ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
F7IX06 | MSVTTPRRETSLLSRALRATAAAATAVVATVALAAPAQAANPYERGPNPTESMLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASSAVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGAEYDTIASVTLHSKPFYNSIPSPTDKAYLELDGASHFAPNITNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLSDVEEYRSTCPF | Cofactor: Can also bind other divalent metal ions with lower efficiency . Calcium ion binding contributes to the thermostability of the protein .
Function: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle . Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) . Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (By similarity). Can also depolymerize the synthetic polyesters poly(epsilon-caprolactone) (PCL), poly(butylene succinate-co-adipate) (PBSA), poly(butylene succinate) (PBS), and poly(lactic acid) (PLA) .
Catalytic Activity: an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+)
Sequence Mass (Da): 32353
Sequence Length: 300
Subcellular Location: Secreted
EC: 3.1.1.74
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Q85FM5 | MDSVTIAWAALMAISTFSLSLVVRGRSGL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3054
Sequence Length: 29
Subcellular Location: Plastid
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P61039 | MDIVSLAWAALMVVFTFSLSLVVWGRSGL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3170
Sequence Length: 29
Subcellular Location: Plastid
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O14136 | METNQNEKGPSLPSYPAGGIMSVSNSNADTNQGVTQHPLANRIVNPNYYNMGFNPYSGFNSFIPSFNPFVPLETNLPGNGPISSLQVIESIVGAVGSIAQVLESTLMAAHMSYNTFVSVSENLNKLKSSIGAIFGIVSLLSRLKRLVLKFFKHSKIDEMNSQEYDVFEKEEGNHKNSIYSIVSSLAIILGLVGLPYAIIRLFKNIYEKEKQIQQAKIRKKIDSLEFCKADYEFMSRDPGVEMSLKKGDIIAILSKTDTQGNPCEWWQGRKRSGETGWFPSNYCSIISR | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32055
Sequence Length: 288
Subcellular Location: Peroxisome membrane
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P80667 | MSSTAVPRPKPWETSASLEEPQRNAQSLSAMMTSNQQDSRPTEESNNSNSASESAPEVLPRPAALNSSGTYGESNTIPGIYGNSNYGIPYDNNPYSMNSIYGNSIGRYGYGGSYYGNNYGSFYGGGYGAGAGYGMNNGSGLGESTKATFQLIESLIGAVTGFAQMLESTYMATHNSFFTMISVAEQFGNLKEMLGSFFGIFAIMKFLKKILYRATKGRLGIPPKNFAESEGSKNKLIEDFQKFNDSGTINSNEKATRRKISWKPLLFFLMAVFGFPYLLNKFITKLQTSGTIRASQGNGSEPIDPSKLEFARALYDFVPENPEMEVALKKGDLMAILSKKDPLGRDSDWWKVRTKNGNIGYIPYNYIEIIKRRKKIEHVDDETRTH | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX21 receptors . The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm . Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42706
Sequence Length: 386
Subcellular Location: Peroxisome membrane
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Q9FXT6 | MATHQQTQPPSDFPALADENSQIPEATKPANEVQQATIAQDPPTSVFKNSEPIREDQIQNAIKFLSHPRVRGSPVIHRRSFLERKGLTKEEIDEAFRRVPDPPPSSQTTVTTSQDGQQAVSTVQPQAMQPVVAAPAPLIVTPQAAFLSRFRWYHAILAVGVLAASGAGTAVFIKRSLIPRFKSWVQRIMLEEETDPLKKADAKPSLAEEAVAAAKAASAAASDVARVSQEMMITKNEERKYFEDLTHLLGVQVQEMKSLSNNIRKLEGQSNNIPKIYSADQEVYNGSVTTARKPYTNGSNVDYDTRSARSASPPAAPADSSAPPHPKSYMDIMSMIQRGEKPSNIREINDMPPNPNQPLSDPRIAPKSKPWDYGQAPQDESSNGQWWQQKNPRSTDFGYETTTAARFTANQNETSTMEPAAFQRQRSWVPPQPPPVAMAEAVEAIRRPKPQAKIDQEAAASDGQSGVSDELQKITKFSESGGDGSGGIKIAEIQEETEQQHISQEGN | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor . The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55595
Sequence Length: 507
Subcellular Location: Peroxisome membrane
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Q54C55 | MDNDDINNNNNNNNNNNNNNNSQELDQQEQTQEEITKQRIQKRKEEAKRIMEERKKREQQPPSQRQYEDVEDDQQQQPIRPIKQLPQRQQQYDDNDEPPQQQQYEPKISQRKVPLPPMKQPTTSSTASAATGSILSPSSNFREDMVKKAVLFLNNPNVKNTALARKVAYLEKKGLTSDEVKEALKRVETGNINGSSTNNSNITQSNSISRTRNDNYGNNNNNSSNNNNNIQQQQYYQQQQQQHQQQQQMALTQIQSYQKRLEADDQRIAQLMMNNNRFSWNSFLFSVTAIVGAASGLAYLTSNYIIPFLNGGKTNKDASANMDKKITSLQEEIIKLQSTIIQQGNDFRESTKSLKTLIEQQQQQILQQQQINSVSTTTNSATSASNSSEIVEIKKELKNLINLIGNKENSNNSNNNSNNSNNNNGYSKYNGFNGVYNKSSYDDVSTNNNNKTNSPPSPNKPTTTTTTTATSTPGSNISNTNKTLPPIIKTNPYSHLSWKLPTDQPPVIPSWQQKSSNPPSDLSNANDKSSPSNSNPSTPTKPYQSSFNYGDVNSFVGGSNTLNFDEKPTTTTTTSTTPSNERPSSPSVNNNNNNNNNNNNNNNNNNNNNNNTTIASTSNESNNSKVETTSNDSDKSTSPSSSSNNTTSTTATTTTITSASTEDNKQQSDETPYSSDFLDVINQLKQGKTPPGIRTDIDDKPLENSTVTKSAKERPKKPWERDTLTSVTNNLSVEETQTINNTDSSVEK | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (By similarity). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 83361
Sequence Length: 748
Subcellular Location: Peroxisome membrane
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O75381 | MASSEQAEQPSQPSSTPGSENVLPREPLIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQQSGTAADEPSSLGPATQVVPVQPPHLISQPYSPAGSRWRDYGALAIIMAGIAFGFHQLYKKYLLPLILGGREDRKQLERMEAGLSELSGSVAQTVTQLQTTLASVQELLIQQQQKIQELAHELAAAKATTSTNWILESQNINELKSEINSLKGLLLNRRQFPPSPSAPKIPSWQIPVKSPSPSSPAAVNHHSSSDISPVSNESTSSSPGKEGHSPEGSTVTYHLLGPQEEGEGVVDVKGQVRMEVQGEEEKREDKEDEEDEEDDDVSHVDEEDCLGVQREDRRGGDGQINEQVEKLRRPEGASNESERD | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor . The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix . Plays a key role for peroxisome movement through a direct interaction with tubulin .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 41237
Sequence Length: 377
Subcellular Location: Peroxisome membrane
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Q9R0A0 | MASSEQAEQPNQPSSPPGSENVVPREPLIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDLAFQQSGTAADEPSPLGPATPVVPVQPPHLTPQPYSPRGSRWRDYGALAIIMAGIAFGFHQLYKRYLLPLILGGREDRKQLERMAASLSELSGTVAQTVTQVQTTLASVQELLRQQQQKVQELAHELATAKATTSTNWILESQNINELKSEINSLKGLLLNRRQFPPSPSAPKIPSWQIPVKSSSPSSPAAVNHHSSSDISPVSNESTSSSPGKDSHSPEGSTATYHLLGPQEEGEGVLDVKGQVRMEVQGEEEKREDKEDEDDEDDDVSHVDEEDVLGVQREDRRGGDGQINEQVEKLRRPEGASNETERD | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (By similarity). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix. Plays a key role for peroxisome movement through a direct interaction with tubulin (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 41208
Sequence Length: 376
Subcellular Location: Peroxisome membrane
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P78723 | MSQQPATTSRAELVSSAVEFLLDQSIADSPLAKKVEFLESKGLTQQEIEEALQKARTGTVQASPSQQSVVPPRPPVPDYYPSAPPLPERDWKDYFIMATATAGISYGVYQFVKRYVVPKILPPSKTQLEQDKAAIDHEFQRVESLLEKFEADQKEFYQKQEAKSKKIDETLQEVDEIINKTNEKNLNNEETLKYLKLEIENIKTTLLKTLDSQKATLNAELSAMEKQLQDIKFDIKTSGIAVAPQLSTPPSESTSRQSPAAEAKPKINLNIPPTTSIPSLRDVLSREKDKDVNSDSIAQYEQRTANEKDVERSIPAWQLSASNGGSSTTSGVAGDEQKEPKRGIPAWQLNA | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39034
Sequence Length: 351
Subcellular Location: Peroxisome membrane
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Q9HG09 | MSSIREEMVTSAVEFLKNPQIADSPLAKKIEFIESKGLNEAEVKEALLRSQGGNGSSSVASQVSSYSPSASQSSVAPSPPPFPDHYRNAPPLPERDWKDYFVMATATAGVSFGLYKVISNYVLPKLLPPSKEAIELDKEAIDREFTRVEALLNTFEEDQKAFYEEQREKSGKIEDTLTEIDAIISKTNEKNLNNEESLKYLKLEIESIKNTLMKNIDSQKSTISSELGSIEAQLDELKKLIVAKPEDEPIRAAPQPSLTTGANSLTSESSGRSSIPHSQSVPIRTQLTTPPSDSDTSGPAKLHIPPATSIPSLKDILRKEKNRTVDTFSKSNLGKDLESVAQSDPDKVEKYEGRRDLKSLERPEEDEKKEDDVEDGGDKDKLASSLESVKLPPSSEQVQAPAPKERTSSSSSRSGIPAWQLAAQS | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX20 receptors . The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 (or PEX20) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (By similarity).
PTM: Phosphorylated on serine or threonine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46589
Sequence Length: 425
Subcellular Location: Peroxisome membrane
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O60065 | MREDLLRNSVEFLREKTVLDAPDVKKIEFLKSKGLTAEEIQEAFKLAKNPLFPSYPRFENTSNFVSRDWRDWFIMGVISTGFAWSAYSLVKKYIAPMFRAPSQNAYEADKNALDAKFLEAHKILENLDEQTRKLSERTEKQQDELDIALDDLEETLNTLKRTSENRDREIARISQDVYTMSTITLPQSLEQIKKSQEEALQNLSREISSLRCLQTDSKKDDTFATTSNSSIPVLENPLDTSEGFQTKKVGTASLPDWQISMHNEASKNIDFNDIDPAESYVAEDAY | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32814
Sequence Length: 286
Subcellular Location: Peroxisome membrane
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P53112 | MSDVVSKDRKALFDSAVSFLKDESIKDAPLLKKIEFLKSKGLTEKEIEIAMKEPKKDGIVGDEVSKKIGSTENRASQDMYLYEAMPPTLPHRDWKDYFVMATATAGLLYGAYEVTRRYVIPNILPEAKSKLEGDKKEIDDQFSKIDTVLNAIEAEQAEFRKKESETLKELSDTIAELKQALVQTTRSREKIEDEFRIVKLEVVNMQNTIDKFVSDNDGMQELNNIQKEMESLKSLMNNRMESGNAQDNRLFSISPNGIPGIDTIPSASEILAKMGMQEESDKEKENGSDANKDDNAVPAWKKAREQTIDSNASIPEWQKNTAANEISVPDWQNGQVEDSIP | Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX21 receptors . The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm . Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38420
Sequence Length: 341
Subcellular Location: Peroxisome membrane
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Q08215 | MAASEIMNNLPMHSLDSSLRDLLNDDLFIESDESTKSVNDQRSEVFQECVNLFIKRDIKDCLEKMSEVGFIDITVFKSNPMILDLFVSACDIMPSFTKLGLTLQSEILNIFTLDTPQCIETRKIILGDLSKLLVINKFFRCCIKVIQFNLTDHTEQEEKTLELESIMSDFIFVYITKMRTTIDVVGLQELIEIFIFQVKVKLHHKKPSPNMYWALCKTLPKLSPTLKGLYLSKDVSIEDAILNSIDNKIQKDKAKSKGKQRGVKQKIHHFHEPMLHNSSEEQVKVEDAFNQRTSTDSRLQSTGTAPRKKNNDITVLAGSFWAVLKHHFTRSVLNKNGLLLTGLLLLLCLKKYKSLMAIFKHVPAAFHTVYPQIVGLLKLLASI | Function: Peroxisomal docking factor that anchors PEX1 and PEX6 to peroxisome membranes . PEX26 is therefore required for the formation of the PEX1-PEX6 AAA ATPase complex, a complex that mediates the extraction of the PEX5 receptor from peroxisomal membrane .
