEVAAKLALPDDALVVNVQGDEPLIQPELINRLAELLAGADAPVATLAHALHDAADHFNPNVVKVALDKHGRALYFSRAPIPYARDAYAADRSALPAGLPVYRHIGMYGYRAGFLAAYAGLEPGPLEQYEALEQLRVLWHGYGIAVALADEAPAAGVDTPEDLERVRRLFA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 26626
Sequence Length: 251
Pathway: Nucleotide-suga... |
B6J1K0 | MEFRVIIPARFDSTRLPGKALVDIAGKPMIQHVYESAIKSGAEEVVIATDDKRIRQVAEDFGAVVCMTSSDHQSGTERIAEAAVALGFEDDEIIVCLQGDEPLIPPDAIRKLAEDLDEHDNVKVASLCTPITEVDELFNPHSTKVVLNRRNYALYFSHAPIPWGRDTFSDKENLQLNGSHYRHVGIYAYRVGFLEEYLSWDACPAEKMEALEQLRILWHGGRIHMVVAKSKCPPGVDTEEDLERVRAYF | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28025
Sequence Length: 249
Pathway: Nucleotide-suga... |
Q88LM7 | MSLEFTVVIPARLRSTRLPGKPLLLIAGKPMVQHVWEQARKSGASRVVIATDDTSILEACQAFGAEVMMTRADHESGTDRLAEVAAYLGLPADAIVVNVQGDEPLIPPVIIDQVAANLAAHPEAGIATLAEPIHEPETVFNPNAVKVVSDKNGLALTFSRAPLPWARDTFAKARDVLPEGVPYRRHIGMYAYRVGFLHDFVSWGPCWLEQAEALEQLRALWHGVRIHIEDAIEAPAVGVDTPEDLERVRRLLEA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27809
Sequence Length: 254
Pathway: Nucleotide-suga... |
Q98BN3 | MSTLILIPARMASTRLPGKPLADISGAPMIVHVARRAAEAGLGRVVVATDTQSVAEAVRAHGFEAVMTRIDHESGSDRIHEALAALDPGRKVETIVNVQGDLPTIDPGIIAASLRPFEDAAVDIATLGVEIVREEEKTNPNVVKIVGSPLSATRLRALYFTRATAPWGEGPLYHHVGLYAYRRSALERFVALKPSPLERRERLEQLRALEAGMRIDAEIVRSLPLGVDTPQDLERARTILSN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 26283
Sequence Length: 242
Pathway: Nucleotide-suga... |
Q7UI86 | MKCMIVIPARLASSRLSQKLLLQAGGKSVLQHTYEAALKSSVAEEVIVAVDDPRLAAEVDSFGGQARLTSVDCQSGTDRIAEVALMHEDINILINVQGDEPEIDPKTIDAVAKLLMQHPEADIATAACAIKDRERVEDPNCVKAVLGDDHRAITFSRAAVPHPRDGLTDALLNAEPPNYWQHIGLYAYRREFLLWFATQPPGRLEQIEKLEQLRAIEAGKTIVVAPVEASAPGIDTLEDFRAFTARIESQ | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27384
Sequence Length: 250
Pathway: Nucleotide-suga... |
Q0ZAH7 | MLLDGTLIQLLFLLGFMVFMVMLFQRAHIPASIAYLLVGVLLGAHTAGPVISEGYIHKIAEFGIVFLLFTIGLRFSWQQIYQLRHTILGLGTAQVGLTTLLVALLLWAMGVASVVAFVIGAVFAQSSTTIISKQLLEQGEDQSRHGRLGISLSVFQDITAVPFIIVIPVLGVAMAQDIASTLGMALFKAVLATALVVLVGRYLLRHLFHRVSSSDSAELFTLTVLLVCLAAAWLTQSLGLSMAFGAFLAGMVMGETEFKLQVEAAIRPFRDVLLGIFFVSIGMLLDPMLLPEIGHIALAGALLLLLIKIVLVTALVLATG... | Function: May operate as a K(+)/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71766
Sequence Length: 661
Subcellular Location: Cell membrane
|
Q32B14 | MMSQPAKVLLLYAHPESQDSVANRVLLKPATQLSNVTAHDLYAHYPDFFIDIPREQALLREHEVIVFQRPLYTYSCPALLKEWLDRVLSRGFASGPGGNQLAGKYWRSVITTGEPESAYRYDALNRYPMSDVLRPFELAAGMCRMHWLSPIIIYWARRQSAQELASHARAYGDWLANPLSPGGR | Function: Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20949
Sequence Length: 184
Subcellular Location:... |
Q8ZJC5 | MMLQPPKVLLLYAHPESQDSVANRVLLQPVQQLEHVTVHDLYAHYPDFFIDIHHEQQLLRDHQVIVFQHPLYTYSCPALLKEWLDRVLARGFANGVGGHALTGKHWRSVITTGEQEGTYRIGGYNRYPMEDILRPFELTAAMCHMHWINPMIIYWARRQKPETLASHAQAYVQWLQSPLTRGL | Function: Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21332
Sequence Length: 183
Subcellular Location:... |
