ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6MCA2 | MPSTKFKGYFITIEGGEGSGKSTLLNQLGDYFRNKGFEVIQTREPGGTKLGESIRHLLLNHEDSISIGHQAELLLFLAARAQHIEELIQPALKAGKIVLCDRFNDSTIAYQGAARGLNAKKIQEFCQLVCAEILPNWTLFLDVSPEIGLARTQKIQKVHAQMGQLDRIESEKIEFHERVRQAFLSLVQQEPQRIYRIDANESQSKVLQKALEFLEEQWSDSELKT | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 25495
Sequence Length: 225
EC: 2.7.4.9
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A5D690 | MKGKFIVFEGVDGSGKTTQIKLLGEKLESMGCPVVYTREPGGTRVGERIREILLNPLYGELVPWAEALLYAAARAQHVAQVILPALREGKVVLCDRFTDSSLAYQGYGRGVDIEMLEQVNRPAAAGVVPDLVLVLDFDREGQTERMARSGRSADRIEREAQEFYRRVRSGYLALAARAPRRYRVIDASRAEKLVHLDVLKAAEEVLDAFLKGNSRA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23990
Sequence Length: 216
EC: 2.7.4.9
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Q8I4S1 | MTDDKKKGKFIVFEGLDRSGKSTQSKLLVEYLKNNNVEVKHLYFPNRETGIGQIISKYLKMENSMSNETIHLLFSANRWEHMNEIKSLLLKGIWVVCDRYAYSGVAYSSGALNLNKTWCMNPDQGLIKPDVVFYLNVPPNYAQNRSDYGEEIYEKVETQKKIYETYKHFAHEDYWINIDATRKIEDIHNDIVKEVTKIKVEPEEFNFLWS | Function: Catalyzes the phosphorylation of thymidine monophosphate (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the DNA building block dTTP . Can also phosphorylate dGMP and to a lesser extent GMP, dUMP and dIMP . Can use either ATP or dATP as phosphate donors in presence of Mg(2+) .
Catalytic Ac... |
Q9CHU4 | MGQVHLHNRSFNKATSAGFLIALGIVYGDIGTSPLYAMQAIVRGQGGLANLSESFILGAVSLVIWTLTLITTVKYVLIALKADNHHEGGIFSLFTLVRRMRKWLIIPAMIGGATLLADGALTPAVTVTSAIEGLRGVTHVYSNQTAVMVTTLIILAFLFLIQRFGASLVGRLFGPIMFIWFGFLGVSGLINSFLDLSILKAINPYYAIHLLFSPENKAGFFILGSIFLVTTGAEALYSDLGHVGRGNIYVSWPFVKICIILSYCGQGAWLLAHRGEHIEKLNPFFAVLPDNMVIYVVILSTLAAIIASQALISGSFTLVS... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75477
Sequence Length: 671
Subcellular Location: Cell membrane
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Q88SV0 | MRKQRIQERSLIGMLITLGVVYGDIGTSPLYVMNALINDAGQLKNATPDYVIGSVSLIFWTLMLITTVKYVLIALRADNHHEGGIFALYALVRHRAKWLIFVALIGGAALLADGTLTPAVTVTSAVEGLKGLPKLGAFSQYPWLVPLTVTVILLVLFMIQGFGTAVVGRSFGPMMLLWFTVIGIFGLINISQAPVILKAFSPVYAVQVLFNPANKMGIFILGSVFLATTGAEALYSDMGHVGKANIDATWPFVYTTLILNYLGQGAWMLTHYQDAAWRNATNVNPFYAMVPAGGQIAMIILATAAAIIASQALITGSYTL... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75704
Sequence Length: 680
Subcellular Location: Cell membrane
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Q5ZTN5 | MMNESSTEKKNELSLSFAALGVVFGDIGTSPLYAFGQVIKYFPINDHNIYGILSLIFWSLIIIVSIKYLVIVFRADNDGEGGIIALAGLIRQKIKKPGGWLLFITLVGIGLIIGDGILTPAISILSAVEGLESLSPNLAKYVLPVTLIILFFLFKMQSIGTGKIGIYFAPVMLIWFITIGVLGFLQIIQNPKVLMAINPYYAIYFFMIHKYFALFILGGVFLVMTGGEALFADLGHFGKKAIRTGWFAVALPALLLCYFGQGAFVLMHIEYIKYPFFSLSPDWFLPVMIILATIATIIASQAIISAAFSILKQASLLNLI... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71098
Sequence Length: 625
Subcellular Location: Cell inner membrane
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Q2W905 | MSSHVPSFLRGTPDMTAHGGDGKSRNVAGLMLAAIGVVFGDIGTSPLYAMKETFSGPHAVAMDKGNILGVLSLVFWAITIIVSFKYVIIIMRADNRGEGGSLALLALVSHAAESNRRLSLMVSALGIFAAALFYGDSIITPAISVLSAVEGLQVAAPHLEQWVVPLTIVILFVLFAIQSHGTDLVGKMFGPVMLVWFLTLAILGIRNLSHAPSVLAALSPHYAISFLFREGWHAFLALGSVVLAVTGAEALYTDMGHFGRLPIRLAWYLLVLPALILNYFGQGALLIYNPEAIANPFFNLAPASLALPLVILATLATVIA... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70049
Sequence Length: 643
Subcellular Location: Cell inner membrane
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Q122S7 | MSSKKSSLAALTLGAIGVVYGDIGTSVLYAIKEVFGSGHVPFTPGNIYGILSIFFWTLTVIVSIKYVVLVLRADNNGEGGLIAMLALASTAVKDKPKLRRILLIVGVFGTSLFYGDGVITPAISVLSAVEGLEVVSPAFKEGVIPITLVILFCLFALQKHGTAGIGRYFGPITLIWFVVIALLGISQIVTNPAILKAISPHYALLFMWHNPGTTFIILGAVVLCVTGAEALYADLGHFGKRPIRLAWFSVVMPSLVLNYFGQGALLLNNPAAVKNPFYLMAPEWALLPLVGLATMATVIASQAMITGAFSVTKQAVQMGY... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67676
Sequence Length: 622
Subcellular Location: Cell inner membrane
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Q98KL7 | MDLASRDSEAETVEQSSHSGAEQHSTKVLMLGALGVVYGDIGTSPIYAFREALHASPGIDTRAQVLGVLSLIVWALTIIVTIKYVAFVLRADNKGEGGTLSLMSLARTAYPKGARLILAIGLCGAALFFGDSIITPAISVLSAVEGLRVVTPTLDPYVVPITLLILAILFSVQRFGTGKVAAVFGPVTALWFLAIGVAGLYHLLDDPSILLAINPYYAVTYLASTPTAAFVTVGAVFLAVTGAEALYVDLGHFGRKPIVLAWFSVVFPCLLLNYFGQGAFVLANGGRPTNPFFQMLPDWALMPMVGLATAATVIASQAVI... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69094
Sequence Length: 637
Subcellular Location: Cell inner membrane
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A9AWD5 | MSLIVDILIDDLRALIRDLGQNGGLMSPSVYDTSQALRLYPTPSEEHVWPAVNWLISQQQSDGGWGNPSMPLSRAVPTLAAILALRRHCQRRSTFDGLLEAKRFLRRQLEYWEKPLPDNLPVGMELLLPYMLEEAYREEHQDDIDDVPIKLRLNIPLAPYRELIALGEHKRSLIQQKKPRAGTAPVYSWEAWASHADPELIDGSGGIGHSPAATAAWLFAANHNPNLRNEIAGAENYLRQASLATSESAPCIMPTAWPIPRFEQSFSLYALVTGGILDFPSIQDVLKPQIADLHQALKPRGIGFSDDFMPDGDDTAAAVA... | Function: Involved in the biosynthesis of (+)-O-methylkolavelool. Catalyzes the conversion of geranylgeranyl diphosphate into (+)-kolavenyl diphosphate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (+)-kolavenyl diphosphate
Sequence Mass (Da): 58496
Sequence Length: 521
Domain: The Asp-Xaa-Asp-Asp (DXDD... |
Q9XXD1 | MNSAIMQGAAMATSHGIARLNRHNAQRNHFHIPTANRLFYQLQTPCTSTEEERRTVQTDDVAEIGMQRPDYQMYCGEEEISEQFVKLNVGGQRFMLRKDTIRRRGVGRLLDLINKPVADSNADAFFSSTSEFYFERPPSLFHIVYQFYLNGVIHQPSNLCPVDIIEELEYWRIIPDQYLASCCCAQQIDDDDEEVEEQDKPNLFKTLRFGEIRRCVWNIIEEPASSGKAQAFAVCSVVFVLISISGLVLGSLPELQVATKQRNNLTGEEFTEMEPMPILGYIEYVCIVWFTMEYGLKMLVSAERSKTFRQLLNIIDLLAI... | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56966
Sequence Length: 503
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively ... |
P0DW45 | MQRNTYNKVGLYILSLAMLFVFIIILTAKIPFCFTSDCSFIGLKKLVLTNIVPIVCFVFFLFSIYFYNRLKNITKYNGQDSVKITSCQSESYESLTFLATYIVPFMGFSFEDMQKNIAYLLLVVVIGIIFIKTDKYYANPTLALFGFKLYRVNILHPGSGETKNLIAISNDVLKVDDNVYYSFFDEFVFIARKKI | Function: Component of antiviral defense system Kiwa, composed of KwaA and KwaB. Expression of Kiwa in E.coli (strain MG1655) confers resistance to phages lambda and SECphi18.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22507
Sequence Length: 195
Subcellular Location: Cell inner membrane
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Q6P1M3 | MRRFLRPGHDPVRERLKRDLFQFNKTVEHGFPHQPSALGYSPSLRILAIGTRSGAIKLYGAPGVEFMGLHQENNAVTQIHLLPGQCQLVTLLDDNSLHLWSLKVKGGASELQEDESFTLRGPPGAAPSATQITVVLPHSSCELLYLGTESGNVFVVQLPAFRALEDRTISSDAVLQRLPEEARHRRVFEMVEALQEHPRDPNQILIGYSRGLVVIWDLQGSRVLYHFLSSQQLENIWWQRDGRLLVSCHSDGSYCQWPVSSEAQQPEPLRSLVPYGPFPCKAITRILWLTTRQGLPFTIFQGGMPRASYGDRHCISVIHD... | Function: Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6, which may ensure the correct organization and orientation of bipolar spindles for normal cell division. This complex plays roles in the initial phase of the establishment of epithelial cell polarity.