PTM: Phosphorylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43676
Sequence Length: 383
Subcellular Location: Peroxisome membrane
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Q8S8S1 | MEAYKQWVWRNREYVQSFGSFANGLTWLLPEKFSASEIGPEAVTAFLGIFSTINEHIIENAPTPRGHVGSSGNDPSLSYPLLIAILKDLETVVEVAAEHFYGDKKWNYIILTEAMKAVIRLALFRNSGYKMLLQGGETPNEEKDSNQSESQNRAGNSGRNLGPHGLGNQNHHNPWNLEGRAMSALSSFGQNARTTTSSTPGWSRRIQHQQAVIEPPMIKERRRTMSELLTEKGVNGALFAIGEVLYITRPLIYVLFIRKYGVRSWIPWAISLSVDTLGMGLLANSKWWGEKSKQVHFSGPEKDELRRRKLIWALYLMRDPFFTKYTRQKLESSQKKLELIPLIGFLTEKIVELLEGAQSRYTYISGS | Function: Involved in the formation of peroxisomes, lipid bodies and protein bodies.
PTM: The detection of an additional immunorelated polypeptide of 52 kDa suggests a post-translational modification of PEX16.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41611
Sequence Length: 367
Domain: The internal domain (235-279) containing two internal membrane helices and the intervening residues that include the basic cluster VRS is sufficient for targeting recombinant proteins to endoplasmic reticulum and then to peroxisomes.
Subcellular Location: Peroxisome membrane
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Q2KII7 | MEKLRLLGLRYQEYVTRHPAATAQLETAVRGLSYLLAGRFADSHELSELVYSASNLLVLLNDGILRKELRKKLPMSLSQQRLLTWLSVLECVEVFMEMGATKVWGEVGRWLVIALIQLAKAVLRMFLLIWFKAGLQTSPPIVPLDREIQAQSRDGDHSSGSQEQSYVGKRSNRVVRTLQNTPSLHSRHWGAPQQREELGVAPTPLGLQETIAESLHIARPLLHLLSLGLWGQRSWTPWLLSGVVDVTSLSLLSDRKGLTRRERLELRRRTILLLYYLLRSPFYDRFSEAKILFLLQLLADHVPGIGLVTRPLMDYLPNWQKIYFYSWG | Function: Required for peroxisome membrane biogenesis. May play a role in early stages of peroxisome assembly. Can recruit other peroxisomal proteins, such as PEX3 and PMP34, to de novo peroxisomes derived from the endoplasmic reticulum (ER). May function as receptor for PEX3 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37574
Sequence Length: 328
Subcellular Location: Peroxisome membrane
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Q4QRH7 | MEKLTRVFERYQEYVRTSPAAASHLESTVRALSYLIAGRFSDSHEISELVYSASNLLVLLNDGILRKNLSRTLPMSISQQKLLTWLSVLEYVEVFVEMAAAKMWGDAGRWLVIVLIQIAKAVLRCLLLFWYKSGIQTSPPIIPLDRDSQLCSQDNNEEEDDEDSSFVGQRSGRVVRPLGSAPSLQSRLWGLPRKKKVSRNQEEELHSSPTPLGLQETIAESLYIARPLLHLASLGICGKRSWKPWILSGLLEITSFSLLSDMKALNRRERAEMRRRAFLLLYYLLRSPFYDRYSETKILFLLRFLADYVPGVGLVARPLMEYLPIWQKIYFYNWG | Function: Involved in peroxisome biogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38555
Sequence Length: 335
Subcellular Location: Peroxisome membrane
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Q9Y5Y5 | MEKLRLLGLRYQEYVTRHPAATAQLETAVRGFSYLLAGRFADSHELSELVYSASNLLVLLNDGILRKELRKKLPVSLSQQKLLTWLSVLECVEVFMEMGAAKVWGEVGRWLVIALVQLAKAVLRMLLLLWFKAGLQTSPPIVPLDRETQAQPPDGDHSPGNHEQSYVGKRSNRVVRTLQNTPSLHSRHWGAPQQREGRQQQHHEELSATPTPLGLQETIAEFLYIARPLLHLLSLGLWGQRSWKPWLLAGVVDVTSLSLLSDRKGLTRRERRELRRRTILLLYYLLRSPFYDRFSEARILFLLQLLADHVPGVGLVTRPLMDYLPTWQKIYFYSWG | Function: Required for peroxisome membrane biogenesis. May play a role in early stages of peroxisome assembly. Can recruit other peroxisomal proteins, such as PEX3 and PMP34, to de novo peroxisomes derived from the endoplasmic reticulum (ER). May function as receptor for PEX3.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38629
Sequence Length: 336
Subcellular Location: Peroxisome membrane
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Q91XC9 | MEKLRLLSLRYQEYVTRHPAATAQLETAVRGLSYLLAGRFSDSHELSELVYSASNLLVLLNDGILRKELRKKLPVSLSQQKLLTWLSVLECVEVFMEMGAAKVWGEVGRWLVIALIQLAKAVLRMLLLIWFKAGIQTSPPIVPLDRETQAQPLDGDHNPGSQEPSYVGKRSHRVVRTLQNSPSLHSRYWGAPQQREIRQKQQQEELSTPPTPLGLQETIAESLYIARPLLHLLSLGLWGQRSWTPWLLSGVVDMTSLSLLSDRKNLTRRERLELRRRTILLLYYLLRSPFYDRFSEAKILFLLQLLTDHIPGVGLVARPLMDYLPSWQKIYFYSWG | Function: Required for peroxisome membrane biogenesis. May play a role in early stages of peroxisome assembly. Can recruit other peroxisomal proteins, such as PEX3 and PMP34, to de novo peroxisomes derived from the endoplasmic reticulum (ER). May function as receptor for PEX3 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38677
Sequence Length: 336
Subcellular Location: Peroxisome membrane
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A7MAS3 | MVTKDSIIRDLERENVGPEFGEFLNTLQTDLNSEKPPIEQVKSQLETHFNLAHETQEFSRKNDNAPVDKLLTNYYNNYEVNVLEFVLQMGFSRDLSIPLNVWFVLDMISQLSTSKQDLPLDYYLVLNNSQTGKYSDFVRYLIYEAVGAEIHCFEQGSMPEQYRSSRWEDKVKGPALANRGPIRGNVGAGDRKITFHLLCKKTARMILVGDDRETDFEMSDRSFVTLLLDYYQRVGTTKKIDLLLLTNNFDTNMNNKLQQLKILESLNMLKSNCYVLDYQITVDQVTANFNSYVEGIPAFRRHEIANFLKKRKTPKNADELIFKYVGRWNICYQKKFHQGNISIHQISGYLD | Function: Structural subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Not required for catalytic activity. Fine-tunes allosteric regulation of the ATP-PFK by ATP, fructose 2,6-bisphosphate and AMP.
Sequence Mass (Da): 40796
Sequence Length: 351
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
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Q9FC99 | MRIGVLTSGGDCPGLNAVIRSVVHRAVVDHGDEVIGFRDGWKGLLECDYLKLDLDAVGGILARGGTILGSSRVRPEHLRDGVERARGHVEELGLDAIIPIGGEGTLKAARLLSDNGLPIVGVPKTIDNDIAVTDVTFGFDTAVTVATEALDRLKTTAESHQRVLIVEVMGRHTGWIALHSGMAAGAHAVVVPERPFDIDELTAKVGERFSAGKRFAIVVAAEGAKPKAGTMDFDEGGKDVYGHERFAGIARQLSIELEERLGKEARPVILGHVQRGGTPTAYDRVLATRFGWHAVEAVHRGEFGKMTALRGTDIEMVSLADAVESLKTVPDARYAEAECVL | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 36432
Sequence Length: 341
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q9FKG3 | MEASISFLGSTKPNISLFNPSSNVLPRRDFPLPALKLKKVSVLPRILHQKRLIRAQCSDGFKPEEDDGFVLEDVPHLTKFLPDLPSYPNPLKESQAYAIVKRTFVSSEDVVAQNIVVQKGSKRGVHFRRAGPRERVYFRSDEVKACIVTCGGLCPGINTVIREIVCGLNNMYGVNNILGIQGGYRGFYSKNTMNLTPKVVNDIHKRGGTFLQTSRGGHDTAKIVDNIQDRGINQVYIIGGGGTQKGAEKIYEEVERRGLQVAVSGIPKTIDNDIAVIDKSFGFDTAVEEAQRAINAAHVEVESVENGVGIVKLMGRYSGFIAMIATLANRDVDCCLIPESPFFLEGKGGLFEFIEERLKENRHMVIVIAEGAGQDYVAQSMRASETKDASGNRLLLDVGLWLTQQIKDHFTNVRKMMINMKYIDPTYMIRAIPSNASDNVYCTLLAQSAVHGAMAGYSGFTVGPVNSRHAYIPISQVTEVTNTVKLTDRMWARLLASTNQPSFLTGEGALQNVIDMETQEKIDNMKISSI | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 58467
Sequence Length: 530
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Plastid
EC: 2.7.1.11
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Q8VYN6 | MDALSQAISSGISVPYKNNSSSLVPSHGLTSLILRKSRSPVNPSSRSRVSVRASEIQHSKTSASSIDLSDPDWKLKYEKDFEQRFSIPHITDVLPDAEAIRSTFCLKMRSPTEDFVGGYPSDEEWHGYINNNDRVLLKVISYSSPTSAGAECLDHDCSWVEQWIHRAGPREKIYFRPEEVKAAIITCGGLCPGLNDVIRHIVITLEIYGVKNIVGIPFGYRGFSDKDLTEMPLSRKVVQNIHLSGGSLLGVSRGGPSVSEIVDSMEERGINMLFVLGGNGTHAGANAIHNECRKRKIKVAVVGVPKTIDNDILHMDKTFGFDTAVEEAQRAINSAYIEAHSAYHGIGVVKLMGRNSGFIAMQASLASGQVDICLIPEVPFNLHGPNGVLKHLKYLIETKGSAVICVAEGAGQNFLEKTNAKDASGNAVLGDFGVYIQQETKKYFKEISTPIDVKYIDPTYMIRAVRANASDGILCTVLGQNAVHGAFAGYSGITVGIINTHYAYLPITEVIAYPKSVDPNSRMWHRCLTSTGQPDFI | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 58615
Sequence Length: 537
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Plastid
EC: 2.7.1.11
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Q9M076 | MASNGVDEQIKLVEGPAGYVLEDVPHLSDYILDLPTYPNPLQSNAAYSVVRQYFVDEDDTVQEKIVVHKDSPRGTHFRRAGPRQKVYFKPSDVRACIVTCGGLCPGLNTVIREIVCGLHFMYGVTEVIGVDCGFRGFYSKNTVALTPKTVSDIHKRGGTILGTSRGGHDTSKIVDNIQDREINQVYIIGGDGTQKGANAIYKEIRRRGLKVAVAGIPKTIDNDIPVIDKSFGFDTAVEEAQRAINAAHVEATSVENGIGIVKLMGRYSGFIAMYATLASRDVDCCLIPESPFYLEGKGGLYEFIAKRLRENGHMVIVIAEGAGQDLVAESIEQQDASGNKLLKDVGLWMSLKIKEYFAKHNVMDITLKYIDPTYMIRAIPANASDNVYSTLLAQSAVHGAMAGYTGFVSGLVNGRHTYIPFNRITERQNKVVITDRMWARMLSSTNQPSFMNPPKGTTEFTD | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 50788
Sequence Length: 462
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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P17858 | MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDGSLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQKAMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFSPVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis . Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity).
PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 85018
Sequence Length: 780
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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P30835 | MATVDLEKLRMSGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKPANWLSVSNIIQLGGTIIGSARCKAFTTREGRLAAAYNLLQHGITNLCVIGGDGSLTGANIFRNEWGSLLEELVKEGKISESTAQNYAHLSIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRHGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRVLSSKMGMEAVMALLEATPDTPACVVSLSGNQSVRLPLMECVQVTKDVQKAMDEKRFDEAIQLRGRSFENNWKIYKLLAHQKVSKEKSNFSLAILNVGAPAAGMNAAVRSAVRTGISEGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKPHLEAIVENLRTYNIHALLVIGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKANVEHMTEKMKTDIQRGLVLRNEKCHEHYTTEFLYNLYSSEGRGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWMSEKLRDVYRKGRVFANAPDSACVIGLRKKVVAFSSVTELKKETDFEHRMPREQWWLNLRLMLKMLAHYRISMADYVSGELEHVTRRTLSIDKGF | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity).
PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation (By similarity).
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 85339
Sequence Length: 780
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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P08237 | MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
PTM: GlcNAcylation decreases enzyme activity.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 85183
Sequence Length: 780
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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P06999 | MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRCIVDSSGEALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 32456
Sequence Length: 309
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
EC: 2.7.1.11
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P9WID2 | MTEPAAWDEGKPRIITLTMNPALDITTSVDVVRPTEKMRCGAPRYDPGGGGINVARIVHVLGGCSTALFPAGGSTGSLLMALLGDAGVPFRVIPIAASTRESFTVNESRTAKQYRFVLPGPSLTVAEQEQCLDELRGAAASAAFVVASGSLPPGVAADYYQRVADICRRSSTPLILDTSGGGLQHISSGVFLLKASVRELRECVGSELLTEPEQLAAAHELIDRGRAEVVVVSLGSQGALLATRHASHRFSSIPMTAVSGVGAGDAMVAAITVGLSRGWSLIKSVRLGNAAGAAMLLTPGTAACNRDDVERFFELAAEPTEVGQDQYVWHPIVNPEASP | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Can also catalyze the phosphorylation of tagatose-6-phosphate.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35401
Sequence Length: 339
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
EC: 2.7.1.11
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D9TT10 | MFNFNDKIVFDDKKYDVLTVGEMLVDMISTDYGDDFECDTYKKYFGGSPANIAINSKMLGINSIIVSSVGNDGLGKFLLKKLQEHHIEIKYVRQVDYSTSMVLVTKSKSSPTPIFYRDADYHIEYSDELKYLIENTKIVHFSSWPISRNPSRSTVEILIDECKKYDVLVCYDPNYHSMIWERGHDGREYIKSLIAKVDIIKPSEDDAERIFGKDTPENQLKKFLDLGAKLVILTLGKDGAIVSNGEETIRFNTLADEVVDTTGAGDAFWSGFYSGLIKGYTLKKSLELGFAVSAYKLRYVGAIVDLPDIDTIKSMYDLKKLR | Function: Catalyzes the ATP-dependent phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate. Together with the adjacently encoded sucrose 6'-phosphate phosphorylase, may be involved in a new pathway for the degradation of sucrose. Cannot phosphorylate D-fructose.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 36535
Sequence Length: 322
EC: 2.7.1.11
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Q4A724 | MENKFARTVLGDIPVEKLGITDCHDHFIKNGGPEVEEHIDFLMLNVDASIKEFKEFIDRGGSTIVTMDPPNVGRDVLKTLEIANAVKNLGGNVIMSTGFHKAKFYDKYSSWLAVVPTEEIVKMCVAEIEEGMDEYNYNGPVVKRSKAKAGIIKAGTGYGAIDRLELKALEVAARTSILTGCPILVHTQLGTMALEVAKHLIGFGANPDKIQISHLNKNPDKYYYEKVIKETGVTLCFDGPDRVKYYPDSLLAENIKYLVDKGLQKHITLSLDAGRILYQRNYGLTKGKQTFGLAYLFDRFLPLLKQVGVSKEAIFDILVNNPKRVLAFDEKRNFDPLKVSKEVLELKKELNLN | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the hydrolysis of D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Also able to hydrolyze carboxy 1,4-lactones.
Catalytic Activity: a 1,4-lactone + H2O = a 4-hydroxyacid + H(+)
Sequence Mass (Da): 39499
Sequence Length: 353
EC: 3.1.1.104
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Q46267 | MVMGRIHSIESMGLVDGPGIRTVVFFQGCGLRCSYCHNPDTWNMAGGKELTAEELLKKLLRFKPYFDRSGGGVTFSGGEVLLQPEFLIDILKLCKEQGIHTAIDTAGYGYGNYEEILKHTDLVLLDIKHVDDDGYKCITGKGKRGFDDFLKAVENIGVKVWIRHVIVPTLTDSKENIRKLANIIKNIRNVEKVELLPYHTLGINKYEKLNLDYKLRDIEAMDKEKRKKLEKYLKELLE | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
Catalytic Activity: glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[formate C-acetyltransferase] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence Mass (Da): 27148
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 1.97.1.4
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P9WIG3 | MSFVIAAPEVIAAAATDLASLGSSISAANAAAAANTTALMAAGADEVSTAIAALFGAHGQAYQALSAQAQAFHAQFVQALTSGGGAYAAAEAAAVSPLLDPINEFFLANTGRPLIGNGANGAPGTGANGGDGGWLIGNGGAGGSGAAGVNGGAGGNGGAGGNGGAGGLIGNGGAGGAGGVASSGIGGSGGAGGNAMLFGAGGAGGAGGGVVALTGGAGGAGGAGGNAGLLFGAAGVGGAGGFTNGSALGGAGGAGGAGGLFATGGVGGSGGAGSSGGAGGAGGAGGLFGAGGTGGHGGFADSSFGGVGGAGGAGGLFGAGGEGGSGGHSLVAGGDGGAGGNAGMLALGAAGGAGGIGGDGGTLTAGGIGGAGGAGGNAGLLFGSGGSGGAGGFGFADGGQGGPGGNAGTVFGSGGAGGNGGVGQGFAGGIGGAGGTPGLIGNGGNGGNGGASAVTGGNGGIGGTGVLIGNGGNGGSGGIGAGKAGVGGVSGLLLGLDGFNAPASTSPLHTLQQNVLNVVNEPFQTLTGRPLIGNGANGTPGTGADGGAGGWLFGNGANGTPGTGAAGGAGGWLFGNGGNGGHGATNTAATATGGAGGAGGILFGTGGNGGTGGIATGAGGIGGAGGAGGVSLLIGSGGTGGNGGNSIGVAGIGGAGGRGGDAGLLFGAAGTGGHGAAGGVPAGVGGAGGNGGLFANGGAGGAGGFNAAGGNGGNGGLFGTGGTGGAGTNFGAGGNGGNGGLFGAGGTGGAAGSGGSGITTGGGGHGGNAGLLSLGASGGAGGSGGASSLAGGAGGTGGNGALLFGFRGAGGAGGHGGAALTSIQQGGAGGAGGNGGLLFGSAGAGGAGGSGANALGAGTGGTGGDGGHAGVFGNGGDGGCRRVWRRYRRQRWCRRQRRADRQRRQRRQRRQSRGHARCRRHRRAAARRERTQRLAIAGRPATTRGVEGISCSPQMMP | Function: The arginine-rich C-terminal region protrudes from the mycobacterial membrane and mediates M.tuberculosis entry into host epithelial cells . May serve as a bridge between mycobacteria and host cells by interacting with specific host phospholipids and extracting them from host cells, for their direct integration or as a source of phosphate, during phases of TB pathogenesis when M.tuberculosis is short of phosphate supply .
PTM: A cleavage of the protein removes the N-terminal 120-150 residues, immediately upstream the PGRS domain . The exact position of the cleavage site could not be identified .
Sequence Mass (Da): 81904
Sequence Length: 957
Domain: The 77 amino acids long, arginine-rich C-terminal domain plays a critical role in tuberculosis pathogenesis . This positively charged helical domain specifically binds phosphorylated phosphatidylinositols and cardiolipin, whereas it is unable to bind other phospholipids .
Subcellular Location: Cell outer membrane
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P18384 | MIALLILSLTCSVSTYRLQGFTNAGIVAYKNIQDDNIVFSPFGYSFSMFMSLLPASGNTRIELLKTMDLRKRDLGPAFTELISGLAKLKTSKYTYTDLTYQSFVDNTVCIKPSYYQQYHRFGLYRLNFRRDAVNKINSIVERRSGMSNVVDSNMLDNNTLWAIINTIYFKGIWQYPFDITKTRNASFTNKYGTKTVPMMNVVTKLQGNTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFTDSITAAKLDYWSFQLGNKVYNLKLPKFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEKLEFNTPFVFIIRHDITGFILFMGKVESP | Function: Negatively regulates superinfection and syncytium formation in infected host cells. Acts in concert with OPG185/A56 protein at the host cell membrane by interacting with and inhibiting the mature virion entry/fusion complex (EFC). This mechanism ensures that new virions released from the cell cannot enter already infected cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42286
Sequence Length: 369
Subcellular Location: Virion membrane
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P21030 | MGGGVSVELPKRDPPPGVPTDEMLLNVDKMHDVIAPAKLLEYVHIGPLAKDKEDKVKKRYPEFRLVNTGPGGLSALLRQSYNGTAPNCCRTFNRTHYWKKDGKISDKYEEGAVLESCWPDVHDTGKCDVDLFDWCQGDTFDRNICHQWIGSAFNRSNRTVEGQQSLINLYNKMQTLCSKDASVPICESFLHHLRAHNTEDSKEMIDYILRQQSADFKQKYMRCSYPTRDKLEESLKYAEPRECWDPECSNANVNFLLTRNYNNLGLCNIVRCNTSVNNLQMDKTSSLRLSCGLSNSDRFSTVPVNRAKVVQHNIKHSFDLKLHLISLLSLLVIWILIVAI | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Unglycosylated because produced in viral factories instead of the classic ER -Golgi route.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 38786
Sequence Length: 340
Subcellular Location: Virion membrane
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P15910 | MGAAASIQTTVTTINKKISEKLEQTASASATANCDINIGNIIFKKNKGCNVLVKNMCSANASAQLDAIVSAVREVYDQLTEQQKAYAPSLLTAALNIQTNVSTITQDFETYIKQKCNSDAVINNIINVQSLEVDECSAPPGQIMTFEFINTGTATGNCAMKSVLDVLTKSSDRVSGNQSTGNDFSKYLYIIGGIICFLILLYYAKKLFFMSTNDKVKVLLAKKPDVHWTTYIDTYFRSSPVLV | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Myristoylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26519
Sequence Length: 243
Subcellular Location: Virion membrane
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P07612 | MGAAASIQTTVNTLSERISSKLEQEANASAQTKCDIEIGNFYIRQNHGCNLTVKNMCSADADAQLDAVLSAATETYSGLTPEQKAYVPAMFTAALNIQTSVNTVVRDFENYVKQTCNSSAVVDNKLKIQNVIIDECYGAPGSPTNLEFINTGSSKGNCAIKALMQLTTKATTQIAPKQVAGTGVQFYMIVIGVIILAALFMYYAKRMLFTSTNDKIKLILANKENVHWTTYMDTFFRTSPMVIATTDMQN | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Myristoylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27279
Sequence Length: 250
Subcellular Location: Virion membrane
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P0DSR7 | MITLFLILCYFILIFNIIVPAISEKMRRERAAYVNYKRLNKNFICVDDRLFSYNFTTSGIKAKVAVDNKNVPIPCSEINEVNNNKDVDTLYCDKDRDDIPGFTRSCYRAYSDLFFTT | Function: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation).
PTM: Contains two intramolecular disulfide bonds. They are created by the viral disulfide bond formation pathway, a poxvirus-specific pathway that operates on the cytoplasmic side of the MV membranes.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 13676
Sequence Length: 117
Subcellular Location: Virion membrane
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Q5AF39 | MQFSSAIILSAVAGSALATYANSTVTDIATTVVTITSCEENKCHETEVTTGVTTVTEVETTYTTYCPLPTAKAPVASTSNSTTTPPVSTAEGAAAANAVPAVAAGLLALGAFM | Function: Cell wall protein necessary for cell wall integrity. Plays only a minor role in hyphal morphogenesis and is not critical to biofilm formation.