Q2GLF7 | MLKSVGVILVLSSPSGCGKTTVANKLLEKQKNNIVKSVSVTTRAARKGEKEGKDYYFVDREEFLRLCSNGEIIEHAEVFGNFYGVPRKNLEDNVDKGVSTLLVIDWQGAFKFMEMMREHVVSIFIMPPSMEELRRRLCGRRADDSEVVEARLKGAAFEISHCEAYDYVIVNEDIEETADRISNILRAEQMKTCRQVGLRELLESRFPIED | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23928
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q5P3M0 | MPGTLIIITAPSGAGKTTLVSGLLERDPQVNLSVSYTTREPRPGERDGREYHFVDVATFRALRDRGEFLEWAEVHGNYYATSKVWLKQQIATGRDILLEIDWQGAQQVRKSFPDAVGVFILPPSLEELEARLRGRGTDSDDVIMRRLLGARGEMRHVGEFDYVILNNDLQCALDDLVAVVRASRLRYANQHERHLQYFDFLEQD | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23259
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q2NIH1 | MKLNKKGLLIILSGPSGVGKATVRKALFEMTNHNFVYSVSATTRKPRPGEQDGKDYHFLTKEEFEKGIENNCFLEWAKFIDHYYGTPKKQIQDFLKQGKEVFLEIEVEGATHLRKKRMPNTVFIFLVPPKKKDLYDRLKKRGTEQEINIVQRIAKANNEFRLAHKYDYIVVNDEVANAADRIIAIIRAEHAKTKRSIRNYLKILEDNVYAE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24544
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q5L9N9 | MNPTERITTPHKTGEAKVIIFSAPSGSGKSTIINYLLAQKLNLAFSISATSRPPRGNEKHGVEYFFLSPDEFRQRIANNEFLEYEEVYTDRFYGTLKAQVEKQLAAGQNVVFDVDVVGGCNIKKYYGERALSLFIQPPCIDELRRRLIGRGTDTPEVIESRIAKAEYELSFAPKFDKVIINDDLETAKAHALKVIKEFLGIDTE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22980
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
O34328 | MKERGLLIVLSGPSGVGKGTVRQAIFSQEDTKFEYSISVTTRSPREGEVNGVDYFFKTRDEFEQMIADNKLLEWAEYVGNYYGTPVDYVEQTLQDGKDVFLEIEVQGALQVRNAFPEGLFIFLAPPSLSELKNRIVTRGTETDALIENRMKAAKAEIEMMDAYDYVVENDNVETACDKIKAIVLAEHLKRERVAPRYKKMLEVE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23218
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q8A677 | MSTFSVFNFQFSIKQMTGKLIIFSAPSGSGKSTIINYLLTQNLNLAFSISATSRPPRGTEKHGVEYFFLTPEEFRCRIENNEFLEYEEVYKDRYYGTLKEQVEKQLEKGQNVVFDLDVVGGCNIKKYYGERALSIFVQPPSIEELRCRLTGRGTDEPEVIECRIAKAEYEMTFAPQFDRVIVNDDLEAAKAETLEVIKEFLNKE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23464
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q6G439 | MVTFFENELSAKKRNQRRGFLFILSSPSGAGKSTLSRLLLKDGKLELSISMTTRQKRPSEVDGLHYHFISKKEFKRKRDGNEFIEWAEVHGNYYGTLRESVENVLSTGRDMLFDIDYQGTKQLQKKMPGDTVSVFILPPSMKELISRLYRRAEDSQDIINLRLKNARTEMQHWRSYDYVIINENLNQSVSLIKSIYLAETVKRERCFFLEPFINGLIAEKID | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 25925
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q3ZAF9 | MMTNWNFNKANKPLLLVVSGPSGVGKDAVLARMKERKLPLAYIVTTTTRTKREKETEGVDYNFIRPAEFQQLIGQNELLEWANVYGNFYGVPKAPIRQALAHGFDVIVKVDVQGAASIKKIVPNAVFIFLMPPDMDELTRRLEHRLTESPESLKRRLATAPLEIEKLPDFDYVVVNPEGEIDNAVSEIMSIISAEHCRINPRSIEL | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23246
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9RS38 | MMASAPQDRPAGTPPQGRGLLIVVTGASGVGKGTLRERWLAGQDVFYSTSWTTREPRPGEVNGRDYVFVSPAEFLAKAQQNGFLEHAQFVGNHYGTPIEPIEAALERGQDVVLEIEVEGAMQVKDRMGEQAILVFIMPPSLTELRRRLTGRATETPERIEKRLTRARDEIQAAHDFRYVIVNDNLDRAVSELLAVQQAERAAQKAAEHWTPEEQQARALADTVRSTALSREALQQVVES | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 26528
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q24TX4 | MEQNHGLLIVLSGPSGAGKGTLCQELLRQLPQVKYSVSATTRQPRPGEMDGLHYYFRSREEFQTMIEQDQLLEWAEFCGNYYGTPQFAVEQAIQAGNDVILEIEIQGALQVKQRFPQGVFIFVVPPSMDELSQRIHKRGTESEEVIQKRLQTAARELEYVSEYDYVVVNDEIPLAVDKLKSILLAEKCRVKRKPYVFQGV | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22840