PTM: Phosphorylated at Ser-653 by PRKCI. Phosph... |
A0A011QK89 | MESIEAVVIGAGVVGLACARELARRGFETVILERHGAFGTETSARNSEVIHAGLYYPTDSLKARLCVAGRQQLYAFCATHAISHQRCGKLVVATSPAQESRLAALQKQGEANGVDDLQRLSAAEARALEPGLACTAALLSPSTGIVDSHGLMLALLGDAETAGAALALHSPLLRGSLDANTPGIVLESGGADGLRFKARRVINAAGLWAPQVAASLAGFPRTLIPANFHAKGSYYALTGRTPFSRLVYPLPEAGGLGVHLTLDLGGQARFGPDVEWLPDPTPGQPIDEPDYRVDPARADAFYAEIRRYWPALPDAALTPA... | Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate) (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological .
Catalytic A... |
A0A0M7LBC1 | MSVDVDCVVIGAGVVGLAIARALAQSGREVLVAEATEAIGTGTSSRNSEVIHAGIYYPAGSLKARLCVRGKHLLYSYCAERGVPYKRLGKLIVATTTEQAAQLEGIAQRARANGVDDLQFISGEDAMRLEPALRCTAALSSPSTGIVDSHALMLSFQGDAENAGAQCVFHTPLVSGRVRPEGGFELQFGGDDAMTLSCNVLINSAGLHAPALARRIDGLPASNIPKDYLCKGSYFTLSGRAPFSRLIYPVPQHAGLGVHLTLDLGGQAKFGPDTEWVETEDYTLDPARADVFYEAVRSYWPALPDDALAPGYTGIRPKIS... | Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate) (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological .
Catalytic A... |
Q9LES4 | MKHKPETAAFSLIRPLEAWAANANKACNTKKMLPCLGRKWMRLSTRNLKPTWNLINVVDASKTIVRGISGGAETIAKERVDTVVIGAGVVGLAVARELSLRGREVLILDAASSFGTVTSSRNSEVVHAGIYYPPNSLKAKFCVRGRELLYKYCSEYEIPHKKIGKLIVATGSSEIPKLDLLMHLGTQNRVSGLRMLEGFEAMRMEPQLRCVKALLSPESGILDTHSFMLSLVEKSFDFMVYRDNNNLRLQGEAQNNHATFSYNTVVLNGRVEEKKMHLYVADTRFSESRCEAEAQLELIPNLVVNSAGLGAQALAKRLHG... | Function: Catalyzes the oxidation of (S)-2-hydroxyglutarate to 2-oxoglutarate. Is specific for the (S) enantiomer and possesses very poor activity toward (R)-2-hydroxyglutarate. Has no activity toward related 2-hydroxy acids, such as glycolate, L-lactate or D-lactate.
Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-... |
A7MBI3 | MVPALRYLGSVCGRARGIFPGGFSAAHTPASGKSRLLCQGGRRASTSSFDIVIIGGGIVGLASARALILRHPALSIGVLEKEKNLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALIYEYCNQKGISYKQCGKLIVAVEQEEIPRLQALYERGLQNGVQGLRLIQQEDIKKKEPYCRGLMAIDCPYTGIVDYRQVAFSFAKDFQEAGGSVLTNFEVEDIEMARESPSRSKDGMKYPIVIRNTKGEEVRCQYVVTCAGLYSDRISELSGCNPNPRIVPFRGDYLVLKPEKRYLVKGNIYPVPDSRFPFLGVHFTPRMD... | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 51022
Sequence Length: 463
Subcellular Location: Mitochondrion
EC: 1.1.99.2
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Q9N4Z0 | MLNRGTFQVFRGISGPPKKSVDLPKYDLVIVGGGIVGCATARQLLIEKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDKEKVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCRDIEMIDSSKITELEPHCRGLKALWSPHTGIVDWGYVTKRFGEDFEKRGGKIYTSYPLEKISDNHDPGYPIRVSSGPALAEFETKNLITCAGLQSDRVAALSGCSTDPKIVPFRGEYLLLKPEKRHLVKTNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLAYKREGYSYFSISPSDLLE... | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 47901
Sequence Length: 433
Subcellular Location: Mitochondrion
EC: 1.1.99.2
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Q55GI5 | MKNSSSMLKGVKSFIGSGIYTNKPIYDVAIVGGGIVGLATGRELLKRNPKLKIVILEKENEIAPHQSSHNSGVIHCGIYYKPGSLRAKLCTKGSKLMYDYCNENQINYENCGKLIVATKKEEFQQLEQLYKRGIENGVPNIKLLESKEQLLSIEPFINGGLRAIHTPSTGIIDYKEVSKSFGNDITEKFGKDSKSEIKLNFNAKNFKYNSNDKLLLISTGDDDDDEEQQQSILTKYSIVCGGMNSDRIAKVAYGNDEPSIVPFRGSFLQFKPEFRHLIKGNVYPLPNASFPFLGVHFTKRINGEVWLGPNAVLSFDREGY... | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 49908
Sequence Length: 446
Subcellular Location: Mitochondrion
EC: 1.1.99.2
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Q9H9P8 | MVPALRYLVGACGRARGLFAGGSPGACGFASGRPRPLCGGSRSASTSSFDIVIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMD... | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 50316
Sequence Length: 463
Subcellular Location: Mitochondrion
EC: 1.1.99.2
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S2DJ52 | MDFQVIIIGGGIVGLATGLKIKQRNPNIKVALLEKEEEVAKHQTGNNSGVIHSGLYYKPGSLKAKNCIEGYHELVRFCEEENIPFELTGKVVVATRKEQVPLLNSLLERGLQNGLKGTRSITLDELKHFEPYCAGVAAIHVPQTGIVDYKLVAEKYAEKFQILGGQVFLGHKVIKVETQNTASIIHTSKGSFSTNLLINCAGLYSDKVAQMNQKESLDVKIIPFRGEYYKIKKEREYLVKNLIYPVPDPNFPFLGVHFTRMMKGGVEAGPNAVLAFKREGYKKSQVNFSELAETLSWPGFQKVASKYWKTGMGELFRSFS... | Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCPIP). Also displays a very low oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the e... |
Q91YP0 | MWPTLRYVGGVCGLARYCVAGGFLRASGPASGVPGLLCGGGRRSSSTSSFDIVIVGGGIVGLASARTLILKHPGLSIGVVEKEKDLALHQTGHNSGVIHSGIYYKPESLKAKLCVEGAALIYEYCNLKGIPYRQCGKLIVAVEQEEIPRLQALYERGLQNGVEGLRLIQQEDIKKKEPYCRGLMAIDCPYTGIVNYQQVALSFAQDFQEAGGSILRDFEVKGIEIAKENSSRSKDGMNYPIAVKNSKGKEIRCRYVVTCAGLYSDRISELSGCNPDPQIVPFRGDYLVLKPEKGYLVKGNIYPVPDSRFPFLGVHFTPRL... | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 50899
Sequence Length: 464
Subcellular Location: Mitochondrion
EC: 1.1.99.2
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A7SMW7 | MLKTSFLLSKRNAVSLSRVLATGISGRNVRHLTLQPSEHYDVAIVGGGIVGLATARELILRHPKLTFCVLEKEKELSMHQSGHNSGVIHCGIYYTPGSLKAKLCVQGLDLTYQYCDEHNIPYKKCGKLIVAVEDKEIPLLNNLYERGKKNGVKDLTMVDKRGIKEIEPHCEGMFAIVSPNTGIVDWAQVALAYGDDFRKGGGDIFTGYEVTDFKCASESGKSQEKEAGLTHPVTVFSNNKQTIKCRYVITCGGLYSDRLAEKSGCNREPRIVPFRGDYLVLKPEKCHLVKGNIYPVPDPNFPFLGVHFTPRMDGSVWLGP... | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 50175
Sequence Length: 456
Subcellular Location: Mitochondrion
EC: 1.1.99.2
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Q24372 | MWRPSISNCVWSTLLLAIFVQQTLAQRTPTISYITQEQIKDIGGTVEFDCSVQYAKEYNVLFLKTDSDPVFLSTGSTLVIKDSRFSLRYDPNSSTYKLQIKDIQETDAGTYTCQVVISTVHKVSAEVKLSVRRPPVISDNSTQSVVASEGSEVQMECYASGYPTPTITWRRENNAILPTDSATYVGNTLRIKSVKKEDRGTYYCVADNGVSKGDRRNINVEVEFAPVITVPRPRLGQALQYDMDLECHIEAYPPPAIVWTKDDIQLANNQHYSISHFATADEYTDSTLRVITVEKRQYGDYVCKATNRFGEAEARVNLFE... | Function: Required for normal tracheal development and maintenance of the trans-epithelial diffusion barrier. Functions as a homophilic cell-adhesion molecule. May play a role in early neuronal differentiation and axon outgrowth.
