ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P27695 | MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endo... |
Q9UBZ4 | MLRVVSWNINGIRRPLQGVANQEPSNCAAVAVGRILDELDADIVCLQETKVTRDALTEPLAIVEGYNSYFSFSRNRSGYSGVATFCKDNATPVAAEEGLSGLFATQNGDVGCYGNMDEFTQEELRALDSEGRALLTQHKIRTWEGKEKTLTLINVYCPHADPGRPERLVFKMRFYRLLQIRAEALLAAGSHVIILGDLNTAHRPIDHWDAVNLECFEEDPGRKWMDSLLSNLGCQSASHVGPFIDSYRCFQPKQEGAFTCWSAVTGARHLNYGSRLDYVLGDRTLVIDTFQASFLLPEVMGSDHCPVGAVLSVSSVPAKQ... | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents . Initiates repair of AP sites in DNA by catalyzing hydrolytic inci... |
Q6DDT4 | MKIVSWNINGIRATRVGLKETLDSLDADIICLQETKVTRDLLDEPSAIVEGYNSYFSFSRVRSGYSGVATFCKSSTTPQAAEEGLSGVFCNRTGSVGCYGNTEQFLEEELQSLDQEGRAVLTQHRILNCEDKEETLTVINVYCPRADPEKPERKTYKLRFYHLLQTRAEAILQNGGHVIILGDVNTSHRPLDHCDPTDLETFEENPGRQWLNQFLGDPIPSQKGDSETVMPPSAGSGLFYDSFRYFHPTQKNAFTCWCSASGARQTNYGTRIDYILGNRELVESEFLDSVIMPEVEGSDHCPVKAFMKCQPIAANKCPPL... | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents . Initiates repair of AP sites in DNA by catalyzing hydrolytic inci... |
P27916 | MDARSLLLLWLLLPLLLLLGCEVQGAHLTQQDEPTSPDLLETLSTYWDSAKAAAQGLYNNTYLPAVDETIRDIYSKGSAAISTYTGILTDQILTMLQGKQ | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein ... |
P0DUX7 | MGSRFLLALFLVLLVLGCEVQAAQQLQQDDPGSPALLDKVQESISSYWDTAKAAAQDLYQKTYLTSVDEKLRDMYSKSSAAMTTYASIFTDQILTLLKGE | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase.
PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycop... |
P02655 | MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein ... |
P0DMN9 | MGTRFLLALFLVLLVLGFEVQGAQLPQQDEPSSPTLLTQMQESLSSYWDSAKEAARGLYEKTYLPTVDEKLRDMYSKSTAAVSTYAGIFTDQLLTLLKGD | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein ... |
T1W425 | MGTRCLLVLLLVLLVLKCEVQGDDMARQDEATGPTLLSQMQESLYGYWGSAKAAAQDLYEKTYLTAMDEKIRDMYSTSTAAVRIYTGILTDQILSMLTGDP | Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase, the enzyme which hydrolyzes the triacylglycerols on chylomicrons and VLDL.
PT... |
Q9LKL2 | MDLNGECKGGDGFIDRSRVRILLCDNDSTSLGEVFTLLSECSYQVTAVKSARQVIDALNAEGPDIDIILAEIDLPMAKGMKMLRYITRDKDLRRIPVIMMSRQDEVPVVVKCLKLGAADYLVKPLRTNELLNLWTHMWRRRRMLGLAEKNMLSYDFDLVGSDQSDPNTNSTNLFSDDTDDRSLRSTNPQRGNLSHQENEWSVATAPVHARDGGLGADGTATSSLAVTAIEPPLDHLAGSHHEPMKRNSNPAQFSSAPKKSRLKIGESSAFFTYVKSTVLRTNGQDPPLVDGNGSLHLHRGLAEKFQVVASEGINNTKQAR... | Function: Controls photoperiodic flowering response. Component of the circadian clock. Expression of several members of the ARR-like family is controlled by circadian rhythm. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of th... |
Q9LVG4 | MCFNNIETGDEVETERQVFGSSEEDEFRVEDTARNTNNVQISQQQQQPLAHVVKWERYLPVRSLKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKSCIDLVLTEVDMPVHSGTGLLSKIMSHKTLKNIPVIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNLWQHVWRRCHSSSGSGSESGIHDKKSVKPESTQGSENDASISDEHRNESGSSGGLSNQDGGSDNGSGTQSSWTKRASDTKSTSPSNQFPDAPNKKGTYENGCAHVNRLKEAEDQKEQIGTGSQTGMSMSKKAEEPGDLEKNAK... | Function: Controls photoperiodic flowering response. Component of the circadian clock. Controls the degradation of APRR1/TOC1 by the SCF(ZTL) complex. Expression of several members of the ARR-like family is controlled by circadian rhythm. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 an... |
Q6LA42 | MTSSEEVVEVTVVKAPEAGGGKLSRRKIRKKDAGVDGLVKWERFLPKIALRVLLVEADDSTRQIIAALLRKCSYRVAAVPDGLKAWEMLKGKPESVDLILTEVDLPSISGYALLTLIMEHDICKNIPVIMMSTQDSVNTVYKCMLKGAADYLVKPLRRNELRNLWQHVWRRQTSLAPDSFPWNESVGQQKAEGASANNSNGKRDDHVVSGNGGDAQSSCTRPEMEGESADVEVSARDAVQMECAKSQFNETRLLANELQSKQAEAIDFMGASFRRTGRRNREESVAQYESRIELDLSLRRPNASENQSSGDRPSLHPSSA... | Function: Transcriptional repressor of CCA1 and LHY, thereby controlling photoperiodic flowering response. Involved in the positive and negative feedback loops of the circadian clock. With RVE8, forms a negative feedback loop of the circadian clock . Expression of several members of the ARR-like family is controlled by... |
Q93WK5 | MNANEEGEGSRYPITDRKTGETKFDRVESRTEKHSEEEKTNGITMDVRNGSSGGLQIPLSQQTAATVCWERFLHVRTIRVLLVENDDCTRYIVTALLRNCSYEVVEASNGIQAWKVLEDLNNHIDIVLTEVIMPYLSGIGLLCKILNHKSRRNIPVIMMSSHDSMGLVFKCLSKGAVDFLVKPIRKNELKILWQHVWRRCQSSSGSGSESGTHQTQKSVKSKSIKKSDQDSGSSDENENGSIGLNASDGSSDGSGAQSSWTKKAVDVDDSPRAVSLWDRVDSTCAQVVHSNPEFPSNQLVAPPAEKETQEHDDKFEDVTM... | Function: Transcriptional repressor of CCA1 and LHY, and positive regulator of LWD1 and LWD2 expression. Represses the expression of other clock proteins and master regulators of plant growth, development and response to abiotic stress. Involved in the positive and negative feedback loops of the circadian clock. Contro... |
Q8L500 | MGEIVVLSSDDGMETIKNRVKSSEVVQWEKYLPKTVLRVLLVESDYSTRQIITALLRKCCYKVVAVSDGLAAWEVLKEKSHNIDLILTELDLPSISGFALLALVMEHEACKNIPVIMMSSQDSIKMVLKCMLRGAADYLIKPMRKNELKNLWQHVWRRLTLRDDPTAHAQSLPASQHNLEDTDETCEDSRYHSDQGSGAQAINYNGHNKLMENGKSVDERDEFKETFDVTMDLIGGIDKRPDSIYKDKSRDECVGPELGLSLKRSCSVSFENQDESKHQKLSLSDASAFSRFEESKSAEKAVVALEESTSGEPKTPTESH... | Function: Transcriptional repressor of CCA1 and LHY, and positive regulator of LWD1 and LWD2 expression. Controls photoperiodic flowering response and temperature compensation. Involved in the positive and negative feedback loops of the circadian clock. Expression of several members of the ARR-like family is controlled... |