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q6AJ91 | MNKGKLFVISAPSGAGKTTILGRVMANVGRLNFSISHTTRTARPGEQDGVDYHFVEQEDFIEMQEKGIFLESAYVHKNYYGTSREAVMAQLSEGVDVVLDIDVQGATILMESASLPATYIFIAPPDLSVLEERLRKRGSDSEETIKLRMGNAAGEMLSSRKYDYLIVNDDLAQASTLLKSIIWAERAKSRRTPAGLPIKLVVE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22414
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q72DM9 | MGRERSGIVLVLCAPSGTGKTTLTRRLLTEFPRFAFSVSYTTRKPRNGEVDGKDYHFVTVEAFLRLRDAGFFAEWAEVHGNFYGTPLKATLDLLDEGRDVLFDIDVQGARQLRASLQRGRYVFIMPPSRDELEHRLRARGTDDEETIARRLANAAKELREARRFDAWIVNDDLERAYDELRAAYIEETLSPECRSAFLDGLLQGWND | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23721
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q54XF2 | MDNNSVDSLIPIIITGPSGVGKGTLIDKLRKEYEGSFGHIVSHTTRKPREGEINGVHYHFTDIPTMTEGIKNGDFIEHANVHGNFYGTSKKALKDVSDKNKICILDIDVQGCESVKKANIPCKFIFISPPTFETLQERLIGRGTENEETLKKRLETAKKEMVYRDIPGFFDHVIVNNVLDVAYGELKSIISPFISFQSKSNK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22600
Sequence Length: 202
EC: 2.7.4.8
|
Q14GD9 | MNNYIFIVSAPSGAGKSSLLKAFLATDIGKDNYAVAISHTTREPRVGEINSREYYFVTVAEFEQLLSQDGFIEYAKVFKNYYGTSKAELDRLLALGKNIILEIDWQGAQQTRAIYGDRAKSIFILPPSLDELRKRLEKRNTDSKETIDYRMEQAQSEISHADEYDYLLVNDDFSQSLEQFCKYFEQNIQS | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 21857
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q5SI18 | MKGMRGRLFVMTGASGVGKGTVRAKVLERTRLFYSISMTTRPPRPGEVDGVDYYFVDRPTFEALVREDGFLEYAEYVGHLYGTPRAPVERALSRGEDVLLEIEVQGALQVKRAVPEAVLIFLLPPSLSELKRRLVYRGKDSPEKIQKRLEQAEWEIRNAHLFDYVVVNDVLEEAVADFLAILTAERRRSGRMGEALEMALRRDLALEAELDEILRRRYGGTGH | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 25338
Sequence Length: 223
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q83HT8 | MQLFDLWTDLLDLLTIVAGPTAVGKGTVISHLRKCHPQVKVSISATTREPRDSERDGIDYYFVTDEVFDCMVRSGQMLEWATVHGLHKYGTPKEEVERLLHTGQPVILEIDLQGMRKVRKILPAVRTVILLPPAWDDLICRIKRRGSESQDEIDARLATAKKELEAIGEFDYKIVNADVEIAANELWLAMNRV | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 21894
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9PQS9 | MKRGKLIVFSGPSGVGKHTILSKIINRKDLNLAYSISMTTRKKREGEVNGVDYYFVNDEEFKKAILNNELIEWAEFVGNKYGTPRTIVEKLRDEGKNVILEIEVVGALKVLDLYKNDDLISIFLLPPSIDELKKRLLKRNTETLETIKKRIQKATHEITIKDYYQYNIINDNPDHAANQLAEIILNEIKQS | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22005
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9KNM4 | MGKGTLYIVSAPSGAGKSSLIAALLEQNPTYAMKVSVSHTTRGMRPGEQDGVHYHFVEKEHFIELIGKGEFLEYAEVFGNYYGTSRVWIENTLNKGIDVFLDIDWQGARQIRSQMPEAKSIFILPPSKEELERRLNTRGQDSDAVIAKRMGEAKSEISHYSEYDYVIINDDFDVALMDFKAIIRAERLKQDKQAAKYSAMLSALLAE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23333
Sequence Length: 207
Pathway: Purine metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q87TA9 | MGKGTLYIVSAPSGAGKSSLISAMLERNPTYAMKVSVSHTTRNMRPGEEDGVHYHFVAKEEFETLIAKGDFLEYAEVFGNYYGTSRVWIEETLEKGIDVFLDIDWQGARQIREQMPKAKSIFILPPSNGELERRLNTRGQDSAEVIAKRMAEAKSEISHYSEYDYVIVNDDFDTALMDFKAILRAERLKEEKQAAKYKGMLDALLAE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23446