Location Topology: Lipid-anchor
Sequence Mass (Da): 39939
Sequence Length: 359
Subcellular... |
Q25092 | EGCKPCECDKSGSRLEQCNLYDGQCDCVDGRGGRDCSQCPEMSWGDPFLGCKSCTCNPDGARSLYCNKVTGQCECPRGVTGLNCDRCDRGTYGALPQCIPCGECFDNWDKLIAQLRDEAAAQLRIGTEIKLSGPPGAFAKEFEELEQVLMDMKSHVNSANVSSDQLENIDQELDNLSSKLKDLKPNLASHGSRTGEASVKISELYSRVLNLQSEFNKSSAKTKELRENALEIQEQDVSGAYASIQESLVKSSALQAKLTDAENSKNISVYFRTSVEHFLQNSNFSDANSENGNENSLDKVVEFMKAVDENVSSINTELCG... | Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Sequence Mass (Da): 43262
Sequence Length: 400
Domain: The alpha-helical domains... |
P31242 | MMITLRKLPLAVAVAAGVMSAQALAVDFHGYARSGIGWTGSGGEQQCFKATGAQSKYRLGNECETYAELKLGQELWKEGDKSFYFDTNVAYSVNQEDDWESTSPAFREANIQGKNLIDWLPGSTLWAGKRFYQRHDVHMIDFYYWDISGPGAGLENVDLGFGKLSLAATRNSESGGSYTFSSDDTKKYAAKTANDVFDIRLAGLETNPGGVLELGVDYGRANPQDDYRLEDGASKDGWMWTGEHTQSIWGGFNKFVVQYATDAMTSWNSGHSQGTSIDNNGSMIRVLDHGAMDFNDDWGLMYVAMYQELDLDSKNGSTWY... | Function: Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages.
Catalytic Activity: beta-maltose(in) = beta-maltose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47805
Sequence Length: 429
Subcellular Location: Cell outer membrane
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Q65QT7 | MKKTLLAVAIGGAMFATSAAAVDFHGYARSGIGWTSGGGEQTALKVNGGGSKYRLGNETETYAEFKLGQELFKDGNKSIYLDSNIAYSIDQQVDWEATDPAFREINVQFKNFAEDLLPGATLWAGKRFYQRHDVHMNDFYYWDISGPGAGVENIDLGFGKLSLAVTRNTEGGGTATYGQDKVYYIDNNGQIQYRYEDRKADVYNDVFDIRLAELNVNPNGKLEIGFDYGNAHTKNGYHLEPGASKNGYMITLEHTQGEFFGGFNKFVAQYATDSMTSWNTGHSQGGSVNNNGDMLRLIDHGVVQFSPKVEMMYALIYEKT... | Function: Involved in the transport of maltose and maltodextrins.
Catalytic Activity: beta-maltose(in) = beta-maltose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47895
Sequence Length: 428
Subcellular Location: Cell outer membrane
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Q6D2C3 | MKRKLLTTSIALSLAMLATPSYSVDFSGYFRSGVGVSNHGKQQTADKSYVGRLGNEDDTYGEIQLGQQLYNENGKTFYFDSMISMFSNSSNDNETTKNDDAEFGLRQLNLQAKGFVPGLPDATVWAGKRYYQRHDLHIIDTKYWNISGAGAGIENVKAGEGAFSFAWIRADAENMDVDCGNSLNSQECSSREDTYNDLNINYLDARYAGWKPWDGAWTEFGISYAMPNEADTQKNIFLAEGQKFDPKNSMMITGELSHYFSGLKSNQKLVLQYADKGLAHNMVDQGGGWYDVWSINDSAKGYRVIQAGDLPITDHISLSH... | Function: Involved in the transport of maltose and maltodextrins.
Catalytic Activity: beta-maltose(in) = beta-maltose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48922
Sequence Length: 435
Subcellular Location: Cell outer membrane
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O87237 | MKEKNMKKNDTIELQLGKYLEDDMIELAEGDESHGGTTPATPAISILSAYISTNTCPTTKCTRAC | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A2 exh... |
P83675 | MRNDVLTLTNPMEENELEQILGGGNGVLKTISHECNMNTWQFLFTCC | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin... |
P83674 | MRNDVLTLTNPMEEKELEQILGGGNGVLKTISHECNMNTWQFLFTCC | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin... |
H2A7G5 | MMNATENQIFVETVSDQELEMLIGGADRGWIKTLTKDCPNVISSICAGTIITACKNCA | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. Macedovicin inhibits a broad spectrum of lactic acid bacteria, several food spoilage species (e.g. Clostridium spp.) and oral streptococci . The bactericidal activity of lantibiotics is based on depolarization of energiz... |
P36501 | MEKNNEVINSIQEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCCS | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
PTM: Maturation of lantibiotics involv... |
F1MVX2 | MAQRAFPNPYADYNKSLAEGYFDSAGRLTPEFSQRLNNKIRELLQQMERGLKSADPRDSTVYTGWAGIAVLYLHLYDVFGDPNYLQMAHGYVKQSLNSLSKHSITFLCGDGGPLAVAAVVHHKMNNEKQAEECITRLIHLNKIDPHAPSEMLYGRMGYISALLFVNKNFGEEKIPQSHIQQICETVLTSGEDLARKRRFTGKTPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSHAKLHNLVKPSVDYVCQLKFPSGNYPPCVDDSRDLLIHWCHGAPGVIYMLTQAYKVFKEERYLNDAYQCADVIWQYGLLKKGYG... | Function: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxi... |
Q90ZL2 | MSEQRALKNPYPDYTGLGCAQDLFDMQGNLTQHFATSISSKISELLAILENGLKNADPRDCTGYTGWAGIALLYLHLHSVFGDPTFLQRALDYVNRSLRSLTQRWVTFLCGDAGPLAIAAVVYHRLQKHQESDECLNRLLQLQPSVVQGKGRLPDELLYGRTGYLYSLIFVNQQFQQEKIPFQYIQQICDAILESGQILSQRNKIQDQSPLMYEWYQEEYVGAAHGLSGIYYYLMQPGLVAGQDRVFSLVKPSVNYVCQLKFPSGNYAPCVGDARDLLVHWCHGSPGVIYMLIQAFKVFGVRQYLEDALQCGEVIWQRGL... | Function: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate (By similarity). Binds glutathione (By similarity).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + ... |
O43813 | MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYG... | Function: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxi... |
Q9NS86 | MGETMSKRLKLHLGGEAEMEERAFVNPFPDYEAAAGALLASGAAEETGCVRPPATTDEPGLPFHQDGKIIHNFIRRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNGRRVTFLCGDAGPLAVGAVIYHKLRSDCESQECVTKLLQLQRSVVCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIKEVVNAIIESGKTLSREERKTERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHW... | Function: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.