B0CHX9 | MESGFKVTLKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKLPRDTARIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEALGLPVRTLVAFEGD | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19586
Sequence Length: 181
Pathway: Purine metabolism; AMP biosynthesis via salva... |
P07741 | MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19608
Sequence Length: 180
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q31JG9 | MKQHPLAQYLEAVPDFPKEGILFQDISPLLRDHFVATIDAMSLLFSAKEWAEVDYLVGVESRGFIFASALALKHDKGFVKVRKPGKLPNVHASMEYGLEYGTDKLEMQKGNGKKVIICDDLIATGGSMQAAAKLCNEVGYEVVGMACLVDLKALNSFSHDGMTVRSVIQFDD | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18913
Sequence Length: 172
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q1G9R7 | MSIDFKKYIASVKDFPNEGIIFRDITPILQDGEAFAAATHEIAEYAKSRQADVIVGPEARGFLVGTPVAIELGIGFVPARKPHKLPREVEAAAYDLEYGSNVLEMHKDAIKPGQRVVICDDLMATAGTMHATKELIERLGGKVVGAAFYIELTDLKGREKFPDVDIFSLVQYTGA | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19125
Sequence Length: 175
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q9CHT5 | MELKDYIATIENYPKEGVVFRDISPLMADGNAYNYAATEIVQYARDKEIDMVVGPEARGFIIGCPVAFALGVGFAPVRKPGKLPREVIEATYEKEYGTDTLTMHSDSIKPGQRVLIVDDLLATGGTIAATIELVEKMGGIVVGCAFLIELDELKGREKIGDYDYKVLMHY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18713
Sequence Length: 170
Pathway: Purine metabolism; AMP biosynthesis via salva... |
B1XL39 | MDLKSLIRDIPDFPKPGILFRDITTLLNHPEGMRYTMDALVQLCLEANLKPDHVVGMESRGFIFGPTLAYNLNAGFVPVRKPGKLLAAVHTVEYELEYGTDTLEIHQDAVGSGDKIVIVDDLIATGGTAKATAELLTKIGCDIIGFVFIVELLDLKGRDRLPDAPVLSLIQY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18849
Sequence Length: 172
Pathway: Purine metabolism; AMP biosynthesis via salva... |
P73935 | MDLKALIRDIPDFPKPGIMFRDITTLLNSPEGLRYTIDSLVEQCESQELVPDHVVGMESRGFLFGMPLAYQMNAGFIPVRKPGKLPAPVHRVEYDLEYGKDSLEIHQDAVAPHHRVLIVDDLIATGGTAKATAELLTKLGCEVLGFAFIIELAALNGRQCLPDLPIISLVEY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18997
Sequence Length: 172
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q9X1A4 | MFKLDLKRFIRDIPDFPQKGIVFRDITPLLRNQEAFKEAIDRMCELVFDREFDLVVAPEARGFILGAAMAYKLGKGFVPVRKPGKLPYKTVYEEYQLEYGTEQLHIHEDAIEKGQKVLIVDDVLATGGTAEALIRLVKKLGGEVVSLAFLVELSYLEPRKRLEGYDVKTLIVY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19766
Sequence Length: 173
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q73M27 | MTIAKIRCRLFIMKDKIIDAAIRRVPDFPKKGILFYDITGILVNPEVFSYCLDKMTEMYKDKKVDAVAAIEARGFIFAAPFAYKMGIPLILIRKKGKLPGETYSASYDLEYGQASVEVHKTDVVKGQKVLLLDDLIATGGTLNAARSILEEGGAKVVGFCGVVGLPFLNYSKVLGDLPVKTLIEYDSEKI | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20975
Sequence Length: 190
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q13520 | MDAVEPGGRGWASMLACRLWKAISRALFAEFLATGLYVFFGVGSVMRWPTALPSVLQIAITFNLVTAMAVQVTWKASGAHANPAVTLAFLVGSHISLPRAVAYVAAQLVGATVGAALLYGVMPGDIRETLGINVVRNSVSTGQAVAVELLLTLQLVLCVFASTDSRQTSGSPATMIGISVALGHLIGIHFTGCSMNPARSFGPAIIIGKFTVHWVFWVGPLMGALLASLIYNFVLFPDTKTLAQRLAILTGTVEVGTGAGAGAEPLKKESQPGSGAVEMESV | Function: Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29370
Sequence Length: 282
Domain: Aquaporins contain two tandem repeats each con... |
B0DLE4 | MDDKFDDDALPNSKTTPEDYGDKLAEYDYTNTFPNTWMRLREPFREYIAEFVGVAVLIIFGVGADCQVVLSANTGVAPSPKGDYLSLNCGWAIGTAMGVWISGGISGGHINPAVTLALMAWRGFPWWKVPGFIFAQLLGGIVGAGLVYVNYIHAIDIVEGGRHIRTLDTAGLFATYAADYMTNVSCFFSEFLATAVLIVVIHAMNDKRNAPPPAGLAPLVLFFLILGIGASLGMETGYAINPARDLGPRMLTAMVGYGRQVFAFRNQYWIWCPVIAPFLGAQVGTIFYDLFFYKGQDNVFGRLGSHIHISPA | Function: Water channel required to facilitate the transport of water across membranes . In addition to water, shows also strong glycerol and ammonium transport activities . May be involved in fungal nitrogen (ammonium) support of the plant host in symbiosis . Glycerol accumulation has never been observed in ectomycorr... |
G5CTG3 | MAFMDKSEVRQRLQKVLQQCAKAPTWSPKEEVRQSIFWKSIRAELIGSLVLMVFSCSRDSIYGPVSYGCTYAILSYCFKSISAHFNPVITIAALLLRSITPFRCISLVLAQTLGTLSGASVCYYGLSNETETGSAPISPVLNVSPAKGFGYEFFGTFVIILTMSSYLDCNDYVSESGDSNLLPLIFGLSVGLSSGMARQATGGFLNPMRAFSLALFELNHWSNHYIYWIGPIFGCLLAVFTFDYTRPIIPNRDSNNRINFPTFNKNNKYEVEMQPETEITLATLA | Function: Probable water-specific aquaporin that may modulate the water content and osmolytes during anhydrobiosis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31694
Sequence Length: 285
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-form... |
Q9WTY0 | MEPGLCNRAYLLVGGLWTAISKALFAEFLATGLYVFFGVGSVLPWPVALPSVLQVAITFNLATATAVQISWKTSGAHANPAVTLAYLVGSHISLPRAVAYIAAQLAGATVGAALLYGVTPGGVRETLGVNVVHNSTSTGQAVAVELVLTLQLVLCVFASMDSRQTLGSPAAMIGTSVALGHLIGIYFTGCSMNPARSFGPAVIVGKFAVHWIFWVGPLTGAVLASLIYNFILFPDTKTVAQRLAILVGTTKVEKVVDLEPQKKESQTNSEDTEVSV | Function: Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28860
Sequence Length: 276
Domain: Aquaporins contain two tandem repeats each con... |
A0A384J409 | MNINEPRDGGGFVLPFFNDSKKSRKSHAGRDSLKSNRVPFTKWVPDTVSYTTKPLKNAHRWLHLHNKTRNHFVATVAEFAGTTLFLFFAFSGTQVALLATPANDSNVVGTPSNPAQLLYVSLCFGFSLAVNAWVFFRISGGLFNPAVTMGMCIVGALPYFRGLLLIFAQIIGGIAAAAIVSALFPGPITFRTSLGGGTSIVQGLFIEMFLTAELVFTIFMLAAEKHKGTFIAPIGIGLSLFIAELTGVYFTGGSVNPARSFGPSVVSGQFTGYHWIYWVGPILGAILASAFYKFIKMLEYETANPGQDAGRVGEVIDPEA... | Function: Water channel required to facilitate the transport of water across membranes (Probable). Involved in conidiation .