PTM: N- and O-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 11249
Sequence Length: 113
Subcellular Location: Secreted
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Q59VW6 | MTTLSTIWLFLITITAIFQLGLSSNVTTIIDDDNNNNNNNNNNADDFLEPQIETIKVIGNKFFECESGHQFFIKGIAYQKTRQEGEIYDTTKEPHYIDPLANPFTCLRDLDYLKELGINLVRVYQIHPNANHDVCMNAFAEAGIYVLADLSEPTISIRRDYPHWDTEIFNRYQQVIDSMSNYKNLLGFFAGNEVTNCQSNIDASPFVRAAIRDCKKYINQQGYRKIPIGYASNDDANIRKNLANYFVCQLDEDEDKGQEHLNSQADFFAINVYEWCGYSTYTTSGYRDLTTMFKDYSVPVFFSEFGCNIITPRPFTEVEAIYGSTMKKVWSGGIAYEYFEEVNHYGILLTKKDGSITKLPDFDTLKMRFHAATPIGITMDEATICEPPICSNSVIDDKSSSSSSSSSFWDVALTLPPTPNEAKCECLWQSLSCVVSEDATFDEEVALRELCFKVDCEDINANGRSGKYGRYSDCNPTVRTSYALNKYYEQCGKKQEICDFQGRGELLPNRNGGLQDLENKFSSDGQNCLSLLEGKEEEKEVQEEEPDVPGLPGSNKGKEVESTPKRKGKGKSKEKEKGKLIEEEEEEEEEEEENNKTPSSGEKSPKTSKSIAGGNAITFKNDSIWKTFIEILFTCSAAILI | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 72378
Sequence Length: 641
Subcellular Location: Cell membrane
EC: 2.4.1.-
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Q5A8I6 | MKSGLLLAVILPVAFAVKKDQQSCNSSCVKVLQKQQESCPSGSDADCLCKLSDSDYWEPLTDCDCINPDKKLSASEIKVQICGAPSSSSTPTSSTETTSSTEAETTEAETTEQPSSSTSSNTESSKTTILETPSIQELNAESTTSVITPLTESAVAAVANTDTSTLIEPQNTEATPEVAPLIQPQLNNGSDLAQVSVQAFENGAGRAAVIGSGSLLALLLNFI | Function: Probable GPI-anchored cell wall protein that may be involved in cell wall organization, hyphal growth, as well as in virulence.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23182
Sequence Length: 223
Subcellular Location: Secreted
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Q5AF41 | MQFSSAVVLSAVAGSALAAYSNSTVTDIQTTVVTITSCEENKCHETEVTTGVTTVTEVDTTYTTYCPLSTTEAPAPSTATDVSTTVVTITSCEEDKCHETAVTTGVTTVTEGTTIYTTYCPLPSTEAPGPAPSTAEESKPAESSPVPTTAAESSPAKTTAAESSPAQETTPKTVAAESSSAETTAPAVSTAEAGAAANAVPVAAGLLALAALF | Function: Cell wall protein necessary for cell wall integrity. Plays only a minor role in hyphal morphogenesis and is not critical to biofilm formation.
PTM: N- and O-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21255
Sequence Length: 213
Subcellular Location: Secreted
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Q5APJ9 | MQFQTLLVVAGSLVASTLAVNSTVTEHHTTEITITHCSDNKCATSVAPAVQSVNTVTIEGVVTEYTTYCPLTASEHKHKESSSPSSVAPVASTESVVTTTISGVHTSYTTYCPLSGSSEASTVITPGTVAGESSSSSEEVSYVDVTSTPVVESTTDVELTLTAQSTLFTSYANSTGSSSSSSVVPSANVTTFEGGAVGGASNQITVGFAAIAGLAAILL | Function: Probable cell wall protein that participates directly in adhesive cell-cell interactions.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 22101
Sequence Length: 219
Subcellular Location: Secreted
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Q59UT5 | MHFIFYLILLVSAADYGNFGTYPKVPKTASINGFADPIYDLLPDCAKECVKFSTSNTPCPYWDTGCFCVMPQWAGLVGQCVAQKCKGEDVASARFLATSLCSVVGANTWMMPASISSMLSTAAGDAKEVTTIEGKTAKSWVTAPGSAAGSVVSETGSASETGSSESAQSTTTGSSSTGSSSTDSSSSSSSSPSSSANFAVLQTGGIGSVILGFMMYLLV | Function: GPI-linked hyphal surface heme-binding protein involved in heme-iron utilization . Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and form a cross-cell wall heme-transfer cascade . The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation .
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22420
Sequence Length: 219
Domain: The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens . The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (By similarity).
Subcellular Location: Secreted
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P69435 | MYSSSRKRCPKTKWALKLLTAAFLAASPAAKSAVNNAYDALIIEARKGNTQPALSWFALKSALSNNQIADWLQIALWAGQDKQVITVYNRYRHQQLPARGYAAVAVAYRNLQQWQNSLTLWQKALSLEPQNKDYQRGQILTLADAGHYDTALVKLKQLNSGAPDKANLLAEAYIYKLAGRHQDELRAMTESLPENASTQQYPTEYVQALRNNQLAAAIDDANLTPDIRADIHAELVRLSFMPTRSESERYAIADRALAQYAALEILWHDNPDRTAQYQRIQVDHLGALLTRDRYKDVISHYQRLKKTGQIIPPWGQYWVASAYLKDHQPKKAQSIMTELFYHKETIAPDLSDEELADLFYSHLESENYPGALTVTQHTINTSPPFLRLMGTPTSIPNDTWLQGHSFLSTVAKYSNDLPQAEMTARELAYNAPGNQGLRIDYASVLQARGWPRAAENELKKAEVIEPRNINLEVEQAWTALTLQEWQQAAVLTHDVVEREPQDPGVVRLKRAVDVHNLAELRIAGSTGIDAEGPDSGKHDVDLTTIVYSPPLKDNWRGFAGFGYADGQFSEGKGIVRDWLAGVEWRSRNIWLEAEYAERVFNHEHKPGARLSGWYDFNDNWRIGSQLERLSHRVPLRAMKNGVTGNSAQAYVRWYQNERRKYGVSWAFTDFSDSNQRHEVSLEGQERIWSSPYLIVDFLPSLYYEQNTEHDTPYYNPIKTFDIVPAFEASHLLWRSYENSWEQIFSAGVGASWQKHYGTDVVTQLGYGQRISWNDVIDAGATLRWEKRPYDGDREHNLYVEFDMTFRF | Function: Exports the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PGA) across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92207
Sequence Length: 807
Domain: Contains a predicted C-terminal beta-barrel porin domain and a N-terminal periplasmic superhelical domain containing tetratricopeptide repeats, which may mediate protein-protein interactions, perhaps with PgaB.
Subcellular Location: Cell outer membrane
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P75906 | MLRNGNKYLLMLVSIIMLTACISQSRTSFIPPQDRESLLAEQPWPHNGFVAISWHNVEDEAADQRFMSVRTSALREQFAWLRENGYQPVSIAQIREAHRGGKPLPEKAVVLTFDDGYQSFYTRVFPILQAFQWPAVWAPVGSWVDTPADKQVKFGDELVDREYFATWQQVREVARSRLVELASHTWNSHYGIQANATGSLLPVYVNRAYFTDHARYETAAEYRERIRLDAVKMTEYLRTKVEVNPHVFVWPYGEANGIAIEELKKLGYDMFFTLESGLANASQLDSIPRVLIANNPSLKEFAQQIITVQEKSPQRIMHIDLDYVYDENLQQMDRNIDVLIQRVKDMQISTVYLQAFADPDGDGLVKEVWFPNRLLPMKADIFSRVAWQLRTRSGVNIYAWMPVLSWDLDPTLTRVKYLPTGEKKAQIHPEQYHRLSPFDDRVRAQVGMLYEDLAGHAAFDGILFHDDALLSDYEDASAPAITAYQQAGFSGSLSEIRQNPEQFKQWARFKSRALTDFTLELSARVKAIRGPHIKTARNIFALPVIQPESEAWFAQNYADFLKSYDWTAIMAMPYLEGVAEKSADQWLIQLTNQIKNIPQAKDKSILELQAQNWQKNGQHQAISSQQLAHWMSLLQLNGVKNYGYYPDNFLHNQPEIDLIRPEFSTAWYPKND | Function: Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation promotes PGA export through the PgaA porin.
Location Topology: Lipid-anchor
Sequence Mass (Da): 77413
Sequence Length: 672
Domain: Contains a N-terminal polysaccharide deacetylase domain, and a C-terminal domain required for PGA N-deacetylation that may be involved in binding to unmodified poly-beta-1,6-GlcNAc and thereby assists catalysis by the deacetylase domain.
Subcellular Location: Cell outer membrane
EC: 3.5.1.-
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P75905 | MINRIVSFFILCLVLCIPLCVAYFHSGELMMRFVFFWPFFMSIMWIVGGVYFWVYRERHWPWGENAPAPQLKDNPSISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDRMAAQIPHLRVIHLAQNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRMWPLFFEYCLTTIWAFTCLVGFIIYAVQLAGVPLNIELTHIAATHTAGILLCTLCLLQFIVSLMIENRYEHNLTSSLFWIIWFPVIFWMLSLATTLVSFTRVMLMPKKQRARWVSPDRGILRG | Function: Probable N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homomer poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50766
Sequence Length: 441
Subcellular Location: Cell inner membrane
EC: 2.4.1.-
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P69433 | MNNLIITTRQSPVRLLVDYVATTILWTLFALFIFLFAMDLLTGYYWQSEARSRLQFYFLLAVANAVVLIVWALYNKLRFQKQQHHAAYQYTPQEYAESLAIPDELYQQLQKSHRMSVHFTSQGQIKMVVSEKALVRA | Function: Required for the synthesis of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide. May assist the glycosyltransferase PgaC in the polymerization of PGA (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16082
Sequence Length: 137
Subcellular Location: Cell inner membrane
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P91268 | MRASTACLVALLAPFYISALPVEYFYGDEQQPIEEGAENSAVFEQDRELIGLFNPSKEIGQVSGLAVNKNGHIVAFHRSGRVWDEKSFNDHETFNKDLGVINNKTIAIISREKKVIDEFGAGLFYMPHGLTIDNNGDYWVTDVGSHQVHKIDAKTQKIVMSLGEKMVPGEDQAHFCKPTDVAVAKNGHIFVADGYCNSRILKFDAKGNLMAQINAATEENQPSEFVVPHSLSLIEDMNIVCVADRENQRVQCFSAGLSEGDRTLPTGIPITSATDIGRVFAIREREHYLIGVTGNSEDVEAQMFSIDMQTGKTETFAKGVRNTHALAIAADGVMFVSQLEPSRILEIRLL | Function: Probable lyase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Mediates the dismutation of the unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the corresponding desglycine peptide amide. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity (By similarity).
Catalytic Activity: a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-terminal amide + glyoxylate
Sequence Mass (Da): 38593
Sequence Length: 350
Subcellular Location: Secreted
EC: 4.3.2.5
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P18669 | MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKAKK | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate . Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate .
PTM: Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28804
Sequence Length: 254
EC: 5.4.2.11
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P08966 | MSLAPKKTIDDAVVKGKKVLIRVDFNVPVKNGEITNDFRIRSALPTIQKVLKEGGSCILMSHLGRPKGAKMSDPKPAKSVRGYEEAATLRPVAARLSELLGQKVEFAPDCLDAASYAAKLKGGDVLLLENVRFYAEEGSKKEEERDAMAKVLAAYGDVYVSDAFGTAHRDSADMTGIPKVLGAGYAGYLMEKEINYFAQVLNNPPRPLVAIVGGAKVSDKIQLLDNMLGRINYLVIGGAMAYTFQKAQGHAIGISMCEEDKLDLAKSLLKKAQERNVEVLLPVDHVCNKEFQGVDAPLVTKDVEIPEGYMALDIGPKTIKIYEDVIAKCKSTIWNGPMGVFEMPCYSKGTFAVAKAMGNGTQKNGLMSIIGGGDTASAAELSGEAKNMSHVSTGGGASLELLEGKSLPGVTVLTNKE | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 44603
Sequence Length: 417
Domain: This cytosolic PGK lacks a C-terminal extension of 38 AA which is present in the glycosomal isoenzyme.