PTM: Myristoylated. Essential for membrane association.
Sequence Mass (Da): 50854
Sequence Length: 450
Subcellular Location: Nucleus
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Q9JJK2 | MGETMSKRLKFHLGEAEMEERSFPNPFPDYEAAASAAGLAAGSAEETGRVCPLPTTEDPGLPFHPNGKIVPNFIKRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTGDQTYLLRSLDYVKRTLRNLSGRRVTFLCGDAGPLAVGAVIYHKLKSECESQECITKLLQMHRTIVCQESELPDELLYGRAGYLYALLYLNTEIGPGTVGETAIKEVVSAIIESGKSLSREERKSERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPEAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHW... | Function: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.
PTM: Myristoylated. Essential for membrane association.
Sequence Mass (Da): 50777
Sequence Length: 450
Subcellular Location: Nucleus
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Q8BSM7 | MAPTLKQAYRRRWWMACTAVVENLFFSAVLLGWASLLIMLKKEGFYSSLCPAENRTNTTQDEQHQWTSCDQQEKMLNLGFTIGSFLLSATTLPLGILMDRFGPRPLRLVGSACFAASCTLMALASRDTEVLSPLIFLALSLNGFAGICLTFTSLTLPNMFGNLRSTFMALMIGSYASSAITFPGIKLIYDAGVPFTVIMFTWSGLACLIFLNCALNWPAEAFPAPEEVDYTKKIKLIGLALDHKVTGDRFYTHVTIVGQRLSQKSPSLEEGADAFISSPDIPGTSEETPEKSVPFRKSLCSPIFLWSLVTMGMTQLRVIF... | Function: Uniport that mediates the transport of neutral amino acids such as L-leucine, L-isoleucine, L-valine, and L-phenylalanine . The transport activity is sodium ions-independent, electroneutral and mediated by a facilitated diffusion .
Catalytic Activity: D-leucine(in) = D-leucine(out)
Location Topology: Multi-pa... |
Q1ELU5 | MKFSIIALALAVAFVCVAESRSEEEGYDVSEEIQAEELEEAERGGIDRKLMEVVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDTEEARGLKDKFKSMGEKLKQYIQTWKAKFG | Function: M-zodatoxin-Lt4a: Has antimicrobial activity against Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC=0.3 uM), and B.subtilis VKM B-501 (MIC=1.1 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=4.5 uM), E.coli MH1 (MIC=3.2 uM), and P.aeruginosa PAO1 (MIC>35 uM)), and yeasts (P.pastoris GS115 (MIC=36 ... |
Q8N370 | MAPTLATAHRRRWWMACTAVLENLLFSAVLLGWGSLLIMLKSEGFYSYLCTEPENVTNGTVGGTAEPGHEEVSWMNGWLSCQAQDEMLNLAFTVGSFLLSAITLPLGIVMDKYGPRKLRLLGSACFAVSCLLIAYGASKPNALSVLIFIALALNGFGGMCMTFTSLTLPNMFGDLRSTFIALMIGSYASSAVTFPGIKLIYDAGVSFIVVLVVWAGCSGLVFLNCFFNWPLEPFPGPEDMDYSVKIKFSWLGFDHKITGKQFYKQVTTVGRRLSVGSSMRSAKEQVALQEGHKLCLSTVDLEVKCQPDAAVAPSFMHSVF... | Function: Uniporter that mediates the transport of the stereospecific L-phenylalanine, L-methionine and L-branched-chain amino acids, between the extracellular space and the cytoplasm and may control the transepithelial (re)absorption of neutral amino acid in kidney and small intestine . The transport activity is media... |
A4IHK6 | MAPTLATAHRRRWWMACTAVVENLFFSAVLLGWGSLLIMLKSEGFYSYLCHYPDNTTYHNSTGNETNQELVMDMNGWLICKEQDEMLNLAFTVGSFLLSAISLPLGIIMDKYGPRKLRLSGSASFGVSCLLIAYGASNPNSLSVLIFVALCLNGFGGMCMTFTSLTLPNMFGDLRSTFIALMIGSYASSAVTFPFIKVIYDLGVSFITILIVWAACAGLVFFNCFFNWPLEPFPGPEDMDYTVKIKFSWLGFDHKITGKQFYKQVTTVGRRLSVGGSMKNPKELSALQNGNKLCLSTVDLEVKCQADNAATPSFMKSVFS... | Function: Uniporter that mediates the transport of the stereospecific L-phenylalanine, L-methionine and L-branched-chain amino acids, between the extracellular space and the cytoplasm and may control the transepithelial (re)absorption of neutral amino acid in kidney and small intestine. The transport activity is mediat... |
Q1ELU9 | MKYCVVILALLVALVCITESRSTETGYAVAETLEDNDLDELQAYLEEIAEASEMEDFSNIEEARGFFGKMKEYFKKFGASFKRRFANLKKRLG | Function: Has antimicrobial activity against. Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC=1.1 uM), and B.subtilis VKM B-501 (MIC=0.6 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=0.6 uM), E.coli MH1 (MIC=0.6 uM), and P.aeruginosa PAO1 (MIC=18 uM)), and yeasts (P.pastoris GS115 (MIC>37 uM), and S.cerevi... |
Q1ELU8 | MKYFVVALTLAVAFVCIEECKTVEIGYAVSEDFDQNEIDNEEARQAFKTFTPDWNKIRNDAKRMQDNLEQMKKRFNLNLEEARQAFQTFKPDWNKIRYDAMKMQTSLGQMKKRFNL | Function: Does not have antimicrobial activity against neither Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC>70 uM), and B.subtilis VKM B-501 (MIC>70 uM)), nor Gram-negative bacteria (E.coli DH5-alpha (MIC>70 uM), E.coli MH1 (MIC>70 uM), and P.aeruginosa PAO1 (MIC>70 uM)), nor yeasts (P.pastoris GS115 (MIC>70 ... |
P0DJE4 | IVGTIAAAAMTVTHVASGRLNDYILKLEEPNGILLHFKAPLFSIIQEGYAVPKSSLVGTGTSNNEGLLDRNGVDEMLNEKYAVQYASETLFSKDLYNAASNPDSAVGFKLMESPEININERNDWPVASTLLRSSNVNVNLKNSDTPLNLAYFIDQGADINTRNGHLNIVKYLVEEEDLSVDGSKYGIDMTIRTALDIATDLK | Function: Presynaptic neurotoxin that causes massive release of neurotransmitters from vertebrate (but not invertebrate) nerve terminals and endocrine cells via a complex mechanism involving activation of receptor(s) and toxin insertion into the plasma membrane with subsequent pore formation. Binds to neurexin-1-alpha ... |
Q8MLV1 | MQHSPSTTTDHIHFAARFFDRNSYTMDRRLRRPRRTEDVSSGPLLAQSKQPSLLPVTRRTGSVTAAGATATATATAGPATRTRASPSRNKVVAPPSPDLGPRTRRSSRPRSSVGPLTGSGSGSSLPIKAAIKARTPIPEVSEVSSPIRLSTSNLPMTLTTNTSSGAPNKAFNTSSVNSGNSFSRTTTSSTTTTTERIEIRAEGDGEVDTDSIRKRITERLRRSVSKTISNLAGTPVTNTEEGSRYSRSVSRSVYDDEKSSKRSYSTGEEDIDEEDELEEDQFRSFNVTRKSATPAEISCRQLKAPREFGGWLGAFLFLLL... | Function: Anchors the lamina and the heterochromatin to the inner nuclear membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83185
Sequence Length: 741
Subcellular Location: Nucleus inner membrane
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Q14739 | MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRSRSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDAPHKNTQEKFSLSQESSYIATQYSLRPRREEVKLKEIDSKEEKYVAKELAVRTFEVTPIRAKDLEFGGVPGVFLIMFGLPVFLFLLLLMCKQKDPSLLNFPPPLPALYELWETRVFGVYLLWFLIQVLFYLLPIGKVVEGTPLIDGRRLKYRLNGFYAFILTSAVIGTSLFQGVEFH... | Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis . Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activa... |