Catalytic Activity: H2O(in) = H2O(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48351
Sequence Length: 454
Domain: Aquaporins contain two tandem repeats each containing ... |
O14520 | MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVS... | Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH . The channel is also permeable to urea . Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export fro... |
B0D4J9 | MSGQHQITEQSSRNPLSRVSTLLPEKPLSPTSTYAGTQKHPEAPRQSSFLIQLQNIRNAIRKPMAEFFGVALLIIFGAGSACQVVLSTNPDVASSARGSFLSINFGWAIGIAMGVWVSGGISGGHINPAITIAMATYRGFPWRKVPSYILAQVLGGVVGAGLVYANYIHAIDIFEGGHHIRTQATASLFATYALPYMTQASCFFSEFLATAVLSMMVFALTDKRNHSPTNGLLPFALFILFVGLGASLGMETAYALNPARDFGPRLFLAMAGYGKALFNYRSQYWLWAPIIAPVLGAQAGGLLYDTFLNDGDNSPIKWRC... | Function: Water channel required to facilitate the transport of water across membranes . Acts as thre most efficient Laccaria water channel . In addition to water, shows also strong ammonium transport activity . May be involved in fungal nitrogen (ammonium) support of the plant host in symbiosis .
Catalytic Activity: H... |
Q4R691 | MVQTSRHRRSTRGSKMVSWSVMAKIQEILQKKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGHISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYTLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNAALPGTQALVIGILVVIIGVSLGMNTGYAINPSRDLPPRVFTFIAGWGKEVFSEGENWWWVPVVAPLLGACLGGIIYLVFIGSTTPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVS... | Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (By similarity). The channel is also permeable to urea (By similarity). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids... |
G5CTG4 | MAHNEKDPSSVEPIKRKRFSNEYVRLFLAEFLGTFILIVFGCGTVAVTILSKHQSQDFFSVNVGFFLGIAFGVFIAGGVSGGHLNPAVTLAFAVINKCKWRKVPVYMAAQYLGAWVGSAILTAIYYDALHNHDQGNRTIETAGIYASYPQEFLTWQGGLADQIFATLLLMMGILALTDERNMVGPTGRAYVPLLVGLLVLAIGLAFGFNCGYPINPARDFGPRLFTAMAGWGTQVFSEPRGTYNWWWIPIIGPHVGAIIGALAYNFFIGYHWPKERDDVQLQSPSSPIVIVKNDAYQPLRPSRSVYSEELRITTS | Function: Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34796
Sequence Length: 315
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the... |
O54794 | MAPRSVLETIQSVLQKNMVREFLAEFLSTYVMMVFGLGSVAHMVLGENSGSYLGVNLGFGFGVTMGVHVAGGISGAHMNAAVTFTNCALGRMTWKKFPVYVLGQFLGSFSAAATTYLIFYGAINHFAGGDLLVTGSKATANIFATYLPEYMTLWRGFLDEAFVTGMLQLCLFAITDKKNSPALQGTEPLVIGILVTVLGVSLGMNSGYAINPSRDLPPRLFTFIAGWGKQVFRAGNNWWWVPVVAPLLGAYLGGIVYLGLIHPSIPQDPQRLENFTARDQKVTASYKNAASANISGSVPLEHF | Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH . The channel is also permeable to urea (By similarity). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids . Mediates gly... |
P56403 | MAGSVLENIQSVLQKTWVREFLAEFLSTYVLMVFGLGSVAHMVLGERLGSYLGVNLGFGFGVTMGIHVAGGISGAHMNAAVTFTNCALGRMAWKKFPIYVLGQFLGSFLAAATTYLIFYGAINHYAGGELLVTGPKSTANIFATYLPEHMTLWRGFVDEVFVTGMLQLCIFAITDKLNSPALQGTEPLMIGILVCVLGVSLGMNTGYAINPSRDLPPRFFTFIAGWGKKVFSAGNNWWWVPVVAPLLGAYLGGIVYLGLIHAGIPPQGS | Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH . The channel is also permeable to urea . Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export fro... |
A0A384JP03 | MALRSPARDYLVSMIGELVGTFLFLFFAFAAAQTANQPNGTKPLTPNATDTSKLLYIALAFGASLAANVWVFFRVSGGQFNPAVTLALVLIRAVSPTKALILIPAQLVGGSLAAAAVKGIIPGDDILFAVSLGPGVANVQGLFIELLLTFMLVFTILMLVAEKTKSTFVAPIGIGFSLFIGHLVGIFWTGAGINPARAFSPALIQASFPSYHWIYWLGPALGSFLAAGLYLGLKEMKYELVGGDADKEKREEGLTVQQADLIIETLRGLPRAIQGSGALGQFEGTTEGHRSPVDLERGAEVRILEDDPHIRKSRYGSPDS... | Function: Plasma membrane water channel that regulates the reactive oxygen species (ROS)-signaling pathway through its capacity to act as a membrane channel for hydrogen peroxide uptake . Required for the formation of infection structures and infection, especially on host leaves where it is essential for the penetratio... |
O94778 | MSGEIAMCEPEFGNDKAREPSVGGRWRVSWYERFVQPCLVELLGSALFIFIGCLSVIENGTDTGLLQPALAHGLALGLVIATLGNISGGHFNPAVSLAAMLIGGLNLVMLLPYWVSQLLGGMLGAALAKAVSPEERFWNASGAAFVTVQEQGQVAGALVAEIILTTLLALAVCMGAINEKTKGPLAPFSIGFAVTVDILAGGPVSGGCMNPARAFGPAVVANHWNFHWIYWLGPLLAGLLVGLLIRCFIGDGKTRLILKAR | Function: Channel that allows the facilitated permeation of water and uncharged molecules, such as hydrogen peroxide and the neutral form of ammonia (NH3), through cellular membranes such as plasma membrane, inner mitochondrial membrane and endoplasmic reticulum membrane of several tissues . The transport of the ammoni... |
G5CTG5 | MSTAESRNHYKEVPTIEHYSEAIGITNRKKMDWRGWLRKSTLVRSQLIRGCMAEFLAVFVLMVFIEGSAATAIFTNRRQDILFGSISSGLGVAMAVYVAGGVSGAFLNPAVALAFAVLGKLSWKNCIFYMISQYLAAFVASCTMFAYLYEALNNFDGGERQMFGPNGTAHIWSTYPQPFLSPHTAFADQVFCTAILLIVVLAMCDSKNWKPHNGFLPIAIGLLIITISCTLSYNAGAAMNPSRDLAPRFFSYLAGYGTEPFGVKGYTWFFVPVLGSHCGAIIGGAIYQLFIGGQWPDDTSDTNSVSSMSYNEDNSTLTKR... | Function: Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37279
Sequence Length: 342
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the... |
Q88S84 | MLSVPDYEFWFVTGSQHLYGEEQLKSVAKDAQDIADKLNASGKLPYKVVFKDVMTTAESITNFMKEVNYNDKVAGVITWMHTFSPAKNWIRGTELLQKPLLHLATQYLNNIPYADIDFDYMNLNQSAHGDREYAYINARLQKHNKIVYGYWGDEDVQEQIARWEDVAVAYNESFKVKVARFGDTMRNVAVTEGDKVEAQIKMGWTVDYYGIGDLVEEINKVSDADVDKEYADLESRYEMVQGDNDADTYKHSVRVQLAQYLGIKRFLERGGYTAFTTNFEDLWGMEQLPGLASQLLIRDGYGFGAEGDWKTAALGRVMKI... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of L-arabinose to L-ribulose.