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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P08967 | MSLVPKKSIDDAVVKGKKVLIRVDFNVPVKNGEITNDFRIRSALPTIQKVLKEGGSCILMSHLGRPKGAKMSDPKPAKSVRGYEEAATLRPVAARLSELLGQKVEFAPDCLDAASYAAKLKGGDVLLLENVRFYAEEGSKKEEERDAMAKVLAAYGDVYVSDAFGTAHRDSADMTGIPKVLGAGYAGYLMEKEINYFAQVLNNPPRPLVAIVGGAKVSDKIQLLDNMLGRINYLVIGGAMAYTFQKAQGHAIGISMCEEDKLDLAKSLLKKAQERNVEVLLPVDHVCNKEFQGVDAPLVTKDVEIPEGYMALDIGPKTIKIYEDVIAKCKSTIWNGPMGVFEMPCYSKGTFAVAKAMGNGTQKNGLMSIIGGGDTASAAELSGEAKNMSHVSTGGGASLELLEGKSLPGVTVLTNKDAKAPAAAAAAGGDCPCGSGCAAVPAAATATVSMVLASP | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 47843
Sequence Length: 455
Domain: This glycosomal PGK has a C-terminal extension of 38 AA which is not present in the cytosolic isoenzyme. This domain most likely serves as topogenic signal to direct the glycosomal PKG to the glycosome.
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Glycosome
EC: 2.7.2.3
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P07378 | MTLNEKKSINECDLKGKKVLIRVDFNVPVKNGKITNDYRIRSALPTLKKVLTEGGSCVLMSHLGRPKGIPMAQAGKIRSTGGVPGFQQKATLKPVAKALSELLLRPVTFAPDCLNAADVVSKMSPGDVVLLENVRFYKEEGSKKAKDREAMAKILASYGDVYISDAFGTAHRDSATMTGIPKILGNGAAGYLMEKEISYFAKVLGNPPRPLVAIVGGAKVSDKIQLLDNMLQRIDYLLIGGAMAYTFLKAQGYSIGKSKCEESKLEFARSLLKKAEDRKVQVILPIDHVCHTEFKAVDSPLITEDQNIPEGHMALDIGPKTIEKYVQTIGKCKSAIWNGPMGVFEMVPYSKGTFAIAKAMGRGTHEHGLMSIIGGGDSASAAELSGEAKRMSHVSTGGGASLELLEGKTLPGVTVLDEKSAVVSYASAGTGTLSNRWSSL | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 47119
Sequence Length: 440
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Glycosome
EC: 2.7.2.3
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Q9LD57 | MASAAASSAFSLLKSTGAVASSAGTRARASLLPIPSTSVSARPLGFSATLDSRRFSLHVASKVESVRGKGSRGVVSMAKKSVGDLTSADLKGKKVFVRADLNVPLDDNQTITDDTRIRAAIPTIKYLIENGAKVILSTHLGRPKGVTPKFSLAPLVPRLSELLGIEVTKADDCIGPEVESLVASLPEGGVLLLENVRFYKEEEKNDPEFAKKLASLADLYVNDAFGTAHRAHASTEGVTKFLKPSVAGFLLQKELDYLVGAVSNPKRPFAAIVGGSKVSSKIGVIESLLEKCDILLLGGGMIFTFYKAQGLSVGSSLVEEDKLELATELLAKAKAKGVSLLLPTDVVVADKFAPDANSKIVPASGIEDGWMGLDIGPDSIKTFNEALDTTQTVIWNGPMGVFEMEKFAAGTEAIANKLAELSEKGVTTIIGGGDSVAAVEKVGVAGVMSHISTGGGASLELLEGKVLPGVIALDEAIPVTV | Function: May trigger the phosphorylation of FTSZ2-1 and FTSZ2-2.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 50112
Sequence Length: 481
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 2.7.2.3
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P80659 | ALTEQASKVALTADL | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 1531
Sequence Length: 15
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 2.7.2.3
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P36232 | AKKSVGDLTKADLEGKRVFVRADLNVPLDKEQKXTD | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 3997
Sequence Length: 36
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 2.7.2.3
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Q9SBN4 | MALSMKMRANARVVSGRRVAAVAPRVVPFSSVARPVLRSTFAPEVSIDIRRAGRSRIVVEAVKKSVGDLGKADLEGKRVFVRADLNVPLDKKTLAITDDTRIRAAVPTLKYLLDNGAKVLLTSHLGRPKGGPEDKYRLTPVVARLSELLGKEVKKVDDCIGPSVEQAVASLKSGELLLLENVRFYKEEEKNDPEFAKKLASNADLYVNDAFGTAHRAHASTEGVTKFLKPSVAGFLLQKELDYLDGAVSAPKRPFVAIVGGSKVSSKITVIEKLMEKCDKIIIGGGMIFTFYKARGLKVGSSLVEEDKLELAKNLEAIAKAKGVQLLLPSDVVVADKFDANANTQTVSVEAIPDGWMGLDIGPDSIKTFQDALADAKTVVWNGPMGVFEFPKFAVGTVAIANTLSELTPKGAITIIGGGDSVAAVEQAGVAEKMSHISTGGGASLELLEGKVLPGVAALDEK | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 49141
Sequence Length: 462
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 2.7.2.3
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P83075 | MNKKSIRNVNLKGKRVFDRV | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 2403
Sequence Length: 20
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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Q8A753 | MQTIDKFNFAGKKAFVRVDFNVPLDENFNITDDTRMRAALPTLKKILADGGSIIIGSHLGRPKGVADKFSLKHIIKHLSELLGVEVQFANDCMGEEAAVKAAALQPGEVLLLENLRFYAEEEGKPRGLAEDATDEEKAAAKKAVKESQKEFTKKLASYADCYVNDAFGTAHRAHASTALIAKYFDTDNKMFGYLMEKEVKAVDKVLNDIQRPFTAIMGGSKVSSKIEIIENLLNKVDNLIIAGGMTYTFTKAMGGKIGISICEDDKLDLALDLIKKAKEKGVNLVLAVDAKIADAFSNDANTQFCAVDEIPDGWEGLDIGPKTEEIFANVIKESKTILWNGPTGVFEFENFTHGSRTVGEAIVEATKNGAFSLVGGGDSVACVNKFGLASGVSYVSTGGGALLEAIEGKVLPGIAAINE | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 45026
Sequence Length: 419
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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B2KC44 | MQLENIKKLQDLDVKGKTVLVRVDYNVPLKDGKVDNNKRIVASEKTVKYLLDNNCKVVLMSHLGRPKGKVASEFSLAPVATEVANVFGVKVHFASDCIGEPAAKTIAEAKNGEIVLLENLRFHPEEEKNDETFAAQLAKNGEVFVQEAFGTVHRAHASTSAVTKFLNGGIGYLVQKEVQFLGDALAKPNRPFAAIIGGAKVSDKIMVLNTLLSKVNVLVIGGGMAYTFLKAQGYTTGKSLLEEDKVEEANKILATAKEKGVEILLPVDHVCSTEFSNESPVMTTENANIPEGQMGLDIGPKTIALFDKKLLECKTIFWNGPVGVFEMSNFEKGSFAIASSMVEATKLGATTIIGGGDSLNVLKKAKIKTDLLSHCSTGGGASMEFVEGKELPGLTALAK | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42784
Sequence Length: 399
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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P11977 | MSLTSKLSITDVDLKDKRVLIRVDFNVPLDKNDNTTITNPQRIVGALPTIKYAIDNGAKAVILMSHLGRPDGKKNPKYSLKPVVPKLKELLGRDVIFTEDCVGPEVEETVNKASGGQVILLENLRFHAEEEGSSKDADGNKVKADKDAVAQFRKGLTALGDIYINDAFGTAHRAHSSMVGVDLPQKASGFLVKKELEYFAKALEEPQRPFLAILGGSKVSDKIQLIDNLLPKVNSLIITGGMAFTFKKTLENVKIGSSLFDEAGSKIVGNIIEKAKKHNVKVVLPVDYVTADKFAADAKTGYATDEQGIPDGYMGLDVGEKSVESYKQTIAESKTILWNGPPGVFEMEPFAKATKATLDAAVAAVQNGATVIIGGGDTATVAAKYGAEDKISHVSTGGGASLELLEGKELPGVAALSEKSK | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 44909
Sequence Length: 421
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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Q1AUH7 | MDKRSVRDLELRGKKVLVRVDFNVPVKGGEVTDDTRIRRALPTIRYLLQRGARVALISHLGRPKGEPDPRYRMDPVARRLEELLGEPVRKLDTATGPEVGRALEELERGVILLENSRFYPGETKNDPAFAAELAGPFDLYVNDAFGAAHRAHATTVGVAERLPAAAGFLLEQELDYLDGVLRSPERPFVAILGGAKVSDKLGVIESLLGVADRLLVGGAMCFTFLKARGLGVGASLVEDDYLGEARRLMEGAADRLVLPVDVVVAERMEEGARTRTVPVEEIPEGWMGLDIGPRTVELFRRHILQARTIFWNGPMGVFEIDAFARGTEGVARAVAESGATSVVGGGDSVAAVRKLGLEDRMSHISTGGGASLEYVEGRELPGVAVLPEREEV | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42491
Sequence Length: 392
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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A4FBM5 | MKNLDDLLSEGVRGRRVLVRADLNVPLDGDRITDDGRVRASLPTIEKLTGAGARVVVTAHLGRPKGEPDPKFSLAPVAARLGELLGADVALAGDVVGESAKSAVAAQADGSVVLLENVRFDARETSKDDAERGALADELAALVGDGAAFVSDGFGVVHRKQASVYDIAKRVPGYAGGLVLSEVEVLRTLTGDPRRPYAVVLGGSKVSDKLGVIQALLPKVDKLLIGGGMAYTFLAAQGHSVGKSLLQQDQVESTCKLLEEHGDKLVLPVDVVVADRFAADAESRVVDADAIPADWMGLDIGPRSVELFAGILAGSRTVFWNGPAGVFEFPAFAEGTRGIAQAIVDSGSFSVVGGGDSAAAVRSLGLPEDGFSHISTGGGASLEYLEGKELPGVSVLEEGR | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 41410
Sequence Length: 400
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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P50317 | MGDLTIPTMDDIDIQSKKVLLRIDINSPVDENGKIIDDSRIKAHIGTIKELINKGNSVVLISHQGRPGDKDFTSLEEHAKLISKYLDREVIFVDDVIGPYAREMIKKLENNGILLLDNIRLISEELIEAPPQQHVKSFLVKKLAPLFDIYINDAFATAHRSQPSIVGFPLALPSAAGRVMEREVSALAKIFNAEDTPKIFTLGGGKVHDTIRIIENLVRKRIADRILTGGLVAELFSVAKGMNLNPKNMEILEKLGILSLIPRARKLLLSGAPIEIPVDYKVEINGNVIEEPASKVTGIIKDIGSTTAEIYSSFIKDAKVVVLRGPMGVIEDERFKSGSKSVLKASLEGQGYVIIGGGHMISALDEDMKIDSSKVHISTGGGALLLFLSGERLPALEALSMSVVNSGD | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 44396
Sequence Length: 408
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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P09404 | MAFRTLDDIGDVKGKRVLVREDLNVPMDGDRVTDDTRLRAAIPTVNELAEKGAKVLILAHFGRPKGQPNPEMSLARIKDALAGVLGRPVHFINDIKGEAAAKAVDALNPGAVALLENTRFYAGEEKNDPALAAEVAKLGDFYVNDAFSAAHRAHVSTEGLAHKLPAFAGRAMQKELEALEAALGKPTHPVAAVVGGAKVSTKLDVLTNLVSKVDHLIIGGGMANTFLAAQGVDVGKSLCEHELKDTVKGIFAAAEKTGCKIHLPSDVVVAKEFKANPPIRTIPVSDVAADEMILDVGPKAVAALTEVLKASKTLVWNGPLGAFEIEPFDKATVALAKEAAALTKAGSLISVAGGGDTVAALNHAGVAKDFSFVSTAGGAFLEWMEGKELPGVKALEA | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 41388
Sequence Length: 397
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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Q8H112 | MGSKMLFSLTSPRLFSAVSRKPSSSFSPSPPSPSSRTQWTQLSPGKSISLRRRVFLLPAKATTEQSGPVGGDNVDSNVLPYCSINKAEKKTIGEMEQEFLQALQSFYYDGKAIMSNEEFDNLKEELMWEGSSVVMLSSDEQRFLEASMAYVSGNPILNDEEYDKLKLKLKIDGSDIVSEGPRCSLRSKKVYSDLAVDYFKMLLLNVPATVVALGLFFFLDDITGFEITYIMELPEPYSFIFTWFAAVPVIVYLALSITKLIIKDFLILKGPCPNCGTENTSFFGTILSISSGGKTNTVKCTNCGTAMVYDSGSRLITLPEGSQA | Function: Ferredoxin-plastoquinone reductase involved in cyclic electron flow (CEF) around photosystem I. The homodimer is probably not involved in CEF.