A1XI29 | MIGLSYLLVQVVSFAGILVIDHRWKLAAFRAPAAAALAVTASVALLLTWDVLGVRSGVFFRGQTDFMTGLLVAPEIPFEEVVFLAFLSHLALVCAAGVSRAVDHARDSRAARASRPSRMTGERR | Function: Involved in the biosynthesis of C(50) beta-cyclic carotenoids . May have C(50) carotenoid beta-cyclase activity and produce the C(50) beta-cyclic carotenoid C.p.450 from the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR) (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da... |
A1XI30 | MTSLYTTLNLTMSIPVVAVALLAAWRLRGPERRRWLIGVGGALLILMILTAVFDNIMISAGLVAYDDSLTSGIRLGVAPIEDFAYAVAAAVFVPSVWALLTASPRVGAEVGSPTVSGRGDALLTRAPEPGDDDEVRTPERPGTPGLLTTLFWSSRPVSWVNTAAPFALAYFLATGGFDLVGVIGTIFFLVPYNLAMYGINDVFDYESDLRNPRKGGVEGSVLERSRHTATLVASAVTTVPFLVYLVLTGTVESSLWLAASAFAVIAYSAKGLRFKEIPFLDSLTSAFHFVSPAIVGWTIAGAELTGGVWACLIAFMLWGA... | Function: Involved in the biosynthesis of C(50) beta-cyclic carotenoids . The elongase/hydratase domain catalyzes the elongation of lycopene by attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of the previous end of the molecule (By similarity). The enzyme acts at both ends of the substrate, and cata... |
Q6NYV8 | MVSPRGVCFLLFLLLGSVFGSVFMLGPLLPLMLLSPSRYRWITDRIVATWLTLPVALLELVLGVKVVVTGDGFIPGERSVIIMNHRTRLDWMFLWCCLLRYSYLRQEKICLKAALKSVPGFGWAMQVASFIFIQRRWEDDRTHMSNMLQYFCRIREPVQLLLFPEGTDLTENTRARSDEFAEKNGLQKYEYVLHPRTTGFTFIVDTLRGGDNLDAVHDITVAYPQNIPQTERHLLAGVFPREIHFHVQRFTVASVPAGAAGLQAWCQERWREKERRLQRFYETVPRRFDAPAVGVCVREPCCQSGQCVCVPRCKSEGRVR... | Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling (By similarity). Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl... |
Q6UWP7 | MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSIFMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVIIMNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKSHFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDLQLWCHKRWEEKEERLRSFYQ... | Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling (By similarity). Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl... |
Q3UN02 | MVSWKGIYFILFLFAGSFFGSIFMLGPILPLMFINLSWYRWISSRLVATWLTLPVALLETMFGVRVVITGDAFVPGERSVIIMNHRTRVDWMFLWNCLMRYSYLRVEKICLKSSLKSVPGFGWAMQVAAFIFIHRKWKDDKSHFEDMIDYFCAIHEPLQLLIFPEGTDLTENNKARSNDFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPYNIPQTEKHLLLGDFPKEIHFHVQRYPADSLPTSKEDLQLWCHRRWEEKEERLRSFYQGEKNFHFTGQSTVPPCKSELRVLVVKLLSIVYWALFCS... | Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling . Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors . Also ... |
Q8VY08 | MAESRSNRAAVQATNDDASASKLSCVKKGYMKDDYVHLFVKRPVRRSPIINRGYFSRWAAFRKLMSQFLLSGTSSKKQILSLGAGFDTTYFQLLDEGNGPNLYVELDFKEVTSKKAAVIQNSSQLRDKLGANASISIDEGQVLSDHYKLLPVDLRDIPKLRDVISFADMDLSLPTFIIAECVLIYLDPDSSRAIVNWSSKTFSTAVFFLYEQIHPDDAFGHQMIRNLESRGCALLSIDASPTLLAKERLFLDNGWQRAVAWDMLKVYGSFVDTQEKRRIERLELFDEFEEWHMMQEHYCVTYAVNDAMGIFGDFGFTREG... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A (PP2A) catalytic subunits to form alpha-leucine ester residues (Probable) . Involved in brassinosteroid (BR) signaling. Plays a negative role in BR signaling pathway. Functions as a positive regulator of BRI1 receptor-ki... |
Q4WS57 | MSASQIPNLNTLRRGGGRGRLRGRGGFETGAPSEDRHGSRGLAAQDRVVQGTDNDASVSRLSAVEIGYLEDPFAKVLTPPGSGTRRLPIINRGTYVRTTAIDRLVARFLEGPSQTKKQIISLGAGSDTRVFRLLSSRSSASSSDLIYHEIDFSANTAAKIKFIRAAPLLQRTLGLGSAQNVAIPDSGDALHSPTYHLHPVDLRTLAASGSATTSRSPSSPNPAEKDQPPCPLQGVDPTLPTLLISECCLVYLSPREAADVVDYFTKTLFPASVPLGLIIYEPIRPDDAFGRTMVANLATRGIQLQTLHEYASLEAQRRRL... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenos... |
P46554 | MDSEAVSSDSHVAAAIATRRRSNSVSDDYSVQRTNDDATQCKYFATQKGYWKDEFISRFANSSSNVSEARRFPEISMGYWARTAAIEKYVRDFLNEFDGNAQVVSLGCGFDTLFWRLVSSGAKLVKYVEVDFSSVTSKKIRHILKPIGPNSVDLKKSFESDAVVSHHADLHAGNYHLIGADLRQANELDQKLATCQLSHDIPTIFIAECVLVYMSADSSTALLKQIVSQFKQPAFVNYEQFRTSDAFTKVMEQNLGDRGIQLHGLEMCESAEKQEERFRNAGFKEVKVMDMNQIFNNFLDQKEVSRIREIEMLDEMELLQ... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenos... |
Q5A387 | MLSPQDRQDKLVRATDLDALSCKYSINRNLYLNPPDEFVKDLVESYQRYLQYCVGYTGLSSSRALKGLFQEKKMPIINRGSYLRTRAIDQVVNKFIGEFKDRCQIVSLGSGSDTRAFQIFKSHANVIYHEIDFPESAKVKKLAILQNPVIRELVGTNETSPLINNKEQFESYSSELHTEKYHLHGIDLRTLKKPDSQIKGFQPEVPTLVISECVLCYLSPDEYQRTMNYWTEIADQNYMGFLIYEPMSLNDQFGETMTLNLQSRGLNLQTFSKYPDLISRKKFLEESCHLKNLRLTDMSYIGGYKVRQDGREWIDHKEMG... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenos... |
P0CO56 | MTQCGDRRLLALIIYHGAIQTPPPTDPNAAPAHRPAPRPALGRCRPPHRRRRRLRPPVRPPVSLPVALTTRSSAAQLGYLQDPFASLLYRPPMPQPGAFAPQAVGRARKPPLINVGTHHRTWGIDRLVDRFLQRGGKQVVSLGAGSDTRFWRLMSRATPPDLARYVEIDFPHLTSPKAQRIARHRKLYQYLGPSSTAMPPPGHPYTVSKGGTQLSSPLYTLLPLDLRPSPSEPASSISAILSHHVLPQLDPRLPTLFLAECLFPYMSPEDSREIIKWFGETFCSCMGVVYEMVGLDDSFGNVMKRNLAVRNLSIPGSIFS... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenos... |
P76008 | MSLFHLIAPSGYCIKQHAALRGIQRLTDAGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAHGNVITFSGPMLVANFGADELNAFTEHHFWLALRNETFTIEWQGEGPTCRAEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM | Function: Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc... |
Q9I2S7 | MYKDLKFPVLIVHRDIKADTVAGERVRGIAHELEQDGFSILSTASSAEGRIVASTHHGLACILVAAEGAGENQRLLQDVVELIRVARVRAPQLPIFALGEQVTIENAPAESMADLHQLRGILYLFEDTVPFLARQVARAARNYLAGLLPPFFRALVEHTAQSNYSWHTPGHGGGVAYRKSPVGQAFHQFFGENTLRSDLSVSVPELGSLLDHTGPLAEAEDRAARNFGADHTFFVINGTSTANKIVWHSMVGREDLVLVDRNCHKSILHSIIMTGAIPLYLTPERNELGIIGPIPLSEFSKQSIAAKIAASPLARGREPK... | Function: Plays an essential role in lysine utilization by acting as a lysine decarboxylase.
Catalytic Activity: H(+) + L-lysine = cadaverine + CO2
Sequence Mass (Da): 82757
Sequence Length: 751
EC: 4.1.1.18
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P52095 | MNIIAIMGPHGVFYKDEPIKELESALVAQGFQIIWPQNSVDLLKFIEHNPRICGVIFDWDEYSLDLCSDINQLNEYLPLYAFINTHSTMDVSVQDMRMALWFFEYALGQAEDIAIRMRQYTDEYLDNITPPFTKALFTYVKERKYTFCTPGHMGGTAYQKSPVGCLFYDFFGGNTLKADVSISVTELGSLLDHTGPHLEAEEYIARTFGAEQSYIVTNGTSTSNKIVGMYAAPSGSTLLIDRNCHKSLAHLLMMNDVVPVWLKPTRNALGILGGIPRREFTRDSIEEKVAATTQAQWPVHAVITNSTYDGLLYNTDWIKQ... | Function: Plays a role in lysine utilization by acting as a lysine decarboxylase.