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q8D2E8 | MKKNMYYAISAPSGTGKSSLIKTFLNTNLGMNFRLSISHTTRNIRSEEIEGKDYFFISKEKFKKMIFEKKFIEYTYSFNNYYGTSFKEVKNKIKSNFSLFFDVNYKGVKKIKEFIPKLISIFILPPSKLDLLKRLYNRYNSNEFELNKRFYKYKKDILNYNKYDFILINRDFNNTLNKIKTIIISKNKKAINQIDKINETIKKLLKK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24826
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q73HV1 | MTVKSEGVLLVLSSPSGAGKTTISAKLLEQSTNLVRSVSMTTRKPRPGEINGKDYFFVTEEKFHELCKAGQMLEYAKVFENFYGIPRDFIEQNLSSGISVLLSIDWQGAFHLFKLMRKKVVSVFILPPSMEELRLRLQKRNSDDASEIERRLAEAQKEISKRDKYDYVIINDDIDKSVEEISSILNKERLKKLKEKPSLED | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23021
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q7MAK5 | MERSKGAILVLSGPSGSGKSSLCKTLFKEIKNAYFSVSTTTRTPREGEIEGKHYHFVSKEKFLEGIEENFFLEWAEVHGNYYGTSKESVESALAQGKLVVFDIDIQGHRNIKESYPELTTSVFITTPTQQELRERLVLRGTDDKETIDLRVMHAYTEMKHIKEFDFVIVNRDLKESEKLLLSIARAALSKRILYDVESLVARWKSKETPKTPNSQ | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24566
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
O66132 | MIKIYAPASIGNVGVGFDILGAAIIPVNGSLLGDFVTVKLSNKFNLVNKGIFSNKLPKNTEQNIVWKCWLKFCNTIKRNIPVSIILEKNMPIGSGLGSSACSIVATLVAMNEFCDKPLNSKELLLLMGEVEGEISGSIHYDNVAPCYLGGLQLILEDSKIISQTIPNFKNWFWIVAWPGTKVPTAEARDILPKKYKKETCIKNSRYLAGFIHASYSQQPHLAARLMQDFIAEPYRIKLLPNYLYVKEKIKKIGAISSGISGSGPTIFSISDNINTAQKISAWLTENYLQNTTGFVHICFLDSKGVRKIG | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 34091
Sequence Length: 309
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.... |
Q7NLJ6 | MCVRVPATSANLGPGFDCLGVALDLANEFEFCEADRFRCVVHSTVSPEDARQVATDERNLAWRAFTHLFEHLGKTPPTVALTVMMHVPLGRGLGSSATAIVGGIAAANRWLGSPLSTPEWLLLASRLEGHPDNVVPAALGGCQLSILGETLLTCALDWHPQIALVLAVPDFALATSKARAALPKTVPHTDAVFNAVHLALLVRALATGDARWLAEALQDRLHQPYRTGLIPGWQDVRAAALEAGAWGVVISGAGPSVLALTHLDCAEAVRQAMASTWPNACLYCPGLDPNGCRVEVEAG | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 31594
Sequence Length: 299
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.... |
Q0BQX8 | MAVYTEVTDEALAAFLAEYDIGTAVAFRGIAEGVENSNYVLRTTGGDYILTLYEKRVDPNDLPWFLGLMEHLAARGITCPQPVRGRDGQALRMLCGRHAAITGFLPGVWPRKVQVAHCHPVGEVLAKLHEAGADYAPTRLNALGPEGWPPLLAICRSRADEISPGLGEELQKALDRVLTAWPSDLPAGHIHADLFPDNVFFLDDRLSGVIDFYFAATDALAYDIAIALNAWCFESDHAYNITKGSALLRGYNAIRTLTEAEKAALPVLCQGAALRFALTRLFDWLNTPPGAMVTRKDPMDYVHRLRFHLSAPNAGAYGL | Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 34916
Sequence Length: 319
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
EC: 2.7.1.39
|
Q8N4N8 | MASQFCLPESPCLSPLKPLKPHFGDIQEGIYVAIQRSDKRIHLAVVTEINRENYWVTVEWVEKAVKKGKKIDLETILLLNPALDSAEHPMPPPPLSPLALAPSSAIRDQRTATKWVAMIPQKNQTASGDSLDVRVPSKPCLMKQKKSPCLWEIQKLQEQREKRRRLQQEIRARRALDVNTRNPNYEIMHMIEEYRRHLDSSKISVLEPPQEHRICVCVRKRPLNQRETTLKDLDIITVPSDNVVMVHESKQKVDLTRYLQNQTFCFDHAFDDKASNELVYQFTAQPLVESIFRKGMATCFAYGQTGSGKTYTMGGDFSGT... | Function: Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity . Plays a role in chromosome congression .