Catalytic Activity: beta-L-arabinopyranose = L-ribulose
Sequence Mass (Da): 53573
Sequence Length: 474
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabi... |
Q6D4W5 | MDHFKQLEVWFVIGSQHLYGPETLRQVKENAEKVVAGLNQQANLPVKLVLKPLVKTPDEILALCRDANYQDNCIGLLTWLHTFSPAKMWIGGLSVLSKPLLQFHTQFNAEVPWDTMDMDFMNLNQTAHGGREFGFIGARMRQAHQVVVGHWQDKNAHVRIGKWMRVAAAIQESKQLKVARFGDNMREVAVTEGDKVGAQIQFGYSVSAWGLGDLTAVVDAVSKGDIDALIEEYETSYQLTDAVKLNGANRQNLLDAAQIELGMKRFLEQGGYHAFTTDFENLYGLKQLPGLAVQRLMQQGYGFGGEGDWKTAALLRIMKV... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of L-arabinose to L-ribulose.
Catalytic Activity: beta-L-arabinopyranose = L-ribulose
Sequence Mass (Da): 55893
Sequence Length: 501
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabi... |
Q1JUP6 | MSQAMQPQRTSPSPDAAIAPARARGGVWQLINRSGIVMVFLVLFATLSLTVPDFLTPRNIQGLLLSVTLIGSIAVTMMFVLALGEVDLSVASIVAFSGVVASTLITATHSVVLGIAGGVLAGGAVGLVNGVLIARWRINSLIVTLAMMEVVRGLAFITSNGDAVMISEERFFDLGGGSFLGISYPIWSNIVGFVVFGFLLRKTVFGKNVLAVGGNGEAALLAGLPVMRIKITVFVLQGLVTGFAGVMLASRMSLGDPKTSVGLELGVISACVLGGVSLTGGVATISGVLVGVLIMGSVQDAMSLLNVPTFYQYLIRGGIL... | Function: Part of the ABC transporter complex AraFGH involved in L-arabinose import. Responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35372
Sequence Length: 339
Subcellular Location: Cell inner membrane
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P0AE26 | MSSVSTSGSGAPKSSFSFGRIWDQYGMLVVFAVLFIACAIFVPNFATFINMKGLGLAISMSGMVACGMLFCLASGDFDLSVASVIACAGVTTAVVINLTESLWIGVAAGLLLGVLCGLVNGFVIAKLKINALITTLATMQIVRGLAYIISDGKAVGIEDESFFALGYANWFGLPAPIWLTVACLIIFGLLLNKTTFGRNTLAIGGNEEAARLAGVPVVRTKIIIFVLSGLVSAIAGIILASRMTSGQPMTSIGYELIVISACVLGGVSLKGGIGKISYVVAGILILGTVENAMNLLNISPFAQYVVRGLILLAAVIFDRY... | Function: Part of the binding-protein-dependent transport system for L-arabinose. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34211
Sequence Length: 328
Subcellular Location: Cell inner membrane
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A3KNS9 | MTANVTVSSMYLFTVLLLLFNVYVNSQDTDAQLCQMCEGTIRHDSPVWSFCITKGYVKGHCCFKNNTSDVDTIIGLDLSNCSISHVEHLYNSSTALIIDLSNNPISNLSDYVFQGFSQLTQLLLPSKLECPGGRASWEKVEVKSITRICEGQKNACNQTVQMPLVCPENSLCSPYGPGFFECSCLNNFHGYKCMRQGEFPLVKVLGILTASTVVVSSVLWFTQRRKVKNT | Function: Involved in osteoblast cell differentiation. May play a role in inducing the cell cycle arrest (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25580
Sequence Length: 230
Subcellular Location: Nucleus envelope
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Q6UW56 | MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNCSLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTGDPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS | Function: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway. In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required... |
Q6PGD0 | MASRESGGSRAAALLLVLGVERALALPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPGPNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCPENGSCASDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGSTTLAISILLWGTQRRKAKAS | Function: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway (By similarity). In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates ... |
P23910 | MKKVILSLALGTFGLGMAEFGIMGVLTELAHNVGISIPAAGHMISYYALGVVVGAPIIALFSSRYSLKHILLFLVALCVIGNAMFTLSSSYLMLAIGRLVSGFPHGAFFGVGAIVLSKIIKPGKVTAAVAGMVSGMTVANLLGIPLGTYLSQEFSWRYTFLLIAVFNIAVMASVYFWVPDIRDEAKGNLREQFHFLRSPAPWLIFAATMFGNAGVFAWFSYVKPYMMFISGFSETAMTFIMMLVGLGMVLGNMLSGRISGRYSPLRIAAVTDFIIVLALLMLFFCGGMKTTSLIFAFICCAGLFALSAPLQILLLQNAKG... | Function: May be involved in either the transport or processing of arabinose polymers.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41926
Sequence Length: 394
Subcellular Location: Cell inner membrane
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P83572 | ANFPTVSLNTVGITRQIPQDFMNAV | Function: Toxic type II ribosome-inactivating protein (RIP). Induces apoptosis. Has cytotoxic activity against several human cancer cell lines. Is less cytotoxic to normal human cells.
PTM: Glycosylated.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass... |
Q1JUP5 | MQQIHPAGQATLLADTRNTLGEGATWCDRTRALYWVDIEGAQLWRCRADGSDLTPWPMPERLACFALTDDPDVLLVGLATHLAFFDLRSGAFTRIVEVEPELPTRLNDGRCDGSGAFVFGMKDEGAEPPRAVGGFYRLNADLTLERLALPPAAIANSIGFSPDGSKMYFCDSLVREIFVCDYRPGGEVANVRPFARLTDPDGDPDGSIVDRDGGLWNAQWGGRRVVRYGPDGVETDRVAVPTAQPSCTALDGEGRLYVTSARVGLSDDALADDPHAGGVFVAQTRHAGMATARFAGTPRG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the cleavage of L-arabino-gamma-lactone to L-arabonate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Can also use D-galactono-1,4-lactone as substrate in vitro; howeve... |
P94526 | MRIMASHDTPVSPAGILIDLDGTVFRGNELIEGAREAIKTLRRMGKKIVFLSNRGNISRAMCRKKLLGAGIETDVNDIVLSSSVTAAFLKKHYRFSKVWVLGEQGLVDELRLAGVQNASEPKEADWLVISLHETLTYDDLNQAFQAAAGGARIIATNKDRSFPNEDGNAIDVAGMIGAIETSAQAKTELVVGKPSWLMAEAACTAMGLSAHECMIIGDSIESDIAMGKLYGMKSALVLTGSAKQGEQRLYTPDYVLDSIKDVTKLAEEGILI | Function: Catalyzes the dephosphorylation of C5 and C6 carbon sugars in vitro . Catalyzes the dephosphorylation of 3'-AMP and phosphoserine in vitro .
Catalytic Activity: sugar phosphate + H2O = sugar + phosphate.