Catalytic Activity: H(+) + L-lysine = cadaverine + CO2
Sequence Mass (Da): 80590
Sequence Length: 713
EC: 4.1.1.18
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O34851 | MKGVFSLNYKPKALNKGDTVGVIAPASPPDPKKLDTALLFLEELGLQVKLGKALKNQHGYLAGQDDERLADLHEMFRDDEVKAVLCACGGFGTGRIAAGIDFSLIRKHPKIFWGYSDITFLHTAIHQNTGLVTFHGPMLSTDIGLDDVHPLTKASYKQLFQETEFTYTEELSPLTELVPGKAEGELVGGNLSLLTSTLGTPFEIDTRGKLLFIEDIDEEPYQIDRMLNQLKMGGKLTDAAGILVCDFHNCVPVKREKSLSLEQVLEDYIISAGRPALRGFKIGHCSPSIAVPIGAKAAMNTAEKTAVIEAGVSEGALKT | Function: May be involved in the degradation of peptidoglycan by catalyzing the cleavage of the terminal D-alanine residue from cytoplasmic murein peptides.
Sequence Mass (Da): 34596
Sequence Length: 319
Pathway: Cell wall degradation; peptidoglycan degradation.
Subcellular Location: Cytoplasm
EC: 3.4.16.-
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Q9HTZ1 | MTSRPSSDQTWQPIDGRVALIAPASAIATDVLEATLRQLEVHGVDYHLGRHVEARYRYLAGTVEQRLEDLHNAFDMPDITAVWCLRGGYGCGQLLPGLDWGRLQAASPRPLIGFSDISVLLSAFHRHGLPAIHGPVATGLGLSPLSAPREQQERLASLASVSRLLAGIDHELPVQHLGGHKQRVEGALIGGNLTALACMAGTLGGLHAPAGSILVLEDVGEPYYRLERSLWQLLESIDARQLGAICLGSFTDCPRKEVAHSLERIFGEYAAAIEVPLYHHLPSGHGAQNRAWPYGKTAVLEGNRLRW | Function: Releases the terminal D-alanine residue from the cytoplasmic disaccharide-tetrapeptide GlcNAc-MurNAc-L-Ala-gamma-D-Glu-meso-Dap-D-Ala, which is a murein turnover product. Probably also act on free tetrapetide. May be involved in murein recycling.
Catalytic Activity: H2O + N-acetyl-D-glucosaminyl-N-acetylmuram... |
Q68F33 | MASAENLYQEKMQELQKQMNKVMQTINNHSKVEAFLNSPFGQYLDQHPFVTLSLLVFISLSAVPVGIFLTLIAGTAIAVCLAVLIIEGIVISVGGIALLCILCGLAVMSLGVAAVLCVSYVAGSSVLNYIHAYRVTVGTRGRSGPISLNHETTTAEKSYRSS | Function: Plays an important role in the formation of lipid droplets (LD) which are storage organelles at the center of lipid and energy homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17291
Sequence Length: 162
Subcellular Location: Endoplasmic reticulum membrane
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P55796 | MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPPTQRPITRTVRQAGQEPLWLYQGDNVPRAPSTADHPILPSKIDDVQLDPNRRYVRSVTNPENNEASIEHSHHTVDIGLDQPIESHRNTRDLRFLYPRGKLPVPTLPPFNPKPIYIDMGNRYRRHASEDQEELRQYNEHFLIPRDIFQE | Function: Antibacterial peptide.
PTM: O-glycosylation is important for the antibacterial activity of lebocin.
Sequence Mass (Da): 21013
Sequence Length: 179
Subcellular Location: Secreted
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A9YWS7 | MALSNLKSNRTLSSSLITIFIISLFLQYHNIKSQSSWQSRQVPRSETVAFSITEFEKENPDIFLRGDTSISDGILRLTKTDQSGKPLPNTVGRATYLTPIHIWDKTSGELADFSTSFSFIVNTNDSDLHGDGFAFYLGPLHFDVPKNSSGGYLGLFDPENAFPPSKTPILAIEFDGFTNEWDPPSSFQSPHIGIDVGSIVSLEYAQWPINFVPRNALGEANINYNSESKRLSVFVAYPGTQWNSTRVSVVVDLRSVLPEWVRIGFSATTGELVETHDIINWSFESAL | Function: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31923
Sequence Length: 287
Subcellular Location: Membrane
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P93114 | MAVPMDTISGPWGNNGGNFWSFRPVNKINQIVISYGGGGNNPIALTFSSTKADGSKDTITVGGGGPDSITGTEMVNIGTDEYLTGISGTFGIYLDNNVLRSITFTTNLKAHGPYGQKVGTPFSSANVVGNEIVGFLGRSGYYVDAIGTYNRHK | Function: Mannose-binding lectin . Preferentially binds mannose at concentrations ranging between 5 and 25 mM, but binds also glucose. Has a marked preference for methylated sugar derivatives, such as alpha-MeMan and alpha-MeGlc, at concentration down to 5 mM . Binds to N-glycans, but not to glycolipid-type or other ty... |
P06027 | GCCPTFWTSFGSNCYRFFAVSLTWAEGEQFCQSFSVPSRGDIDSIGHLVSIHSETEQNFVYHYFETSTKDDTTPEMWLGFNDRTTEGNFQWTDGSPNDFTAWVGSNPDNYGSGEDCTQMVMGAGLNWIDLPCSSTRHYLICKLPLWE | Function: Role in the defense system of the organism against microorganisms. This lectin is specific for Gal-GalNAc.
PTM: The identity of the saccharide is not reported in PubMed:3571253, and it is unlikely to be N-acetylgalactosamine. The sugar attached to Ser-38 is represented simply as Hex.
Sequence Mass (Da): 16661... |
D4AL26 | MKLLHFTILLQVSLFPASSLAQAGGNNTEVQVQQTLPGTGIAAVNSVNLLRIYSQDTSGGIREARFEGYWSGGLANDTIAKARANSSIAAASDDLELYKSSSSTNFLLKIRVYYLLPNNTLGEAASDSQSRWYTGSLNQYNFQVASHSRLAAVFVPSTQRPRLRIYAQLGDNTIQEFGYDVSPLSQLEPMFANYLKVGRGWQRLANFGPALPGTGIAALTYTTGLRRSTTRVYFQTTDRRVVERVYDNRSWSDGGTVVRTAKPRTPLAATSFLLTPGNPQSVRVYYGTEDNRILEKGTEGGTYWYDGAFEHSAIPDSQVA... | Function: Probable L-fucose-binding lectin.