PTM: Phosphorylation at Thr-125 by PLK1 is required for activity in the correction of kinetochore-microtubules attachment er... |
Q8C0N1 | MASQFCLPLAPRLSPLKPLKSHFTDFQVGICVAIQRSDKRIHLAVVTEINRENSWVTVEWVEKGVKKGKKIELETVLLLNPALASLEHQRSRRPLRPVSVVPSTAIGDQRTATKWIAMIPHRNETPSGDSQTLMIPSNPCLMKRKKSPCLREIEKLQKQREKRRRLQLEIRARRALDINTGNPNFETMRMIEEYRRRLDSSKMSSLEPPEDHRICVCVRKRPLNQRETTMKDLDIITIPSHNVVMVHESKQKVDLTRYLENQTFCFDHAFDDKASNELVYQFTARPLVESIFRKGMATCFAYGQTGSGKTHTMGGAFLGK... | Function: Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement during mitosis. Has microtubule depolymerization activity. Plays a role in chromosome congression.
PTM: Phosphorylation at Thr-125 by PLK1 is required for activity in the correction of kinetochore-microtubules ... |
Q99661 | MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKEIDFDDVAAINPELLQLLPLHPKDNLPLQENVTIQKQKRRSVNSKIPAPKESLRSRSTRMSTVSELRITAQENDMEVELPAAANSRKQFSVPPAPTRPSCPAVAEIPLRMVSEEMEEQVHSIRGSSSANPVNSVRRKSCLVKEVEKMKNKREEKKAQNSEMRMKRAQEYDSSFPNWEFARMIKEFRATLECHPLTMTDPIEEHRICVCVRKRPLNKQELAKKEIDVISIPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETAS... | Function: In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells . Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis . Plays a role in chromosome congression and is required for the lateral to end-on conv... |
P21613 | MDVASECNIKVICRVRPLNEAEERAGSKFILKFPTDDSISIAGKVFVFDKVLKPNVSQEYVYNVGAKPIVADVLSGCNGTIFAYGQTSSGKTHTMEGVLDKPSMHGIIPRIVQDIFNYIYGMDENLEFHIKISYYEIYLDKIRDLLDVTKTNLAVHEDKNRVPFVKGATERFVSSPEEVMEVIDEGKNNRHVAVTNMNEHSSRSHSVFLINVKQENVETQKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALADGNKSHVPYRDSKLTRILQESLGGNARTTMVICCSPASYNESETKSTLLFG... | Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.
Sequence Mass (Da): 109407
Sequence Length: 967
Domain: Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP an... |
P17210 | MSAEREIPAEDSIKVVCRFRPLNDSEEKAGSKFVVKFPNNVEENCISIAGKVYLFDKVFKPNASQEKVYNEAAKSIVTDVLAGYNGTIFAYGQTSSGKTHTMEGVIGDSVKQGIIPRIVNDIFNHIYAMEVNLEFHIKVSYYEIYMDKIRDLLDVSKVNLSVHEDKNRVPYVKGATERFVSSPEDVFEVIEEGKSNRHIAVTNMNEHSSRSHSVFLINVKQENLENQKKLSGKLYLVDLAGSEKVSKTGAEGTVLDEAKNINKSLSALGNVISALADGNKTHIPYRDSKLTRILQESLGGNARTTIVICCSPASFNESET... | Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria.
Sequence Mass (Da): 110399
Sequence Length: 975
Domain: Co... |
P33176 | MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ... | Function: Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of t... |
P48467 | MSSSANSIKVVARFRPQNRVEIESGGQPIVTFQGPDTCTVDSKEAQGSFTFDRVFDMSCKQSDIFDFSIKPTVDDILNGYNGTVFAYGQTGAGKSYTMMGTSIDDPDGRGVIPRIVEQIFTSILSSAANIEYTVRVSYMEIYMERIRDLLAPQNDNLPVHEEKNRGVYVKGLLEIYVSSVQEVYEVMRRGGNARAVAATNMNQESSRSHSIFVITITQKNVETGSAKSGQLFLVDLAGSEKVGKTGASGQTLEEAKKINKSLSALGMVINALTDGKSSHVPYRDSKLTRILQESLGGNSRTTLIINCSPSSYNDAETLST... | Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Its motor activity is directed toward the microtubule's plus end.
Sequence Mass (Da): 102411
Sequence Length: 928
Domain: Composed of three structural domains: a large globular N-terminal domain which is r... |
Q5JGT7 | MKPMHPGGFLEVITGPMFAGKTTELIKRVERQIFAKRKAALFKPAIDNRYSEREVVAHNGLRYEAFVVPTTEKGVERIKEITLNEGYEVIGIDEVQFFPMSVVEALNELADQGIYVIASGLNLDFKGDPFPVTKELLVRADNIVYLTAVCTVCGKPATRSQRLIDGKPAPRNSPVILVGGRESYEARCREHHLVPDE | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 21983
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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Q9WYN2 | MSGKLTVITGPMYSGKTTELLSFVEIYKLGKKKVAVFKPKIDSRYHSTMIVSHSGNGVEAHVIERPEEMRKYIEEDTRGVFIDEVQFFNPSLFEVVKDLLDRGIDVFCAGLDLTHKQNPFETTALLLSLADTVIKKKAVCHRCGEYNATLTLKVAGGEEEIDVGGQEKYIAVCRDCYNTLKKRV | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 20654
Sequence Length: 184
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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Q9Y4X4 | MNIHMKRKTIKNINTFENRMLMLDGMPAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTASASSPSSTSTSSSSSSRLASSPTVITSVSSASSSSTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRIPVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRGHGKAQMDPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQKFPCSISPFSIESTRRQRRSESPDSRKRRIHRCD... | Function: Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter.