PTM: Disulfide bonds; Cys-300 and Cys-303 are probably involved in the formation of disulfide bridges with 'Cys-11' and 'Cys-105' of PGR5 while Cys-272 and Cys-275 are probably involved in the binding of a Fe-containing cofactor (FCC).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35721
Sequence Length: 324
Domain: The C-terminal loop (258-324) is required for ferredoxin binding.
Subcellular Location: Plastid
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P92990 | MLKQFLLLQSFSFFLFNVVIVGGRTFGGGFSAEENPFTPKASLVRYWNKEIRGQSPRSEFLISKASPLNAVDSATFSKLAAANSLPTRFPDFCSAANLFCFPDLGASLEKHDDDVKFSVYDQKNFTNYGNARAGGADSFKNYSKDGNVVTDSFRRYSRNAAGHDDKFTVYGENSNVVEEGFNSYGTFGTGGAGDFTNYQNNVNNPTSRFTAYSDGGNGRSQTFKTYTHEANAGNGQSFTSYGKNGNGVPNEFTSYGVSSNVIGSGFSNYGESGNAANDTFTSYGSDGNVPQNNFNNYGASGNAAVDTFANYRDKANVGDDSFSSYAKDSNSEKVNFVNYGQSFNPGSETFTGYGKGAEGSKLSFKTYTPNSTFKDYAKKGVAFAKYNVSTTTANTVGDGKTVNKWIEPGKFFRESSLKEGTVIPMPDIKDKMPKRSFLPRSIITKLPFSTSKLGEIKRIFHAVENSTMGGIITDAVTECERPPSVGETKRCVGSAEDMIDFATSVLGRSVVLRTTENVAGSKEKVVIGKVNGINGGKLTKAVSCHQSLYPYLLYYCHSVPKVRVYEADLLELNSKKKINHGIAICHMDTSSWGPSHGAFLALGSKPGRIEVCHWIFENDMNWAIAD | Function: Involved in cell size determination. May serve as a chaperone for expansins through the secretory pathway.
Sequence Mass (Da): 68060
Sequence Length: 626
Domain: The BURP domain located at the C-terminus has not been identified in non-plant proteins . It is critical for PGL3's role in cell growth .
Subcellular Location: Secreted
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G5EBV6 | MEANKRQIVEVDGIKSYFFPHLAHYLASNDELLVNNIAQANKLAAFVLGATDKRPSNEEIAEMILPNDSSAYVLAAGMDVCLILGDDFRPKFDSGAEKLSQLGQAHDLAPIIDDEKKISMLARKTKLKKSNDAKILQVLLKVLGAEEAEEKFVELSELSSALDLDFDVYVLAKLLGFASEELQEEIEIIRDNVTDAFEACKPLLKKLMIEGPKIDSVDPFTQLLLTPQEESIEKAVSHIVARFEEASAVEDDESLVLKSQLGYQLIFLVVRSLADGKRDASRTIQSLMPSSVRAEVFPGLQRSVFKSAVFLASHIIQVFLGSMKSFEDWAFVGLAEDLESTWRRRAIAELLKKFRISVLEQCFSQPIPLLPQSELNNETVIENVNNALQFALWITEFYGSESEKKSLNQLQFLSPKSKNLLVDSFKKFAQGLDSKDHVNRIIESLEKSSSSEPSATAKQTTTSNGPTTVSTAAQVVTVEKMPFSRQTIPCEGTDLANVLNSAKIIGESVTVAAHDVIPEKLNAEKNDNTPSTASPVQFSSDGWDSPTKSVALPPKISTLEEEQEEDTTITKVSPQPQERTGTAWGSGDATPVPLATPVNEYKVSGFGAAPVASGFGQFASSNGTSGRGSYGGGRGGDRGGRGAYGGDRGRGGSGDGSRGYRGGDRGGRGSYGEGSRGYQGGRAGFFGGSRGGS | Function: Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate . P-granule component involved in germline development . Together with the P-granule component pgl-1, is involved in the formation of P-granules . Together with pgl-1, probably recruits other granule components such as pos-1, mex-3 and glh-1, and RNA to P-granules . In vitro, binds mRNA; this interaction is required for the formation of liquid-like droplets that resemble P-granules . Most likely recruits pgl-1 into P-granules during autophagy . Associates with adapters such as sepa-1 and is required for the accumulation and degradation of P-granules by autophagy in somatic cells . This ensures exclusive localization of the P-granules in germ cells . In addition, may act redundantly with pgl-1 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms . This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis . May protect somatic cells from excessive apoptosis during normal development .
PTM: Methylated at arginine residues in the RNA-binding RGG-box by prmt-1. Methylation promotes P-granule degradation by autophagy.
Catalytic Activity: [RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment].
Sequence Mass (Da): 74845
Sequence Length: 693
Domain: The dimerization domain also acts as a hinge; changes in its structure probably impact oligomerization and RNA-binding.
Subcellular Location: Cytoplasmic granule
EC: 4.6.1.24
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Q0P9C9 | MRIGFLSHAGASIYHFRMPIIKALKDRKDEVFVIVPQDEYTQKLRDLGLKVIVYEFSRASLNPFVVLKNFFYLAKVLKNLNLDFIQSAAHKSNTFGILAAKWAKIPYRFALVEGLGSFYIDQGFKANLVRFVINSLYKLSFKFAHQFIFVNESNAEFMRNLGLKENKICVIKSVGINLKKFFPIYVESEKKELFWKNLNIDKKPIVLMIARALWHKGVKEFYESATMLKDKANFVLVGGRDENPSCASLEFLNSGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIVVSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQYDENIIAQRYLKLYDRVIKNV | Function: Adds the first GalNAc residue on to the isoprenoid-linked bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucose) carrier in the N-linked protein glycosylation pathway. Acts first on the undecaprenylpyrophosphate-linked bacillosamine (Und-PP-Bac) substrate to yield the disaccharide.
Catalytic Activity: N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-galactosamine = H(+) + N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP
Sequence Mass (Da): 42816
Sequence Length: 376
Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.290
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B9KDD4 | MKLQQNFTDNNSIKYTCILILIAFAFSVLCRLYWVAWASEFYEFFFNDQLMITTNDGYAFAEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFESIILYMSAFFASLIVVPIILIAREYKLTTYGFIAALLGSIANSYYNRTMSGYYDTDMLVLVLPMLILLTFIRLTINKDIFTLLLSPVFIMIYLWWYPSSYSLNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAWQYKLALIVLLFAIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDVQNLKDAAFMYFNVNETIMEVNTIDPEVFMQRISSSVLVFILSFIGFILLCKDHKSMLLALPMLALGFMALRAGLRFTIYAVPVMALGFGYFLYAFFNFLEKKQIKLSLRNKNILLILIAFFSISPALMHIYYYKSSTVFTSYEASILNDLKNKAQREDYVVAWWDYGYPIRYYSDVKTLIDGGKHLGKDNFFSSFVLSKEQIPAANMARLSVEYTEKSFKENYPDVLKAMVKDYNKTSAKDFLESLNDKDFKFDTNKTRDVYIYMPYRMLRIMPVVAQFANTNPDNGEQEKSLFFSQANAIAQDKTTGSVMLDNGVEIINDFRALKVEGASIPLKAFVDIESITNGKFYYNEIDSKAQIYLLFLREYKSFVILDESLYNSSYIQMFLLNQYDQDLFEQITNDTRAKIYRLKR | Function: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in eubacteria, where Bac(NAc)(2) is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.
Catalytic Activity: tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82729
Sequence Length: 712
Domain: Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell inner membrane
EC: 2.4.99.19
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Q0P9D0 | MYEKVFKRIFDFILALVLLVLFSPVILITALLLKITQGSVIFTQNRPGLDEKIFKIYKFKTMSDERDEKGELLSDELRLKAFGKIVRSLSLDELLQLFNVLKGDMSFVGPRPLLVEYLPLYNKEQKLRHKVRPGITGWAQVNGRNAISWQKKFELDVYYVKNISFLLDLKIMFLTALKVLKRSGVSKEGHVTTEKFNGKN | Function: Glycosyl-1-phosphate transferase that mediates the first step in the biosynthesis of the undecaprenyl-linked heptasaccharide donor in the N-linked protein glycosylation pathway. Catalyzes the linking of uridine 5'-diphosphobacillosamine (UDP-Bac) to undecaprenyl phosphate to create the first membrane-associated intermediate undecaprenylpyrophosphate-linked Bac (Und-PP-Bac).
Catalytic Activity: tri-trans,hepta-cis-undecaprenyl phosphate + UDP-N,N'-diacetylbacillosamine = N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UMP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23144
Sequence Length: 200
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
EC: 2.7.8.36
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Q0P9D1 | MARTEKIYIYGASGHGLVCEDVAKNMGYKECIFLDDFKGMKFESTLPKYDFFIAIGNNEIRKKIYQKISENGFKIVNLIHKSALISPSAIVEENAGILIMPYVVINAKAKIEKGVILNTSSVIEHECVIGEFSHVSVGAKCAGNVKIGKNCFLGINSCVLPNLSLADDSILGGGATLVKNQDEKGVFVGVPAKRM | Function: Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.
Catalytic Activity: acetyl-CoA + UDP-N-acetylbacillosamine = CoA + H(+) + UDP-N,N'-diacetylbacillosamine
Sequence Mass (Da): 21148
Sequence Length: 195
Pathway: Protein modification; protein glycosylation.
EC: 2.3.1.203
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Q0P9D3 | MRFFLSPPHMGGNELKYIEEVFKSNYIAPLGEFVNRFEQSVKAYSKSENALALNSATAALHLALRVAGVKQDDIVLASSFTFIASVAPICYLKAKPVFIDCDETYNIDVDLLKLAIKECEKKPKALILTHLYGNAAKMDEIVEICKENEIVLIEDAAEALGSFYKNKALGTFGEFGAYSYNGNKIITTSGGGMLIGKNKEKIEKARFYSTQARENCLHYEHLDYGYNYRLSNVLGAIGVAQMEVLEQRVLKKREIYEWYKEFLGECFSFLDELENSRSNRWLSTALIDFDKNELNSCQKDINISQKNITLHPKISKLIEDLKNEQIETRPLWKAMHAQEVFKGAKAYLNGNSELFFQKGICLPSGTAMSKDDVYEISKLILKSIKA | Function: Aminotransferase involved in the bacillosamine biosynthesis pathway by producing UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc (UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose), a precursor used in the production of the glycan component 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose. Required for host colonization and virulence. Involved in the N-linked protein glycosylation pathway.
Catalytic Activity: 2-oxoglutarate + UDP-N-acetylbacillosamine = L-glutamate + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose
Sequence Mass (Da): 43654
Sequence Length: 386
Pathway: Protein modification; protein glycosylation.
EC: 2.6.1.34
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Q0P9D4 | MIFYKSKRLAFFLTSDIVLILLSVYLAFSLRFSGDIPSIFYHGMMVSAIILLVLKLSFLFVFRIYKVAWRFFSLNEARKIFIALLLAEFCFFLIFYFFSDFFNPFPRSAIVIDFVLSYMFIGTLRISKRMLVDFKPSRMKEEETPCIVVGATSKALHLLKGAKEGSLGLFPVGVVDARKELIGTYCDKFIVEEKEKIKSYVEQGVKTAIIALRLEQEELKKLFEELVAYGICDVKIFSFTRNEARDISIEDLLARKPKDLDDSAVAAFLKDKVVLVSGAGGTIGSELCKQCIKFGAKHLIMVDHSEYNLYKINDDLNLYKEKITPILLSILDKQSLDEVLKTYKPELILHAAAYKHVPLCEQNPHSAVINNILGTKILCDSAKENKVAKFVMISTDKAVRPTNIMGCTKRVCELYTLSMSDENFEVACVRFGNVLGSSGSVIPKFKAQIANNEPLTLTHPDIVRYFMLVAEAVQLVLQAGAIAKGGELFVLDMGKPVKIIDLAKKMLLLSNRNDLEIKITGLRKGEKLYEELLIDENDAKTQYESIFVAKNEKVDLDWLNKEIENLQICEDISEALLKIVPEFKHNKEGV | Function: C6 dehydratase involved in the bacillosamine biosynthesis pathway by generating UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose from UDP-N-acetyl-alpha-D-glucosamine. Involved in the N-linked protein glycosylation pathway.