Sequence Mass (Da): 29315
Sequence Length: 272
EC: 3.1.3.23
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P94528 | MKKMTVCFLVLMMLLTLVIAGCSAEKSSGKSGETELTFWTFNGLHEQFYVEMVKEWNKKYPDRKIKLNTVVYPYGQMHDNLSISLIAGEGVPDIADVELARFSNFLKGSDIPLADLTPLIEKDRDKFVEARLTLYSKNGKLYGLDTHVGTTVMFYNMDVMKKAGVNPDDIKTWDDYHKAGQKVRKVTGKPMGTVETNDSATFLSMISQQNSGYFDKNGKLILNNDTNVKTLQYLKDMINDKTMIPAPGGGHHSEEYYGFMNQGGAASVLMPIWYMGRFIDYMPDLKGKIAIRPLPAWKEGGDRSAGLGGTATVVPKQSKH... | Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units . AraN captures the substrate and delivers it to the two transmembrane components (Probable).
Location Topology: Lipid-anchor
Seque... |
Q9KEE7 | MGKNILFFSFVGVMVLVLVACGGSSSSSSDADETSVIGDDIEGATELIFWTFAGQHVDLFEDAVVSWNEEFPDRPIKLVAETYPFDQMHNNLLLALQSGSGAPDLADIEVSRFPNFLQGVPQLLPMNDHVEPVIDKFVEARFNLYAKDGEYYGIPTHVGASVMYYNKEIMDEAGVDIESIETWDDYVEAGKQVVERTGKVMTTVPTDDYLPMFQMVSQRGSDFFDENGNLTLDTQENIEVLQFLYDLIYVHEIAELTPGGQPHAEEYYQYMNDGNVASMAMPIWYMGRFLDNMPDLAGKMLIQPLPAWEEGGFRSAGMGG... | Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides (By similarity). AraN captures the substrate and delivers it to the two transmembrane components (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 50220
Sequence Length: 445
Subcellular Location: Ce... |
O53092 | MTEEKPAKKIGLLALIALVISSSIGSGVFGLTSDLASASAPGPVLIAWVIVGFGILMLALSLNNLLMKEPELEGIFSYAEKGFGPFAGFISGWGYWLSAWLGNVTFATILMSALGYFFPIFKSRQNLPSILVASVLSWSLTYFVNRGVEGAAAINTLVTICKLIPLFVFIIFGIVLFKGHLFTQAFWNNMSSSFVAGDVMSQIKNCMMVMMWVFVGIEGASMLSARAEKKSDAGKATILGLVSLLAIYILASVLPYGYLTQDQLASIKQPAMLYIFEQMVGTWGGYFIGVGLIISILGAWLSWTMLPAETMLLMAKQNLL... | Function: Catalyzes electroneutral exchange between L-arginine and L-ornithine.
Catalytic Activity: L-arginine(out) + L-ornithine(in) = L-arginine(in) + L-ornithine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51881
Sequence Length: 475
Subcellular Location: Cell membrane
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P18275 | MSQESSQKLRLGALTALVVGSMIGGGIFSLPQNMAASADVGAVLIGWAITAVGMLTLAFVFQTLANRKPELDGGVYAYAKAGFGDYMGFSSAWGYWISAWLGNVGYFVLLFSTLGYFFPIFGKGDTVAAIVCASVLLWALHFLVLRGIKEAAFINTVTTVAKVVPLFLFILICLFAFKLDIFTADIWGKSNPDLGSVMNQVRNMMLVTVWVFIGIEGASIFSSRAEKRSDVGKATVIGFITVLLLLVLVNVLSMGVMTQPELAKLQNPSMALVLEHVVGHWGAVLISVGLLISLLGALLSWVLLCAEIMFAAAKDHTMPE... | Function: Catalyzes electroneutral exchange between arginine and ornithine to allow high-efficiency energy conversion in the arginine deiminase pathway . Also mediates the proton motive force-driven uptake of arginine and ornithine, but the exchange is several orders of magnitude faster than the proton motive force-dri... |
Q9UU82 | MIAATPAKSKPSDVNLEQTFKGVSETSKIDLRRSRAAYRPLELSPTPSIFARNYQRNAVDFTGFFVLFWVAVSIMIFMSFLENFELTGRPVVGTIFKYFQSNLLDLAKADLAMSSMFLLAFPFQKIFALGYLRWYGLGVYLYSILILLFLSHCVLRCCLSNWSWTHRAMFILHSMVILMKLHSYNVVNGWYSYCYHSLNKLQSKKTDLDDDERSSVEFYEHCLNHHGNTYPENLTIPNALDFLFMPSLCYQLYYPRTAHVRIHYLIECALGTFGCIFLLVIISDHFMVPVLAKAIRTIIEAPEDASATYFAIRLGHTVAF... | Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55157
Sequence Length: 472
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
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O15033 | MFYVIGGITVSVVAFFFTIKFLFELAARVVSFLQNEDRERRGDRTIYDYVRGNYLDPRSCKVSWDWKDPYEVGHSMAFRVHLFYKNGQPFPAHRPVGLRVHISHVELAVEIPVTQEVLQEPNSNVVKVAFTVRKAGRYEITVKLGGLNVAYSPYYKIFQPGMVVPSKTKIVCHFSTLVLTCGQPHTLQIVPRDEYDNPTNNSMSLRDEHNYTLSIHELGPQEEESTGVSFEKSVTSNRQTFQVFLRLTLHSRGCFHACISYQNQPINNGEFDIIVLSEDEKNIVERNVSTSGVSIYFEAYLYNATNCSSTPWHLPPMHMT... | Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-11'- or 'Lys-33'-linked polyubiquitin chains, with some preference for 'Lys-33' linkages . E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted subs... |
P0DKH9 | MGLSDCLIYRLVVRCFLDYSICAPFYFYHKFMLSASEPVF | Function: Negative regulator of the auxin response.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4747
Sequence Length: 40
Subcellular Location: Cytoplasm
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A9B055 | MPTTIQAISAEAINLPLTEPFAIASGAQAVAANVLVKVQLADGTLGLGEAAPFPAVSGETQTGTSAAIERLQSHLLGADVRGWRKLAAMLDHAEHEAAAARCGLEMAMLDALTRHYHMPLHVFFGGVSKQLETDMTITAGDEVHAAASAKAILARGIKSIKVKTAGVDVAYDLARLRAIHQAAPTAPLIVDGNCGYDVERALAFCAACKAESIPMVLFEQPLPREDWAGMAQVTAQSGFAVAADESARSAHDVLRIAREGTASVINIKLMKAGVAEGLKMIAIAQAAGLGLMIGGMVESILAMSFSANLAAGNGGFDFID... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Has epimerase activity with a variety of hydrophobic dipeptides (in vitro). Enzyme activity is highest with L-Phe-L-Tyr, but is still relatively low, suggesting that L-Phe-L-Tyr is not the physiological substrate.