Sequence Mass (Da): 44240
Sequence Length: 402
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. In KLF... |
O35738 | MNIHMKRKTIKNLSALENRMLMLDGMPAVRVKTELVESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTASASSPSSTSTSSSSSSRPASSPTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRIPVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKAQMEPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQKFACSISPFSIESTRRQRRSESPDSRKRRIHRCD... | Function: Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter.
Sequence Mass (Da): 44105
Sequence Length: 402
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. In KLF... |
Q9UIH9 | MVDHLLPVDENFSSPKCPVGYLGDRLVGRRAYHMLPSPVSEDDSDASSPCSCSSPDSQALCSCYGGGLGTESQDSILDFLLSQATLGSGGGSGSSIGASSGPVAWGPWRRAAAPVKGEHFCLPEFPLGDPDDVPRPFQPTLEEIEEFLEENMEPGVKEVPEGNSKDLDACSQLSAGPHKSHLHPGSSGRERCSPPPGGASAGGAQGPGGGPTPDGPIPVLLQIQPVPVKQESGTGPASPGQAPENVKVAQLLVNIQGQTFALVPQVVPSSNLNLPSKFVRIAPVPIAAKPVGSGPLGPGPAGLLMGQKFPKNPAAELIKM... | Function: Transcriptional regulator that binds to the GA element of the CLCNKA promoter. Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart (By similarity). Is a repressor of CCN2 expression, involved in the control of cardiac fibrosis. It is also involved in the control of cardiac hype... |
P58334 | MSAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATPPGTPGAPPPPATAPGPGGATAAPHLLAASILADLRGGPVVATAASTAGGTSPVSSSSAASSPSSGRAPGAAKSHRCPFHGCAKAYYKSSHLKSHLRTHTGERPFACDWPGCDKKFARSDELARHHRTHTGEKRFPCPLCTKRFTRSDHLTKHARRHPGFRPELLRRPGARSVSPSDSLPCSLAGSPTPSPVPSPAPAGL | Function: Transcription factor that binds GC and GT boxes in the D1A, D2 and D3 dopamine receptor promoters and displaces Sp1 and Sp3 from these sequences. It modulates dopaminergic transmission in the brain by repressing or activating transcription from several different promoters depending on cellular context.
Sequen... |
Q9TZ64 | MTSSSINATSSREPLIHIPNKPSLSIDPLARADRSVHLSPSFFQPGLSSISSENDDAEQRIHEATRSFNQFGHQFYESIRELSESTSAYERLKANALRRKLENTFGNDSGAATSSSSSSVFERQSDFSAFAPYKNSHFDSTQSLFQPTTSFNDRLEQIKSDFIAEHQKSMSSFSGFNTPTTALGAAFQGMQVKKSAFAPVLLRENLDTRRPGGHLISDILNRDPLPQSRNLNLNMARNVPIRLIHSTSNFDIASSSSGDSGHQDHESIVVEDADMDSPTSPCVKRSAMNFDLRDEPLTVNVESVSSTSDLPSSVSSSVNS... | Function: Transcription factor which modulates genes involved in lipid metabolism and the phase I detoxification pathway, including cytochrome P450 oxidases . Required for diet restriction- and mitochondrial dysfunction-mediated lifespan extension, perhaps acting in a ubiquitination-dependent manner . Involved in the r... |
Q13351 | MATAETALPSISTLTALGPFPDTQDDFLKWWRSEEAQDMGPGPPDPTEPPLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGAPQTCALAPSEASGAQYPPPPETLGAYAGGPGLVAGLLGSEDHSGWVRPALRARAPDAFVGPALAPAPAPEPKALALQPVYPGPGAGSSGGYFPRTGLSVPAASGAPYGLLSGYPAMYPAPQYQGHFQLFRGLQGPAPGPATSPSFLSCLGPGTVGTGLGGTAEDPGVIAETAPSKRGRRSWARKRQAAHTCAHPGCGKSYTKSSHLKAHLRTHTGEKPYACTWEGCGWRF... | Function: Transcription regulator of erythrocyte development that probably serves as a general switch factor during erythropoiesis. Is a dual regulator of fetal-to-adult globin switching. Binds to the CACCC box in the beta-globin gene promoter and acts as a preferential activator of this gene. Furthermore, it binds to ... |
P00759 | MWLQILSLVLSVGRIDAAPPGQSRIVGGYKCEKNSQPWQVAVINEYLCGGVLIDPSWVITAAHCYSNNYQVLLGRNNLFKDEPFAQRRLVRQSFRHPDYIPLIVTNDTEQPVHDHSNDLMLLHLSEPADITGGVKVIDLPTKEPKVGSTCLASGWGSTNPSEMVVSHDLQCVNIHLLSNEKCIETYKDNVTDVMLCAGEMEGGKDTCAGDSGGPLICDGVLQGITSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP | Cofactor: Binds 1 zinc ion per subunit.