Catalytic Activity: UDP-N-acetyl-alpha-D-glucosamine = H2O + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66766
Sequence Length: 590
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
EC: 4.2.1.135
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Q6KZ42 | MFMTKDLFFVYIFTTMIKLVVLDVDGTLTDKSRMISVNAVNAIRNLKTKVALVSGNVLPVLYGLKIYIGFDGYIFAENGGIALINNNIEKFFEKDGPESFLNDISGYTSARGILTNRWRETSMAFTANHDEMDIIDREAASRDLYIVDSGFTLHILNKGQDKGFAVKKMIDIMNIDYNNVLVIGDSQNDESMFSLGTLSACPGNASEKIKEMSNYVSGKCYGDELFDVFRHFDLIH | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 26486
Sequence Length: 236
EC: 3.1.3.18
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Q8ZT04 | MACKVLVVDLDGTLTLGRNTYELSAEALLALRRARDAGIRVVLATANGLDFALTVARYLGIRDVIAENGCLVHLDGVTYELCSGDMAEVDRLVLSTGVVKPSHQNKCRKYDLAYIPLREDAVERLRDVLGPGYVVESSGYAIHVRPAGVDKGTAVKWLCQRLGVPCFQVASVGDSDVDVGMLSVSWGFAVGNATPAAKKAAKVVVDGPSGIGFKEAVEIILSGGACAP | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 24032
Sequence Length: 228
EC: 3.1.3.18
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O50129 | MKIKAISIDIDGTITYPNRMIHEKALEAIRRAESLGIPIMLVTGNTVQFAEAASILIGTSGPVVAEDGGAISYKKKRIFLASMDEEWILWNEIRKRFPNARTSYTMPDRRAGLVIMRETINVETVREIINELNLNLVAVDSGFAIHVKKPWINKGSGIEKASEFLGIKPKEVAHVGDGENDLDAFKVVGYKVAVAQAPKILKENADYVTKKEYGEGGAEAIYHILEKFGYL | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate (By similarity). Has phosphatase activity towards p-nitrophenylphosphate (in vitro).
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 25606
Sequence Length: 231
EC: 3.1.3.18
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A3DNN7 | MIRLAAFDIDGTLTINRSSTVLCLEAIDALRKLEKNGVIVVLVSSNALPVVVGLKKYIGLSGPAIGETGALIYYGEEEIVATTKYSAKQAYLDVLEKYNEYVYGSWQNMFRLHDYALKIRKQYLSKDNEIYSLIKEYVENKYPYIKVGYSGYAIHLTPKDTGKGKALKQIMEKHGIRREETMGVGDSIMDWEFIKETKIKVAVANADPELRRKADIVTTKPSGYGVVEIVEKILDKPP | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 26765
Sequence Length: 238
EC: 3.1.3.18
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Q96YM5 | MVLSDFDRTLSDEKDNFIIKQEVVEVVNKFSAKFLFFVVTGRERKYMDILAKGLFPTGWIIENGGIIILRDKEIKLVDEKWYKIRKNLAKILDKNGIKYSLGEVIIYVNSAIDYKDKLDKINEAKIEWNRSDAMIMPKNVSKGEAVKILKSILNFEGVTIAIGDSQNDISLFSVADIKVAVANALPEIKAISDIVLDKEDGIGVMRFLEKILNDGSYLEKLIGFRK | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 25654
Sequence Length: 226
EC: 3.1.3.18
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Q9HLQ2 | MIRLAAIDVDGTLTDRDRLISTKAIESIRSAEKKGLTVSLLSGNVIPVVYALKIFLGINGPVFGENGGIMFDNDGSIKKFFSNEGTNKFLEEMSKRTSMRSILTNRWREASTGFDIDPEDVDYVRKEAESRGFVIFYSGYSWHLMNRGEDKAFAVNKLKEMYSLEYDEILVIGDSNNDMPMFQLPVRKACPANATDNIKAVSDFVSDYSYGEEIGQIFKHFELM | Cofactor: Binds 5 Mg(2+) ions per homodimer.
Function: Catalyzes the dephosphorylation of 2-phosphoglycolate. Also has significant, but less efficient, pyrophosphatase activity, since it is able to catalyze the release of phosphate from inorganic pyrophosphate (PPi).
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 25279
Sequence Length: 224
EC: 3.1.3.18
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Q9SL05 | MAAASISAIGCNQTLIGTSFYGGWGSSISGEDYQTMLSKTVAPPQQARVSRKAIRAVPMMKNVNEGKGLFAPLVVVTRNLVGKKRFNQLRGKAIALHSQVITEFCKSIGADAKQRQGLIRLAKKNGERLGFLA | Function: Involved in the regulation of the cyclic electron flow (CEF) around Photosystem I. Essential for the reduction of PGRL1A by ferredoxin and for photoprotection. Contributes to maximize photosynthesis efficiency after a long dark adaptation via the regulation of non-photochemical quenching (NPQ) .
PTM: Disulfide bonds; Cys-11 and Cys-105 are probably involved in the formation of disulfide bridges with 'Cys-300' and 'Cys-303' of PGRL1A. 'Cys-272' and 'Cys-275' of PGRL1A may also be used to form the disulfide bridges, but in this case the cyclic electron flow is lost.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14293
Sequence Length: 133
Subcellular Location: Plastid
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Q17QC0 | MAAEDVAATGADTSELESGGLLQEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKDGEEPTVYSDKEEPKDESTRKND | Function: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21622
Sequence Length: 194
Domain: The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 106 and 130.
Subcellular Location: Microsome membrane
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Q70PY2 | MNTSTAISFVAALVLCCLALSANALQIEPRSSWGAVSARSPSRISGAVDYVIIHHSDNPNGCSTSEQCKRMIKNIQSDHKGRRNFSDIGYNFIVAGDGKVYEGRGFGLQGSHSPNYNRKSIGIVFIGNFERSAPSAQMLQNAKDLIELAKQRGYLKDNYTLFGHRQTKATSCPGDALYNEIKTWPHWRQN | Function: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN), preferentially DAP-type PGNs. Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 20998
Sequence Length: 190
Subcellular Location: Secreted
EC: 3.5.1.28
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Q9VV96 | MKLQLALVLCGLTLALGQIVPRSSWCPVPISPRMPRLMVPVRLIIIHHTVTAPCFNPHQCQLVLRQIRADHMRRKFRDIGYNFLIGGDGRIYEGLGFGIRGEHAPRYNSQSIGIAFIGNFQTGLPPSQMLQAARTLIQIAVQRRQVSPNYSVVGHCQTKATACPGIHLLNELKKWPNWRPKP | Function: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity (By similarity).
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 20459
Sequence Length: 182
Subcellular Location: Secreted
EC: 3.5.1.28
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Q9V4X2 | MANKALILLAVLFCAQAVLGVTIISKSEWGGRSATSKTSLANYLSYAVIHHTAGNYCSTKAACITQLQNIQAYHMDSLGWADIGYNFLIGGDGNVYEGRGWNVMGAHATNWNSKSIGISFLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQVGSTECPGTNIWNEIRTWSNWKA | Function: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity (By similarity).
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 19829
Sequence Length: 184
Subcellular Location: Secreted
EC: 3.5.1.28
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Q8W405 | MVSSKQTQLKKGKQPSWIEMYLPKEVRPYAHLARLDKPIGSWLLAWPAFWSVALAADLESLPKMLAIFGWWAVWIRGAGCTINDYFDRNFDKKVERTKSRPLASGAVSPAQGLWWLAFQLFIGLGVLYQFNVLTLALAIVHVPFVFAYPLMKRITYWPQAFLGVMISWGALLGSSALKGSVVPSIAYPLYISSFFWTLVYDTIYAHQDKVDDAKAGIKSTALRFGDATKMWISWFGVGCIAALVIGGLILNIGLPYYVFVAIATGQLVWQIFTVDLLSPLDCGKKFVSNQWFGAIIFTGILLGRLFP | Function: Prenyltransferase involved in the biosynthesis of shikonin, a naphthoquinone secondary metabolite. Could accept only geranyl diphosphate and not dimethylallyl diphosphate, farnesyl diphosphate, or geranylgeranyl diphosphate as substrate.
Catalytic Activity: (2E)-geranyl diphosphate + 4-hydroxybenzoate = 3-geranyl-4-hydroxybenzoate + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34319
Sequence Length: 307
Domain: The N-terminus (1-130) is determinant for the chain length specificity. Region I (76-96) and region III (201-229) are involved in the recognition of both substrates in a coordinated manner.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.5.1.93
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O14031 | MTARNSASIPTSIRKTSENEVSGDETPAGVGNLSTKTASKTSLTFRQSSSDESTSSYSGNHHNINIQHHPNRPFRTNSSSFSPNDYSISESPSKSKKDGVHVSAVQLDNETDSEVESEVEELERELEAIEDSVYPEVRAAVNPTDDVNLPVNTWRTWVLTTIFVIVFAAVNQFFSLRYPALSISFIVAQLILFPLGKLLNLLPNWKIGYGRFSFYLNSSPFNVKEHAAITIAVSLTSSTAYATNILSAQTSFYKQNLSWGYKILIVLTSQMLGYGFAGLTRRWIVYPAAMIWPQTLVSTVLFRTLHGNSGNDIGVLKNNRISANGWTISRYRFFAYVMIGSFVFYWFPGFIFKGLSYFTVLCWIWPKNRVVNQLFGYNSGLGILPLTFDWQQVVYNSNPLASPWWVICNTFGSVVLIFWIVVPILYYKGVWFSNYLPMLSSSTFDHTGVSYNSSRVLNSDYSFNHTKYESYSPLYMPMSYSMSTALNFAAVTAIFTHCALYNGKDIWQRLWKESGKDECIHRKLMRNYKEAPQWWYATLFIVVFGLTIFTVRYYDTQCPVWALIVALLIFIVNFIPQGVLEGITNQHVGLNIITELIGGYILPGKPLANLMIKLYGFIPMRQGLEFSRDLKLAQYMKIPPRILFFVQLFATILGGITQVAVQEWMNYHIPGICTTSQSNGFTCPNGRSIYNASLIWGAIGPAKMFSKGKPYYPLIFFFLIGAVAPFITWGLRKRFPKSWIGKLNAPVLFTGPGNIPPATGINYSSWAIVGFIFNYVIRKRAIHWWRKYNYVLAAAMDSGVAVAGVVIFLCVSYPGGKITWWGNTVYTKTYDWKSVPYRSLGPNETFGYTNW | Function: High-affinity glutathione transporter which plays a role in scavenging glutathione from the extracellular environment for the maintenance of sulfur homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96302
Sequence Length: 851
Subcellular Location: Endoplasmic reticulum membrane
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Q8VYB7 | MHGRPRNASKPEEEAASAAKAVQLRSLQSQFMTNHHDKIYTNEAIELSTKLLEINPEAYTAWNYRKLAVEDRLARIEPDPNLVSAILDEELRVVESALRQNFKSYGAWHHRKWVLSKGHSSVGNELRLLEKFQKLDSRNFHAWNYRRFVVELTNRSEQDELQYTDDMINNNFSNYSAWHNRSVLLSSLLAQNADGFMPNIKIPEEYDFVHSAIFTEPDDQSGWFYHLWLLDQTLNVETPLLTSSWPSHGSSIILSGAGCLSGSSSMFTTFCSESGSFPLILYFDQAVGGVSSSTVTIDSELKGNEGLVWEPIPNKNSQVSCVWVARLKYVSSDPCEYKVKIRVGNSPGIVSSRGYNFNAPYEFVFTAHVHDTVEDSQEGIVSWTDGFDIWDAKSKDLNSLVTLDRLNAEMDFKWRQEAIDSEVECFGILPDSKIGKLTLARLLMAREAMVSDDAVKGVHYEEILQLYNDLMALDSSHYQYYKDEHSKAFLHKVTSSSESLSRHLLRYRDMNNLVCLRLNNLSLSRIASVEKLLFVQMLDLSHNELHSTEGLEAMQLLSCLNLSHNRIRSFSALDSLRHVKQLKVLDVSHNHIGKHSVDTTRYLCSSPLSNSELGQDDVGKQNPGLVTKYWDAYCVLTDLNLKQLDIAGNEIAGEEFSSFVLQVVPKLVWLDGQKKLGN | Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -CCXX, CXXX, -XCCX and -XCXC, such as RABA1A, RABA2A, RABF2A and RABG2 . In vitro, can prenylate PGGTI targets with the C-terminal Cys-aliphatic-aliphatic-X (CaaX) with leucine in the terminal position. Substrates with the C-terminal sequence -CSIL such as ARAC11/ROP1 or GG2/AGG2 are prenylated independently of REP and when the alpha subunit is associated with a beta subunit (RGTB1 or RGTB2) .