Sequence Mass (Da): 36784
Sequence Length: 356
EC: 5.1... |
B5BLW5 | MPLDPEVRNFLQVYYKANIIDFTKYQFQEIRQKVNELLAKAVPKDPVGETRDMKIKLEDYELPIRIYSPIKRTNNGLVMHFHGGAWILGSIETEDAISRILSNSCECTVISVDYRLAPEYKFPTAVYDCFNAIVWARDNAGELGIDKDKIATFGISAGGNLVAATSLLARDNKLKLTAQVPVVPFVYLDLASKSMNRYRKGYFLDINLPVDYGVKMYIRDEKDLYNPLFSPLIAEDLSNLPQAIVVTAEYDPLRDQGEAYAYRLMESGVPTLSFRVNGNVHAFLGSPRTSRQVTVMIGALLKDIFK | Function: Has a broad substrate specificity. Hydrolyzes various p-nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids in vitro. Most active against paraoxon, phenyl acetate and p-nitrophenyl caproate (C6), respectively. Has also tributyrinase activity, but shows no hydrolytic activity toward other tri... |
Q94231 | MGLFFSKISSFMFPNIECRTLMLGLDGAGKTTILYKLKLNETVNTIPTIGFNVETVTFQKITLTVWDVGGQKKIRALWKYYFPNTTTLVFVVDSSDIERIPEAKEELFSLLAEPELADSHLLVFANKQDMPNARSPAELTQLLDLGSLKNREWFICGTNAHSGQGLYEGLMWVKKQMKT | Function: Small GTPase involved in protein trafficking between different compartments (By similarity). Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-boun... |
P36397 | MGLSFGKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIASKA | Function: GTP-binding protein involved in protein trafficking; required for the sequence-specific vacuolar sorting route to the lytic vacuole, for the ER-to-Golgi transport and for the Golgi-derived transport to the plasma membrane . Involved in the recruitment of COPI and GDAP1 to membranes. Required for recycling of ... |
P51822 | MGLSFTKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEIIDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIASKS | Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 20681
Sequence Length: 181
Subcellular Location: Golgi apparatus
EC: 3.6.5.2
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O00909 | MGLAFGKLFSRFFGKKDMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEFKNINFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEACDELTKMLNEDELRDAVLLVFCNKQDLPNAMSVAEVTDKLNLHSLRSRKWYIQSTCATSGDGLYEGLDWLSNTLTSSSK | Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 20682
Sequence Length: 182
Subcellular Location: Golgi apparatus
EC: 3.6.5.2
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P61209 | MGNVFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIGEAREELMRMLAEDELRDAVLLIFANKQDLPNAMNAAEITDKLGLHSLRNRNWYIQATCATSGDGLYEGLDWLSNQLKNANR | Function: Small GTPase involved in protein trafficking between different compartments. Modulates vesicle budding and uncoating within the Golgi complex. In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is... |
P84077 | MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK | Function: Small GTPase involved in protein trafficking between different compartments . Modulates vesicle budding and uncoating within the Golgi complex . In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane . The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins,... |
Q6FDQ8 | MPHQHKGIDKAKILTEALPYIQRFSGKTLVVKYGGNAMTDPELESSFARDIVLLKTVGLNPIVVHGGGPQVDSLLKRLGQVSDRIDGMRVTDEATMEVVEMVLGGSVNKSIVNLINQHGGRAIGLTGKDGNLIRARKLLMEKHDEQGDIKHIDLGLVGEVVGIKTDVLEMFTQSDFIPVIAPLGVDESGNTYNINADLVAGKVAEALGAEKLILLTNISGVLDENKNLLTGLSTQEVDRLIATGVIYGGMIPKVGCALDAVKGGVVSAHIVDGRVPHATLLEIFTDHGVGTLITNRLHAKSEH | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 32305
Sequence Length: 303
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q5HB82 | MKLRNVSKNNLNKEDTKLSIEQFGGNVEWFNITKTLSESLPYIQQFSGETFIIKYGGAAMTDKKLAESFAHDVVLLKQLGINPIVVHGGGNKINEFLEKINKKSTFINGLRITDAETLEIVEMVLCGLVNKNITQLINNAGGNAIGLCGKDANLIEAKKICYTYKENQSNNVEKILDMGFVGEPHDINTDLLFFMEESDFIPVIAPVCSGENNLTYNVNADLVAGALANAMAAAKLIILTNVSGVTDSNGNLISELSVSHAENLIDNGTAHTGMIPKLQTCVRVVKEGYGSAHIIDGRIPHVLLLELFTIHGTGTMVVNS... | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 34878
Sequence Length: 322
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
B1H0L5 | MSELTVVKFGGSLTENPQAQNKFLEELTLISKRQNIILVHGGGPEINALLEKFAITSRFVNGLRFTDADTLGVVELALSGKVNRVLTTGLIKNGANAVGISGKDGKSVICRQVEYLGFVGEPVKVNRKLIDILIKSRFLPVIASIAADVEGNIMNVNADTLAASIAVAFKAQKLIFLTDVAGVFDKNNNIIKEIKIKEINSLIEDKTITGGMIPKIKGCAESVKKGLKEVWIAEGISGIQKIKGTVIKK | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 26755
Sequence Length: 249
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q0RFA8 | MTDTAPTDITTATDITTATGAATGTGRGPAATARGHAALAKTQVLIEALPWLSRFQGATIVIKYGGNAMTEPALRAAFAADIVFLRYSGLRVVVVHGGGPQITAHLARLGVESTFVGGLRVTTPETMDVVRMVLLGQVNRDVVGLVNDHGPFAVGLSGEDANLFTARRRPAIVDGQEVDVGLVGDIVEVRAETVDALLDSGKVPVVASVARGIDGGVYNVNADTAAAELAVALGATKLVVLTDVEGLYADWPTSDEVLSELSITELEQLLPTLAAGMIPKMEACRRAVRGGVPQAHVLDGRVPHAVLLEIFTDDGIGTLI... | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 35508
Sequence Length: 343
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q2J862 | MNAPTRTPPPSNGGHGSTGSTGSTGDAAPGGGTGRGPAATARGHAALAKTQVLIEALPWLSRFQGATIVVKYGGNAMTEPALREAFAADVVFLRHSGLRVVVVHGGGPQITAHLERLGVPSTFVGGLRVTTPQTMDVVRMVLLGQVNRDVVGLVNDHGPFAVGLSGEDANLFTARRRPAIVDGREVDVGLVGDIVEVRPETINALLGSGKVPVVASVARGVDGGVYNVNADTAAAELAVALGATKLVVLTDVEGLYADWPASDEVISELSITELEQLLPSLTAGMIPKMEACRRAVRGGVPQAHVLDGRVPHAVLLEIFT... | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 36857
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q07905 | MGKTVVIKCGGSVLDELSPAFFASVNAMRKQGMEVVIVHGGGPEIGQMLKTLRVPSEFVNGLRKTTKDVLAVVEMVLSGKVNKQLASMLRQHGLPAVGVSGVDGGLLEAEPIDLAKLGYVGRVKTVRSQLLRTLLAAGYIPVISPLGIDQNGQTYNINADTAAGAVAAAIGASQLAFVTNVPGILRDGALVAEATAEMIERLIEDGVITGGMIPKVQAALSALSDALPEVMIVSGKTTFYQNGTWHGTTIRKEVGVYL | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 26935