Function: This protein has both trypsin- and chymotrypsin-like activities, being able to release angiotensin II from angiotensin I or angiotensinogen.
Catalytic Activity: Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kal... |
P07288 | MWVPVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHPEDTGQVFQVSHSFPHPLYDMSLLKNRFLRPGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVDLHVISNDVCAQVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP | Function: Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum.
Catalytic Activity: Preferential cleavage: -Tyr-|-Xaa-.
Sequence Mass (Da): 28741
Sequence Length: 261
Subcellular Location: Secreted
EC: 3.4.21.77
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P15950 | NYHVLLGQNNLSEDVQHRLVSQSFRHPDYKPFLMRNHTRKPKDYSNDLMLLHLSEPADITDGVKVIDLPTKEPKVGSTCLVSGWGSTNPSEWEFPDDLQCVNIHLLSNEKCIKAYKEKVTDLMLCAGELEGGKDTCRGDSGGPLICDGVLQGITSWGSVPCGEPNKPGIYTKLIKFTSWIKEVMKENP | Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
Catalytic Activity: Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.... |
Q9Y5K2 | MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIGLGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGGHDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQAS | Function: Has a major role in enamel formation . Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity).
PTM: N-glycosylated. The N-glycan structures are of complex diantennary or triantennary type, which may ... |
Q9Z0M1 | MMVTARTPWGWFLGCLILEVTGASASSVSSRIIQGQDCSPHSQPWQAALFSEDGFFCSGVLVHPQWVLSAAHCLQESYIVGLGLHNLKGSQEPGSRMLEAHLSIQHPNFNDPSFANDLMLIKLNESVIESNTIRSIPVATQCPTPGDTCLVSGWGQLKNGKLPSLLQCVNLSVASEETCRLLYDPVYHLSMFCAGGGQDQKDSCNGDSGGPIVCNRSLQGLVSMGQGKCGQPGIPSVYTNLCKFTNWIQTIIQTN | Function: Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix.
PTM: N-glycosylated. The N-glycan structures are of complex diantennary or triantennary type, which may be further modifi... |
Q9Y337 | MATARPPWMWVLCALITALLLGVTEHVLANNDVSCDHPSNTVPSGSNQDLGAGAGEDARSDDSSSRIINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRPGVYTNLCKFTKWIQETIQANS | Function: May be involved in desquamation.
Sequence Mass (Da): 32020
Sequence Length: 293
Subcellular Location: Secreted
EC: 3.4.21.-
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Q92876 | MKKLMVVLSLIAAAWAEEQNKLVHGGPCDKTSHPYQAALYTSGHLLCGGVLIHPLWVLTAAHCKKPNLQVFLGKHNLRQRESSQEQSSVVRAVIHPDYDAASHDQDIMLLRLARPAKLSELIQPLPLERDCSANTTSCHILGWGKTADGDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGDEKYGKDSCQGDSGGPLVCGDHLRGLVSWGNIPCGSKEKPGVYTNVCRYTNWIQKTIQAK | Function: Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Deg... |
P49862 | MARSLLLPLQILLLSLALETAGEEAQGDKIIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVHLGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVKKVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKVYKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQPNDPGVYTQVCKFTKWINDTMKKHR | Function: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-... |
Q91VE3 | MGVWLLSLITVLLSLALETAGQGERIIDGYKCKEGSHPWQVALLKGNQLHCGGVLVDKYWVLTAAHCKMGQYQVQLGSDKIGDQSAQKIKATKSFRHPGYSTKTHVNDIMLVRLDEPVKMSSKVEAVQLPEHCEPPGTSCTVSGWGTTTSPDVTFPSDLMCSDVKLISSRECKKVYKDLLGKTMLCAGIPDSKTNTCNGDSGGPLVCNDTLQGLVSWGTYPCGQPNDPGVYTQVCKYKRWVMETMKTHR | Function: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-... |
O60259 | MGRPRPRAAKTWMFLLLLGGAWAGHSRAQEDKVLGGHECQPHSQPWQAALFQGQQLLCGGVLVGGNWVLTAAHCKKPKYTVRLGDHSLQNKDGPEQEIPVVQSIPHPCYNSSDVEDHNHDLMLLQLRDQASLGSKVKPISLADHCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCEDAYPGQITDGMVCAGSSKGADTCQGDSGGPLVCDGALQGITSWGSDPCGRSDKPGVYTNICRYLDWIKKIIGSKG | Function: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation an... |
Q61955 | MGRPPPCAIQPWILLLLFMGAWAGLTRAQGSKILEGRECIPHSQPWQAALFQGERLICGGVLVGDRWVLTAAHCKKQKYSVRLGDHSLQSRDQPEQEIQVAQSIQHPCYNNSNPEDHSHDIMLIRLQNSANLGDKVKPVQLANLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCERAYPGKITEGMVCAGSSNGADTCQGDSGGPLVCDGMLQGITSWGSDPCGKPEKPGVYTKICRYTTWIKKTMDNRD | Function: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation an... |
P07647 | MWFLILFLALSLGQIDAAPPGQSRVVGGYNCETNSQPWQVAVIGTTFCGGVLIDPSWVITAAHCYSKNYRVLLGRNNLVKDEPFAQRRLVSQSFQHPDYIPVFMRNHTRQRAYDHNNDLMLLHLSKPADITGGVKVIDLPTEEPKVGSICLASGWGMTNPSEMKLSHDLQCVNIHLLSNEKCIETYKNIETDVTLCAGEMDGGKDTCTGDSGGPLICDGVLQGLTSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP | Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. This enzyme has a vasoconstrictor activity. KLK-9 has both a chymotrypsin-like and a trypsin-like properties.