Sequence Mass (Da): 40297
Sequence Length: 365
Domain: Adopts the six-bladed beta-propeller fold and contains six binding sites per monomer, each located between two adjacent blades (By similarity). The six binding sites that are non-equivalent, and owing to minor differences... |
Q8NC56 | MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEARLRDEERLREEARPRGEERLREEARLREDAPLRARPAAASPRAEPWLSQPASGSAYATPGAYGDIRPSAASWVGSRGLAYPARPAQLRRRASVRGSSEEDEDARTPDRATQGPGLAARRWWAASPAPARLPSSLLGPDPRPGLRATRAGPAGAARARPEVGRRLERWLSRLLLWASLGLLLVFLGILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPENLKSKCIPVMEAQEYIANVTSSSSAKF... | Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization, maintenance of nuclear envelope (NE) integrity and NE reformation after mitosis . Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereb... |
P94565 | MRKINFFDTTLRDGEQSPGVNLNTQEKLAIAKQLERLGADIIEAGFPASSRGDFLAVQEIARTIKNCSVTGLARCVKGDIDAAWEALKDGAQPRIHVFIATSDIHLKHKLKMTREQVIERAVGMVKYAKERFPIVQWSAEDACRTELPFLAEIVEKVIDAGASVINLPDTVGYLAPAEYGNIFKYMKENVPNIHKAKLSAHCHDDLGMAVANSLAAIENGADQIECAVNGIGERAGNAALEEIAVALHTRKDFYQVETGITLNEIKRTSDLVSKLTGMAVPRNKAVVGDNAFAHESGIHQDGFLKEKSTYEIISPELVGV... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56912
Seque... |
Q89A49 | MTQKIIIFDTTLRDGEQSLKMSLSVKKKLKIAFALEKLGVDVIEAGFPISSPGDFESVKKISERIKDAKICSLARCIDGDIDIAAKAMKKANSFRIHIFLGTSALHVQSKLKKTFDQIIDMMVSSVKRAQKYTDDVEFSCEDAGRTSLDDLCRIIELAIDLGVKTINIPDTVGYTIPYEFSNIISSIYKKVPNIDKAIISVHCHDDLGMAVANSISAIQVGARQIEGTITGVGERAGNAALEEILMAIKIRKDILNFKTNIKYQEIYSTCRVISSICNIPVPVNKAIIGSNAFSHSSGIHQDGILKDKKTYEIIVPESIG... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 43227
Seque... |
Q9HXK5 | MSMLKDPSQKYRPFSAINLPDRTWPSKTITEVPIWCSSDLRDGNQSLIEPMDAAKKMRFFKTLVQVGLKQIEVAFPSASDTDFNFVRELIEGNHIPDDVTIQVLTQAREDLITRTFESLRGAKKAIVHVYNATAPSFRRIVFNQDKQGVVDIATNAAKLIKKLAAEQPETQWSFQYSPEIFSSTELEFSVEVCNAVIDVWQPTPDNKIILNLPATVECATPNVYADQIEWFGRHVDKRDSVIISLHTHNDRGTGVAATELGLMAGADRVEGCLFGNGERTGNVDLVTLALNMYTQGLHPQLDFSDIDAVRKVVEECNQLP... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 61727
Seque... |
P56933 | MKKNYRIAVLSGDGIGPEVMQEACKILNVLKKYFFLSLEIQKFNIGGIAIEREGVALPKTTLLGCENSDSILLGSVGGKKWDNLPVEQRPERAALLPLRKHFNLFSNLRPAKLYPELKCLSPLRSDIVKNGFDILCVRELTGGIYFGEPKGFVNKNNTKYAFDTEIYHEYEIIRIAHLAFKLARSRKKKVCSIDKSNVLQSSILWREVVESVSKKYPDVHLSHLYIDNAAMQIIKDPNQFDVLLCSNLFGDIISDECATITGSIGMLPSASFNEKNFGLYEPAGGSAPDIEGKNIANPIAQILSLSMLVRYGMNLNQIAD... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
Q9AQC8 | NQFDILLCSNLFGDIISDECAVITGSIGMLPSASFNEKNFGLYEPAGGSAPDIAGKNIANPIAQILSLSMLVRYGMKLKKIADKIDKSVASALKAGYRTADISNNNSYLKTNEMGDVISDFLINGK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity).
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-me... |
B1VZ57 | MSRSIDLAVIPGDGIGQEVVAQGLKVLNAVLPQDVKLETKEYDLGAQRWHRTGDTLPDAELEALKGHDAILLGAIGDPSVPSGVLERGLLLKLRFAFDHFINLRPSKLFPNTATPLAGRPDIDFVVVREGTEGPYTGNGGSLRTGTPAEVATEVSLNTAYGVERVVRDAFERAAARPRKKLTLVHKNNVLVYAGHLWKNTFDKVAAEYPQVSTDYLHVDAATIFFVTQPERFDVIVTDNLFGDILTDLAAAVSGGIGLAASGNINPTGAFPSMFEPVHGSAPDIAGQGKADPTATVLSVALLLRHLGYEAEAARIEDAVS... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
Q8DTG3 | MKKIVTLAGDGIGPEIMAAGLEVFDAVAQKINFDYEIEAKAFGGAGIDASGHPLPDDTLAAAKTADAILLAAIGSPQYDKAPVRPEQGLLAIRKELNLFANIRPVRIFDALRHLSPLKAERIAGVDFVVVRELTGGIYFGQHTLTENSACDINEYSASEIRRIMRKAFAIARGRSKKVTSIDKQNVLATSKLWRQIAEEVAKEYSDVTLEHQLVDSAAMVMITNPACFDVVVTENLFGDILSDESSVLPGTLGVMPSASHSESGPSLYEPIHGSAPDIAGKGIANPISMILSVAMMLRDSFGETAGAEMIEHAVNKTLTQ... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
Q30RK2 | MKTYKIALIKGDGIGPEIIDEAVKVLDAVASCCDLEFSYEEALMGGCAYDITGDPLPQETINISLNSDAVLFGAIGGAKWDNLPREKRPESGLLRFRKELGVYANLRPANVFDELINASSLKAEVIKGVDLMVVRELIGGIYFGEPKGRDENRGWNTMVYTREEIVRIAHQAFKIAMSRSKRVCSIDKANVLDVSQLWREVVIEVAKEYPEVELTHMYVDNAAMQLIRDPRQFDVMLTGNIFGDILSDEASMLSGSIGLLPSASVGAKIGVYEPIHGSAPDIAGQGIANPIATILSASMMLRYALGEHGAADKIDAAVKR... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
P50455 | MGFTVALIQGDGIGPEIVSKSKRILAKINELYSLPIEYIEVEAGDRALARYGEALPKDSLKIIDKADIILKGPVGESAADVVVKLRQIYDMYANIRPAKSIPGIDTKYGNVDILIVRENTEDLYKGFEHIVSDGVAVGMKIITRFASERIAKVGLNFALRRRKKVTCVHKANVMRITDGLFAEACRSVLKGKVEYSEMYVDAAAANLVRNPQMFDVIVTENVYGDILSDEASQIAGSLGIAPSANIGDKKALFEPVHGAAFDIAGKNIGNPTAFLLSVSMMYERMYELSNDDRYIKASRALENAIYLVYKERKALTPDVG... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
Q67JY2 | MAQPTYHIACLPGDGIGPEVTRGAVTVLQAAAAAYGFRLEFSEYLVGGAAYDAVGTPFPDETRDACDRADAILFGAVGGPRYEGLPWDLRPEAGLLAIRKRYDLYANLRPILLYPPLKDASPLKNEIIGGGVDFIIVRELVGGIYFGEPRGIETLPDGTRRGVNTEVYTDAEIARIARMGFEIARGRRRRLTSVDKGNVMEAGKLWRTVVDEVAREFPDVEVEHLLADNAAMQILRRPGDFDVMLASNLFGDFLSDEAAMLTGSIGLLPSASLGAARNRFGLPKGFYEPIHGSAPDIAGQDRANPLAAILCGAMLLRHSL... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
P49601 | MAPKTLYEKIFDSHLVHEEADGTCLIYIDRHLVHEVTSPQAFEGLRNANRKVRRTDCTLATVDHNIPTASRKSYRDTKSFVEQVDSRTQCMTLEENVKAFGLTFFGLSDNRQGIVHIIGPEQGFTLPGATIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKRAKNMLIQVDGELSQGVTSKDIILHIIGLIGTAGGTGHVIEYAGSTIRSLSMEARMSICNMSIEAGARAGLIAPDEITYEYIKGRPLAPKQGEAWDQALAYWKTLPSDEGAQYDTVIKIDAKDIPPTVTWGTSPQDVVAITGTVPDPKNASN... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 83224
Sequence Length: 773
Pathway: Amino-acid biosyn... |
Q2L247 | MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKDAEPTPSPILASLSQLLLPLVGRVAAGSPILAAEHVEREVGVDPSLFSQAPDYLLKVRGMSMRDAGILEGDLLAVKKSSEARNGQIIVARLGDDVTVKRLQRHGSRIELLPENPEFSPILVAPDDEFALEGVAVGLIRTHALH | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q7WCK0 | MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDSATPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFAPIVVANTDEFALEGIAVGLIRTQPLH | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
A6X0K7 | MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLNAQKKFAPSVIEGSLGKTPPPPARPAPVATNDDTSGTVSVPVMGRIAAGVPISAIQNQTHSLSLPPEMIGAGEHYALEVRGDSMIDAGIFDGDTVIIKRGDSANPGEIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVRVQGKLVGLIRRY | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