Sequence Length: 258
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
A4IL48 | MENTVVIKCGGSVLDELSPAFFASVKTMREQGMNVVIVHGGGPEIGKMLKQLNVRSEFVNGLRKTTKEVLAVVEMVLSGKVNKQLVTMFKQHGLPAVGISGVDGGLLEAEPIDGIKLGYVGRVTAVRVDLLQTLLAANYIPVISPLGVGRSGQTYNINADTAAGAIAAAIGANQLAFVTNVPGLLQDGTLIGEATAETVEQLLKDGVITGGMIPKVKAALSALSDALPKVMIVSGKTPFYEQGTWHGTTIRKEVGAYL | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 26981
Sequence Length: 258
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
B0TL87 | MANTRAISSGAKPVMVLKVGGALLQCEMGMARLMEAAAKIIANGQPIIMVHGGGCLVDEQLKANGMTTKKLDGLRVTPQEQIPVIVGALAGTSNKTLQAAAIKAGVTSLGMSLADAGMMSAKVKDPQLGLVGEVEPKDASYLEFVLSKGWMPIVSSIAISEQGEMLNVNADQAATALAKLVSGSLVLLSDVSGVLDGKGQLISSLNRAQVNELTKIGVIEKGMKVKVEAALDVAESMGQAVQIASWRHAQQLIALSRGETVGTQIQPQIQ | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 27994
Sequence Length: 270
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
A7GSF4 | MKVAIIGATGYGGIELIRLLQQHPYFSIVSIHSFSQVGEHITSSYPHLRRFLVYTLQEIDVESIKKEADLVFLATPAGVSVKLTPLLLKAGLKVIDLSGDFRMVNPSIYEMWYKKPAASEEFLQQAVYGLSEWKRDEIQQAKLVANPGCFATATLLAIAPLMRNKIIEENSIIIDAKSGVSGAGKTPTHAAHFPELYDNLHIYKVNEHQHIPEIEQMLIGWNEQAKPITFSTHLIPVSRGIMVTLYAKIRKYVQIEELHNLYTNIYKNAYFVRIRPYGEFPSIKEVRGSNYCDIGIGYDERTKRITVVAVIDNMMKGAAG... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 38838
Sequence Length: 345
Pathway: Amino-ac... |
Q8A1A7 | MIKAGIIGGAGYTAGELIRLLLNHPETEIVFINSSSNAGNRITDVHEGLYGETDLRFTDQLPLDAIDVLFFCTAHGDTKKFMESHNVPEDLKIIDLSMDYRIKSDDHDFIYGLPELNRRATCTAKHVANPGCFATCIQLGLLPLAKNLMLTGDVSVNAITGSTGAGVKPGATSHFSWRNNNISIYKAFDHQHVPEIKQSLKQLQNSFDSEIDFIPYRGDFPRGIFATLVVKTKVALEEIVRMYEEYYAKDSFVHIVDKNIDLKQVVNTNKCLIHLEKHGDKLLIISCIDNLLKGASGQAVHNMNLMFNLEETVGLRLKPS... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 35838
Sequence Length: 322
Pathway: Amino-ac... |
P59305 | MAKYTVAVAGATGYAGGEALRILAAHPDFDITCVAGHSSVGESMAKHMPHIPQLANLVVEDTAPEVLNGHDVIILALPHGASGKLASQLDPNAVVVDLGADHRLEEQAAWDEFYGGDFYEHWTYGMPELITGKAADGSYTRQRAALPGTKRIAGPGCNVTATTLALQPGIAEGLVESQDIVADLVVGYSGAGKNLKRTNLLAAEALQSALPYSVGGKHRHIPEILQNFAHAAGKSAAEASEFTLGFTPILAPMSRGILATVSARMTDKAKTLSDEEIRAVWSKAYEGQDFMVLLPEGTLPATGNIIGSNAAHLQVVTDRK... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 38017
Sequence Length: 364
Pathway: Amino-ac... |
C0QYU7 | MIKVSVIGATGYAGAELIRLLLSHSKVELKNLSSKSFVGKNINEIYPNLNKNLDKLLLDENEIFEDTDVVFASLPAGLSDDIANKCFEKNILFIDLGADFRLDNEEDYKNWYGNEYKYKNLHKEAIYSIPEIIKYDNVYNKKELKNAKIIGNPGCYPTSIGLALAPALVNKFIIKDDIIIDSKSGATGAGRELKLNTHYTECNEAFAPYKIAEHRHTPEIEQTLSNIYGEDIKVTFVPHLLPLNRGIVSTIYAKLENKNIKLKDIHNTYKNFYKDSAFVRVLNIGEIANLKYVKYSNYCDISLHMDDRTNKLIIVSTIDN... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 39651
Sequence Length: 352
Pathway: Amino-ac... |
Q92QR7 | MKPKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAGNNRVRIIDTSTAHRVAPDWAYGFAEMDKAQPQRIRDARHVANPGCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQMEDDQNPDHIGAPHFLYGLTLKHKHVPEMKMHGLLERAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAGQSIVEVVPLDESAKLARIDATELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLMLSA | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 33298
Sequence Length: 310
Pathway: Amino-ac... |
Q7UVL4 | MSSSNLRVALVGSTGYTALEVARLLLTHPGADLVVATSRQDEGKPLSEIHPMLAGRCDVTLQPLDADVIAKSADVAMCCLPHGASAESVKQLAEAGMRVIDFSADFRLSSLETYQHWYGVKHPWPERIGDVVYGMPEFFADEIRSADIVANPGCYPTSAIMPLAPLVKAGLIETDDIIVDSKSGVSGAGRSPKLGTLYCETNESISAYAVGTHRHAPEIADLVERIAGAPIEVMFTPHLTPMDRGILSTIYVKPVGKAGSVEDAVRAMMSLLRDTYSDQPCVHVVDHLPATKYVAGTNHVQISVRPSGKRAVIVCAIDNL... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 36822
Sequence Length: 346
Pathway: Amino-ac... |
Q9LA02 | MTQKIAILGASGYTGAELARIIATHPEMEITALSGDRKAGMRMGEVFPHLRHIGLPDLVKIEEIDFSGIDLAFCALPHATSQAVIAELPRDLKVVDLSADFRLRDAAEYEKWYGKPHAAMDLQAEAVYGLTEFYREELKTARLCAGTGCNAAAGQYAIRPLIEAGVIDLDEIVIDLKAGVSGAGRSLKENLLHAELAGGTMPYSAGGKHRHLGEFDQEFSKVAGRPVRVQFTPHLMPFNRGILATVYVRGTPEDIHAALASRYENEVFLEVLPFGQLASTRSVAGSNFVHLGVIGDRLPGRAVVTVALDNLTKGSSGQAI... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 36780
Sequence Length: 342
Pathway: Amino-ac... |
Q2RRM4 | MSERVNVAILGASGYTGAELVRLLARHPRVTLAALTANRKAGQAFASVFPHLGGLDLPVLSTIEAVDWSAIDFVFCALPHGTTQTIIGDLLNGPHGGRLRIADLSADFRLADPMVYQTWYGHAHEAVELQKEAVYGLTEINRAAIATARLVAVPGCYPTSAQLPLIPLLRAGLIDPDAIIIDAKSGASGAGRDAKEGSLHCEVSEGIHAYGVGTHRHGPEIEQGLSLAVGRPVAVTFTPHLMPMNRGILSTIYLRATAGNDATTLRQALSAAYADEAFVRVVPEGVSPHTRHVRGSNFVLIGVHADRVPGRVIVTCVEDN... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 37298
Sequence Length: 352
Pathway: Amino-ac... |
Q1AS32 | MGLSVGIYGGSGYVGVELVRLLAGHPEVGSLAVASRGHAGRRIGEVYPQVAVGGEYLDPSEVDVSSLDVAFVAYGHGESAEAVRGLLEGGVRLVVDLSADFRLPDVRVYEEWYGEHPAPELLGEAHYGLPEVFGALEGRLVANPGCYPTAAILALAPVVRRMGGEVRSVTINALSGVSGAGAKPSARTHFVSVNESVSPYGVSGGEPRHRHTPEIEIMLRRLGEAPPVTFVPHLLPISRGELETITVEAGELPGAEEVLGWYREDYGGWRFVEAREEVPHISHVANTNRARLSAAVDRRAGKLLLFAAVDNLLKGAAGEA... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 36171
Sequence Length: 340
Pathway: Amino-ac... |
P54638 | MTKPVASYELDEKRFLTLLGKLIGETENLQNRPPALIPIEDNAGRHVIEALTPYLKANGGVLELEQVHCDPVNYPKRGNIIIEYPGTSKGTSSPKTISFVGSHLDVVPADKTAWDRNPFQLIIEGDKLYGRGTTDCLGHVALLTDLFIQLATEKPALKHSIFAVFIVSEENDEIPGIGVDALDHSGKMNPCKNGPVYWVDSADSQPTIGTGGAQTWNLTAHGKNMHSAMPYRTVNSVELVNEALAEIQRRFYIDFKPHPKEAEYKFDCSSTMKPTLWKPIAGSYNTIPGESTICGDIRLTPFYDMKEMRAKVEGYIKDIN... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Catalytic Activity: H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine
Sequence Mass (Da): 49070
Sequence Length: 447
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1.