Catalytic Activity: Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selecti... |
P03952 | MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQE... | Function: The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.
Catalytic Activity: Cle... |
Q69XQ6 | MAAKAAALSSSPFVSSRRLSSPAASLRARTPRCVMGSEQVRVVVEEEGKTKKRMGVAEPRSAPPAVWTPRAPAQEARLAALRTDGRDSRLKIFSGTANRPLAQEIASYLGVDLGKVLIKRFADGEIYVQLQESVRGCDVFLVQPTCSPVNENLMELFVMIDACRRASARSITVVIPYFGYARADRKAQGREAITAKLSANLLTEAGSDRVIVCDIHSTQALGYFDIPVDHIHGQPVILDYLASKTISKDLVVVSPDVGGVVRARAFAKKLSDAPLAIVDKRRQGHNMSEVMHLIGDVKGKVAIMVDDMIDTAGTITSAAA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 43086
Sequence Length: 399
Subcellular Location: Plastid
EC: 2.7.6.1
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Q5XC85 | MTERYADKQIKLFSLTSNLPIAEKIAKAAGIPLGKMSSRQFSDGEIMINIEETVRGDDIYIIQSTSFPVNDNLWELLIMIDACKRASANTVNIVLPYFGYSRQDRVAKPREPITAKLVANMLTKAGIDRVVTLDLHAVQVQGFFDIPVDNLFTVPLFAERYSKLGLSGSDVVVVSPKNSGIKRARSLAEYLDSPIAIIDYAQDDSEREQGYIIGDVSGKKAILIDDILNTGKTFAEAAKILERSGATDTYAVASHGLFAGGAAEVLETAPIKEIIVTDSVKTKNRVPENVTYLSASDLIAEAIIRIHERRPLSPLFSYQP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ri... |
Q93Z66 | MAAISPANATTAASLSLPQFSSTSSSLSSSSSPSFLNFKTASVSNRCIKCGVRSLENHSGHRSLDFLSNGDPISLINPNSSSPITMAAATSESGSKSSKRVCLFHSDETRDLAERIVAKSDCIELRSINWKKFDDGFPNLFIQNAQGIRGQHVAFLASFSSPAVIFEQLSVIYALPKLFVSSFTLVLPFFPTGTSERMEDEGDVATAFTLARILSNIPTSRGGPTSLVTFDIHALQERFYFGDTILPCFESGIPLLKSRLQSLPDSDNISIAFPDDGAWKRFHKQLQHYPTIVCNKVRMGDKRIVRIKEGDAEGRHVVIV... | Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 44697
Sequence Length: 411
Subcellular Location: Plastid
EC: 2.7.6.1
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Q8S2E5 | MATAASASASASPAAAFGAKTRRPGPSPSPSPSPASAFARPSPRASAAGRLHASLHLGGASATGSSIVSNASGIHLAAPVLAPLAVPKMTGAVGAHKNVLLFHCEEMRELAEQVVARNDDIELRSISWRTFADGFPNLFISNAHTIRGQHVAFLASFSSPSVIFEQLSIIYALPKLFISSFTLILPFFPTGTSERMEDEGDVATAFTLARILSNIPISRGGPSSLVIFDIHALQERFYFGDSVLPCFESGIPLLKSRLQELPDSDNITIAFPDDGAWKRFYKQLQHFPMVVCNKVREGEQRIVRIKEGDPRGRHVVIVDD... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 43909
Sequence Length: 409
Subcellular Location: Plastid
EC: 2.7.6.1
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Q9XGA0 | MAATPHRHLLQPCKNPAISSSETLKPSSSFSLSSNPSIPLIRRRLPTFRCDFQNRRKWMNVDHHISKLNPIQIVPNSRRFQMSSNQENSVEFSKKVCLFYCPETKALAERIAAQSDAIQLRSISWRTFEDGFPNLFISNAQGIRGKHVAFLASFSSPGVIFEQLSVIYALPKLFVASFKLVLPFFPTGTSERMEDEGDVATAFTLARILSNIPISREGPTSLVTFDIHALQERFYFGDNILPCFESGIPLLKKKLQQLPDSDNITIAFPDDGAWKRFHKQLQHFPMIVCAKVREGDQRIVRLKEGDPTGRHVVIVDDLVQ... | Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 45437
Sequence Length: 406
Subcellular Location: Mitochondrion
EC: 2.7.6.1
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