P61612 | MDDSNDSSSAGPDGRLHAVDPSLTERQRTILNVIRSSVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGVDDDVAAPATEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGDGTLFLLKVVGDSMVEAAICDGDWVVVRQQHVADNADIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
A0QVY5 | MSDDTGEFTDGSTESPADADGAGRRRAVDNGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRAADDPAAAAVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRARGQVWLMPHNPAYDPIPGNEAAVLGKVVTVIRKI | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q1D406 | MEELTERQREILSFIVKETETRGFPPTIREIGEHMDIRSTNGVNDHLKALERKGYLNRGEQQSRSLVATKRARLLLGLGARKDSGMVEIPLLGKVAAGAPLLAQENMEDSVKIDSFLLGGVNGREVFALRVKGQSMIDDGIHDGDYLFVKKTPSAQPGEIVVALIEDEATVKRYYPEGDRIRFQPANATMQPIYVSRAEFRSTMILGQVVGVYRKLQGGRTP | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q2G6Q5 | MLTRKQHELLTFIQTRLEDSGISPSFEEMKEALDLKSKSGVHRLISALEERGFIRRLPNRARALEVLRQPDSAVGKAAPVSQREAANTNSALPPLRAAPKAAPAPANDVIELPLHGKIAAGVPIEALETTATLPVPAALLGAGEHYALEVSGDSMVEAGIFDGDYALVRKTDVARDGEIVVALVRGEEATLKYLHREKGMVRLDPANAAYDPQYYRPEEVAVQGKLAGLLRRYH | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q8JHF2 | MLKTYRGKVVVSLAGATVTCLGFLLFLSQHQRIQADGMQNESEVGLRSLQSLGDSETDDGAQPEQNAKKGFSAYFSKLTRSRREADKPSEAPGAATDAPPAEDISADDIFIAVKTTKKFHRSRLDLLLDTWISRNMRQTYIFTDGEDEELKKKIGSHAINTNCSAAHSRQALSCKMAVEYDKFIESGKKWFCHVDDDNYVNTKTLVKLLSNYPHTQDMYIGKPSLDRPIEATERLGDNKMRPVNFWFATGGAGFCISRGLALKMSPWASGGHFMNTAEKIRLPDDCTIGYIIESVLGVSLTRSSLFHSHLENLQQVSKSE... | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Involved in the correct formation of boundaries in the somites and hindbrain (By similarity). Required for Delta-Notch-mediated induction of hypochord cell... |
O09010 | MLQRCGRRLLLALVGALLACLLVLTADPPPTPMPAERGRRALRSLAGSSGGAPASGSRAAVDPGVLTREVHSLSEYFSLLTRARRDADPPPGVASRQGDGHPRPPAEVLSPRDVFIAVKTTRKFHRARLDLLFETWISRHKEMTFIFTDGEDEALAKLTGNVVLTNCSSAHSRQALSCKMAVEYDRFIESGKKWFCHVDDDNYVNLRALLRLLASYPHTQDVYIGKPSLDRPIQATERISEHKVRPVHFWFATGGAGFCISRGLALKMGPWASGGHFMSTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQV... | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement ... |
A0R5K5 | MSTCIEGTPSTTRTPTRAWVALAVLALPVLLIAIDNTVLAFALPLIAEDFRPSATTQLWIVDVYSLVLAALLVAMGSLGDRLGRRRLLLIGGAGFAVVSALAAFAPSAELLVGARALLGVFGAMLMPSTLSLIRNIFTDASARRLAIAIWASCFTAGSALGPIVGGALLEHFHWGAVFLVAVPILLPLLVLGPRLVPESRDPNPGPFDPVSIVLSFTTMLPIVWAVKTAAHDGLSAAAAAAFAVGIVSGALFVRRQNRSATPMLDIGLFKVMPFTSSILANFLSIIGLIGFIFFISQHLQLVLGLSPLTAGLVTLPGAVV... | Function: Energy-dependent efflux pump that contributes to drug resistance . Catalyzes the efflux of norfloxacin and several related fluoroquinolones (FQ) . Contributes significantly to the intrinsic MICs for ethidium bromide and acriflavine . Overexpression confers low-level resistance to hydrophilic FQ such as ciprof... |
A3DES1 | MPVFRLTDKLVFPHPSLADEDGILAVGGDLSCERLLLAYKNGIFPWFSEDEPILWWSPNPRCVLFPKDIKISRSMRKFLKKQLYEVTFDTCFRHVIAMCAKLREGNTWITPEIIESYSKLHDLGFAHSVETWYEGRLVGGLYGVSLGKCFFGESMFSTMDNASKTALITLCQKLEEKGFLLIDCQVYSKHLESLGAVNIDRDLFLKYLEAGLSHETLRGNWKFFNEQKQVRNN | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q6FDS1 | MILPSMYVFPDPPEADPEGQGLICIGADLEPSTLFEAYTHGLFPWFNEGDPICWWSPEPRCVIYPEQYQPSKTLIRSMKKYDYQITMNRAFEKVIRSCALPRNYTNETWISEDIVQGYVELFKAGYAYSVEVWENDQLIGGLYGVNIGKGCFGESMFSLRTDTSKIAFYTLMLIGQENQVPWVDCQLVNDHLISLGACTLSRQAYLKSLQDVIIQPPINWKRYQERVFSSKRIAQNAKLTE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
A0KJE0 | MSRYLTQLDDELCWFPDPEHALEEPNGLLAIGGDLSPARLLAAYHKGIFPWNEPHQPLLWWSPDPRGVIRPEQLHIGRTLRKFIRGTSFDISIDRAFNEVIAACAAPRRSASGTWISTPMIDAYRQLHRLGHAHSIEIWQEGQLQAGLYGLSLGRVFCGESMFSRIDNGAKLAMVALCQHFARHDGALIDCQMQNDFLATLGIEEWPRRQFLTTLAQLSRQPLAANCWQTGSILL | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q8UFR8 | MAGRRSRNNDITVDILLRAYSAGLFPMADSADDPELFWVEPEIRGIIPLDDFHVSKSLAKAMRKKPFAIRFNTAFEDVMAGCAAEAADRPSTWINATIRRLYTELHQIGHAHSVEAWEGDELVGGLYGVSLGAAFFGESMFSRRTNASKICLVHLVERLNAKGFVLLDTQFTTEHLKTFGAIDVPKLDYARMLDLAVNRPSLQF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
B2UNS0 | MNDRLTPELVLSAYCQGCFPMADPETGEISFYEPDPRALIPLDDRFHIPHGLKRALNKKPFELRMDTAFPEVVHACARTDQPEEQWIDGQIEEAYGKLHEMGFAHSVECWDEEGLQGGLYGVALGKAFFGESMFHRKTDASKIALVALVQYLRAHRFLFLDTQWTTPHLLKFGTYEVPAKEYRKLLKRALEEQ | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
C4XT58 | MPVFALIDEPVFPSPHLAEPGGLLAVGGDLSVARLLAAYRRGIFPWYDDESPILWWSPDPRPILVPGHVRVSKRLERTIRSGKFTVTLDTDFAGVIRGCAAVPRDADNGTWIVPDMIEGYERLHAAGHAHSVEAWQNGELVGGAYGVAIGKAFFGESMFHRATDASKVAFVTLCRFLDRHEFRFIDCQQATGHLLRFGAVQVRRNEFLRRLEAAREEEGMVGKWVLPRTTRCASPQPTSESSPSAKQ | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q30TE4 | MIPKLLKHELTFPHPNDATEDGIVAWGGDLNPSRLIRAYQNGIFPWYGKNDPIIWWSPNPRLIMELDDFKLSRSLRKSMKKFEYRFDTNFINVMKNCQNIKRVKQDGTWIQDEIIEAYSVLHDMGIAHSVESYLDGELVGGLYGVAVGGLFCGESMFTLVNDASKSAYAVLINHLKIWGYDFIDAQVPTEHLKNLGAKEVSRDYFLDRLHKVNMNIINHKWELLHVNT | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q2LQL0 | MPICPLGKVIVFPPVSLAMEDGLLAVGGDLSPYRLLEAYRQGIFPWYSPGEPILWWAPQPRFVLFPDEILLSRSMRQILRKKHFQVTLDRNFDAVIHACATIGRPAQEGTWITEEMQEAYSILHELGYAHSVEVWRDRGLIGGLYGVSLGGCFFGESMFSRESNASKAALIFLSSLLKILRFTLIDCQVYTSHLALLGARFIPRETFTALIRKSLRRPTLRGNWSTHPETADKLPGHEF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
A0LE95 | MPVFRLTEELIFPPSYLAERDGLLAVGGDLSAERLLLAYRQGIFPWYTEKTPILWWSPDPRLVLFPAELKISISLRRVLRKNVFSVTFDRAFADVIRRCAEVRRARDDSTWIVPGMVTAYSRLHRLGYAHSVESWHEGELVGGLYGVALGRVFYGESMFTRKTDASKVALVHLVDLLTRGGFQLIDCQVTTAHLQSMGAREISRRRFLTLLAENIPEVVHGESWEGESCCGKRP | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q2JWL1 | MQVDIGAILTGYAQGYFLMADEETGSLAWYGTEQHALIPLDERFHCPRSLRPLVRGSCFQVRINGAFEQVVEGCAARPQTWISSELKQIYLALHQAGFAHSFETWQGDTLAGGILGIALGAAFIGESMFYRIPNASKVALVKLVEHLRERGFRLFDAQLMNPHLARFGAFLMDGRDYQELLQQCLRIPCRFD | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
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