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 76909
Sequence Length: 678
EC: 2.5.1.60
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Q9FJ32 | MHGRKREEDPNPEETAAKALELRSLQSQFMSNHHQKIYTKEAIQLSAKLLITNPEFYTAWNYPKLAFESRLDEDSDPSLVNSIIDEELGVVQNALERNVKSYGAWYHRKWVLSKKGHYYPSLENELQLLNDYQKQAHQKQDDEKQDDPSRNFHAWNYRRFVVELTKTSEEDELQYTTDMISDISFTIYSAWHYRSVLVSSLVAKKADGFMPKETIRRELDYVHSAIFTLEEKQSGWFYYLWLLDQTVKMEIPLRFSSWPSDGSIIILSGPDCFNASSSTTKLTTFCSESGSFPLILYFDQAVSGVSSSTVTIGSELKDLVWEPVSDKKNSQVDSCVWVARLKFDCREPCFSRKETKVKVSLGGIVSSMGCNLTAPYEFVFTLRIHDTVEVELSQQESIVSWTDGFDNWDDNALSNDLNSLTALNADTGFEWRKKAIKIEIELFRTLPDSKIGKLILARLLMAEETMISNGVHYKEILQLYNDLMALDSWHNQYYKDEHSVALIHKVTSRTESMSRHLFRYRNMNNIICLRLNNLTLSRIAAVEKLLFVQMLDLSHNELHSAEGLEAMQLLCCLNLSHNRIRSFSALDSLRHLKQLRVLDVSHNHICGELPVDTTRYLCSSPLSNSGETGREVPNKYQDAYLVLRDLMKLKQLDIRGNDLIFAGEEFSSFVRQVVPKLVWLDGHKLTS | Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -CCXX, CXXX, -XCCX and -XCXC, such as RABA1A, RABA2A, RABF2A and RABG2 (By similarity). Does not seem to be a functional Rab-GGT alpha subunit in vitro .
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 79141
Sequence Length: 687
EC: 2.5.1.60
|
O93829 | MQHGIKRVKLSEEAKRLKLEKDQIKIKNYRQLTDEIFELRANENYSDEALIKTNELLIINPEFYTIWNYRREILINNYSSSNDKDDQIYEDILNQDLNFVLVQLKKFPKCYWIWNHRRWLLFELVKLGKVNWKYEFGVVSKLLDLDQRNFHGWHYRRFVVKNMELECKNDTTLILKINLDEFNYTTLKIQKDFSNFSAWHNRTKLIPKIYNLIQQQQQQQQKDGKIFGDLPGIELFQNPILLLKNDLEMIKTGVYMSPEDTSVWLYLYWLLTDDLFTNAFKSHQQDYMNILHEQLQLINEVNEMEKEDTGQDNVGCLKSMIFINALIQNENNKPVLTEQVKSCLKQLAKIDPLRKNKYLDQLAGNAPIFHH | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4 (By similarity).
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 44462
Sequence Length: 371
EC: 2.5.1.60
|
Q55DQ4 | MHGVLKVRTSEEKAKAQRLKELEKIESYNKLVKSFEELREKQNGRYDEISLSVSKLVLIENPEFYTIWNYRRLAILQFTETKENSELQVIYQNEMKFLEECIQRFTKSYWIWFHRQWIALRMDNCDWEREMKLCTKLLNFDLRNFHCWGHRRFILKHSNIKLEDELKYTTEKVEQNFSNYSAWHQRSSILPKIYKEPEQLLEKILEEFELVRNAVYTEPKDSSSWIYHKWLVATIKSIPNSNYIEVLKNELTQIYDLIELEPDCKWPIYTTLLLKIEIGGFEKQELLDIISQLIKLDPDHKNYYKSLETKI | Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to proteins with a C-terminal sequence motif -XCC or -XCXC, where both cysteines may become modified.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 37779
Sequence Length: 311
EC: 2.5.1.60
|
Q92696 | MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQKSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLGRLPEPNWTRELELCARFLEVDERNFHCWDYRRFVATQAAVPPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPEDVLLKELELVQNAFFTDPNDQSAWFYHRWLLGRADPQDALRCLHVSRDEACLTVSFSRPLLVGSRMEILLLMVDDSPLIVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTAGDVQKECVLLKGRQEGWCRDSTTDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFQTLKAVDPMRATYLDDLRSKFLLENSVLKMEYAEVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESLDGVTNLPRLQELLLCNNRLQQPAVLQPLASCPRLVLLNLQGNPLCQAVGILEQLAELLPSVSSVLT | Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 65072
Sequence Length: 567
EC: 2.5.1.60
|
Q3MHI4 | MAQEAGDMDDGQVSDSDSDMTVAPSDRPLPVPKALGGDCGLRPFQSTATACAPASHYRTVKSVDSSEESFSDSDDDSSVWKRKRQKCFNTPPKPEPFQFDQSSQKPPIAGRKKVNNIWSAVLQEQNQDAVATELGILGMEGTIDRSRQSETYNYLLAKKLKRESQEHTKELDKELEEYMHGGKKTGPKEEENGQGHPKRKRPVKDRVGDRLEMNYKGRYEITEDDSQERVADEISFRLQEPKKDLIARVVRIIGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYLENQKEYENKKAARKRRIQVMGKKMKQAIKNLNFQEDDDTSRETFASDTNEALASLDESQEGHGETKLDAEEAIEVDHSHDLDMF | Function: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner. Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA (By similarity).
PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm.
Sequence Mass (Da): 44578
Sequence Length: 394
Subcellular Location: Nucleus
|
Q9H814 | MALEVGDMEDGQLSDSDSDMTVAPSDRPLQLPKVLGGDSAMRAFQNTATACAPVSHYRAVESVDSSEESFSDSDDDSCLWKRKRQKCFNPPPKPEPFQFGQSSQKPPVAGGKKINNIWGAVLQEQNQDAVATELGILGMEGTIDRSRQSETYNYLLAKKLRKESQEHTKDLDKELDEYMHGGKKMGSKEEENGQGHLKRKRPVKDRLGNRPEMNYKGRYEITAEDSQEKVADEISFRLQEPKKDLIARVVRIIGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYIENQKEYENKKAARKRRTQVLGKKMKQAIKSLNFQEDDDTSRETFASDTNEALASLDESQEGHAEAKLEAEEAIEVDHSHDLDIF | Function: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA.
PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm (By similarity).
Sequence Mass (Da): 44403
Sequence Length: 394
Subcellular Location: Nucleus
|
Q9JJT9 | MALEAGDMEEGQLSDSDSDMTVVPSDRPLQMAKVLGGGSAACAPVSHYRTVKHVDSSEESLDSDDDCSLWKRKRQKCHNTPPKPEPFPFGPSGQKTALNGGKKVNNIWGAVLQEQNQDAVATELGILGMEGSIDRSRQSETYNYLLAKKLAKKESQEYTKELDKDLDEYMHGDKKPGSKEDENGQGHLKRKRPVRDRLGNRVEMNYKGRYEITEEDAPEKVADEIAFRLQEPKKDLIARVVRILGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYVENQKEYENKKAARKRRTQLLGKKMKQAIKSLNFQEDDDTSRETFASDTNEALASLDEAQEGPGETKLDAEEAIEVDHPQDLDIF | Function: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner. Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA (By similarity).
PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm.
Sequence Mass (Da): 43247
Sequence Length: 385
Subcellular Location: Nucleus
|
Q63068 | MALEAGDMEEGQLSDSDSDMTVVPSDRPLQMAKVLGGGGAACAPVSNYRTVKHVDSSEESLDSDDDCSLWKRKRQKCHSPPPKPEPFPFGQSGQKPALNGGKKVNNIWGAVLQEQNQDAVATELGILGMEGTIDRSRQSETYNYLLAKKLAKKESQEYTKELDKDLDEYMHGDKKPGSKEEENGQGHLKRKRPVRDRLGNRVEMNYKGRYDITEEDSPEKVADEIAFRLQEPKKDLIARVVTILGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYIENQKEYENKKAARKRRTQLLGKKMKEAIKSLNFQEDDDTSRETFASDTNEALASLDEAQEGPGETKLDAEDAIEVDHPQDLDIF | Function: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner. Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA (By similarity).
PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm.
Sequence Mass (Da): 43166
Sequence Length: 385
Subcellular Location: Nucleus
|
Q51718 | MPLRTLLCGLLLAVCLGQHALAASRCSERPRTLLRPAEVSCSYQSTWLDSGLVGQRKIIYQTPLGTPPAGGWPVVLIYQGSFFPLNDFSYHSNLPFGGYYEGKLVQNLLDHGYAVIAPSAPADLFWQTNIPGLAQAYELSTDYDFLGNVLAAIASGHFGPLNAQRQYATGISSGGYNTSRMAVSFPGKFRALAVQSGSYATCSGPLCVVPDQLPADHPPTLFLHGFVDAVVPWWSMDLYYDRLLHQGIETARYTEPLGGHEWFAASPGKVLAWFNAHP | Function: Hydrolysis of poly(3-hydroxyoctanoic acid).
Catalytic Activity: Hydrolyzes the polyester poly{oxycarbonyl[(R)-2-pentylethylene]} to oligomers.
Sequence Mass (Da): 30267
Sequence Length: 278
Subcellular Location: Secreted
EC: 3.1.1.76
|
B2NHN2 | MFDSVKIAWLVALGAAQVAATALPAFNVNPNSVSVSGLSSGGYMAAQLGVAYSDVFNVGFGVFAGGPYDCARNQYYTSCMYNGYPSITTPTANMKSWSGNQIASVANLGQRKIYMWTGSSDTTVGPNVMNQLKAQLGNFDNSANVSYVTTTGAVHTFPTDFNGAGDNSCSLSTSPYISNCNYDGAGAALKWIYGSLNARNTGTLSGSVLSFAQSGSYGANGMDTTGYLYVPQSCASGATVCSLHVALHGCLQSYSSIGSRFIQNTGYNKWADTNNMIILYPQAIPDYTIHAIWNGGVLSNPNGCWDWVGWYGSNADQIGGVQMAAIVGQVKQIVSGFQG | Function: Esterase involved in the hydrolysis of polyhydroxybutyrate, a microbial polyester that can be produced from renewable resources.
Catalytic Activity: [(3R)-hydroxybutanoate](n) + H2O = (R)-3-hydroxybutanoate + [(3R)-hydroxybutanoate](n-1) + H(+)
Sequence Mass (Da): 35613
Sequence Length: 339
Subcellular Location: Secreted
EC: 3.1.1.75
|
O49460 | MNNVKVPKIPGGGAISTLLKVGIIGGLGLYGATHSLYNVEGGHRAIMFNRLVGIKDKVYPEGTHLMIPWFERPVIYDVRARPYLVESTSGSRDLQMVKIGLRVLTRPMADQLPEIYRSLGENYSERVLPSIINETLKAVVAQYNASQLITQREAVSREIRKILTERAANFNVALDDVSITNLTFGKEFTAAIEAKQVAAQEAERAKFIVEKAEQDKRSAVIRAQGEAKSAQLIGQAIANNQAFITLRKIEAAREIAQTIANSANKVYLSSDDLLLNLQGMNLDVDAKN | Function: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31706
Sequence Length: 288
Subcellular Location: Mitochondrion inner membrane
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Q44104 | MSRIAYFGPVGTFTEQAARTFMAAGDELVAAETIPKALDAVRRGEADAACVPVENSVEGAVPATLDSLAVGEPLIGVAEALLPVHFSVLTRDDVGEIRTVASHPHALAQVRKWLEDNLPGARVVAAGSTAAAAVAVQAGEFDAAVTAPVAVEHYPLKVLATEVADVRDARTRFLLMRRPPVVLPEPTGADRTSIVAAAANRTGTLAELLTELATRGINLTRLDARPHKQNFGEYRFFIDFEGHVAEPRIADALAALRRRCRDVRFLGSFARADGVAATIEPAARNEDFTDAADWVAAVQRGEQA | Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 32321
Sequence Length: 304
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
|
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