EC: 3.5.1.16
|
Q8Y6U2 | MELIKGNIASPKGFYADGKHAGLKRKRNDIGWIYSEVPANAAAVYTMNQMQAAPIFVTKDSFQSNAKLQAIIVNSGNANACTGNQGMLDALAMRAQTAEKLEIPLDSVAVASTGIIGDMLPMDKINAGIEMLEKQTGNAADFEEAILTTDTFQKQISFQTEIGGRKVTMSGVAKGSGMIHPNMATMLAFITTDAAIPAELLQKLLKIKVDKTFNQITVDGDTSTNDMVVVMANGCAENPMLQEGTADFAKFADMFQAVTEHLAKSIARDGEGATKLIEVQVNGATKTEDARMIAKKIVSSSLVKTAAFGGDGNWGRIICA... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
C0PF72 | MSPPSVLLLHSRIPLQPRPFRMNSRAAPSRVVVCSVASTEGFISAAPILLPDGPWKQVEGGVTAAKGFKAAGIYSGLRAKGEKPDLALVACDVDATVAGAFTTNVVAAAPVLYCKHVLSTSKTGRAVLINAGQANAATGDLGYQDAVDSADAVAKLLNVSTDNILIQSTGVIGQRIKKEALLNSLPRLVGSLSSSVQGANSAAVAITTTDLVSKSIAVQTEIGGVAIRIGGMAKGSGMIHPNMATMLGVLTTDAQVSSDVWREMIRMSVSRSFNQITVDGDTSTNDCVIAMASGLSGLSGIQSLDSIEAQQFQACLDAVM... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-ac... |
A8Q9M0 | MWYRTFRTLGYTICRPYATCATKAERFVKTIDPSTLPRGYLVSSTYAGIKNAIRPVTSTNEPSAATTNVPHPQEAPKPDVALIVSSVPAAIAGTFTTNVFKAAPVVHATTALKAAGPNARVRAILTNSGCANAVTGQQGLEDTQTLVNRVQALLSPRNQNAIPTYEQDARSSSTDVLMMSTGVIGVRLPVAHIQRCLEHLAAPSILQSHPDAWLEAARAYMTTDTFPKIRTRQFILGNRRCSIVGIDKGAGMIHPRMTRSGGQLHATLLGVFATDAPISSATLQRCLDEAVRVSFNCISVDGDMSTNDTILALANGQAPF... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
PTM: The alpha and beta chains are autoproteolytically processed from a single... |
Q8TK55 | MKKIEGGICAVKGVTANGIKLGKMGITVIRAEGPAAGVFTKNKVTAAPVVLSKGVIETQHQLSAIIANSGNANAFTGDDGFLDAMEMASALSESLDLEPDTVAVASTGVIGRRLDVSWIREHLPEVLEGLGSSPECSLAAAKAIMTTDKALKEVAVELDCGVRIGAIAKGSGMIEPNMGTMLCFAYTDALVPADVLDAALRIAVDKTFNMVVVDGDTSTNDMVLFTSTCKSGIKPCMECLDEFEDALIYLFTDLAKKMARDGEGATKLIEARVTGAKTYEDARLAVKAIVRSPLVKSAIFGKDPNWGRVVAAAGYSGAEL... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
Q607S6 | MAASPEDRNLSDIRLCPIAGIRLGTAAAAIKHVGRDDVLLIEMAEGSACAAVFTQNAFCAAPVTVAREHLRQAPRWLLVNSGNANAGTGTRGLADARASCEAVAALVGGRADRVMPFSTGVIGEYLPLDKIRAALPKAFEALSEDGWEAAARAIMTTDTRPKKAVRRIEIAGRPVVVSGIAKGAGMIHPNMATMLAFVATDARIGAGLLQSVLERAVNRSFNCITVDGDTSTNDACVLMASQRSEAPLIEPGSAHVEAFQSAVDAVLAELAEAIVRDGEGATKFIRILVEEAASEDEARLVGKTIAHSPLVKTAFFASDP... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
Q57645 | MRVIDGGVTAPKGFKANGYKEGKFGVAIIISEKDAVGAGTFTTNKVVAHPVVLSRELIKNRDKFRAIVANSGNANCFTKDGMEDAKEMQRLVAELFNINEDEVLVASTGVIGRKMDMNIIKDRINKVYNLIKEGNSSINAAKAIMTTDTKPKEIAVEFEVNGKTVRVGGIAKGAGMIAPNMLHATMLCFITTDIEIDKESLTNILQKVVDKTFNNISVDGDTSTNDTVFVLANGLSGVNYEECGEEFENALLYVCRELAKMIVKDGEGATKFMEVVVKGAKTEEDAVKASKAIVNSLLVKTAVFGGDPNWGRIVAAVGYS... | Function: Catalyzes only the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Sequence Mass (Da): 43757
Sequence Length: 402
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornith... |
Q8TX15 | MRAPEGFLLGGIKREGIGVGLIFSERRCAVAGTFTENTLRAAPVEHSEEVCDRGVARGVIVNSGHANAMTGEEGYQDVLRTAEAIAELMGAPEDEIVVCSTGVIGERPPVDKIVRYAREVWEDIGPTERHVREFSRAIMTTDTEEKIALYEGDGWSLLGIAKGAGMIHPNMSTMLAFLLTDVGAKPKELQMWLRDVVNDTFNMITVDGDESTNDSVVLLANGSSNLKVGSDVTITEFQRALEEVCTELAEKIVRDGEGATKLMIVCVHGASNEVEARRAARAIASSNLVKAALFGENPNWGRIGAAVGAARVDVDPDELR... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
Q8PZL8 | MKQIEGGICAVRGVSAYGIKPGKMGIAVIRAEGPAAGVFTRNKVVAAPVTLSRERIETEHRLSAVIANSGNANAFTGDDGFLDAMEMASMVAENLGLDPDNVAVASTGVIGRRLDVSFIKEHLPEVLEGLGSSPECSRAAAKAIMTTDRALKESAVELDCGVRIGAIAKGSGMIEPNMGTMLCFAYTDAKVPADVLDAALKIAVDKTFNMVVVDGDTSTNDMVLFTSTCKSGVKPCLDCLDDFEEGLVCVFTDLAKKMAKDGEGATKLIEARVTGAKKYEDARLVAKTIVRSPLVKSAIFGKDPNWGRVVAAAGYSGAEL... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
O26284 | MYTMELRFIRGGVCAVDGVLAAGCREGKYGVGLIINRGSTAAAVFTSNRVRAEPVKLTERVIADGSISAIVANSGNANCFTGREGMDDARRMARKVAESLSMDESEVAVASTGVIGRRMPIDKIEFLIQSAAAQLENSEAASGALAEAIMTTDTFPKEVAVEFELETGEKARIGAVAKGSGMIAPNMATMLSFITTDVDASSSELTEALRVAVDESFNMLIVDGDESTNDMVIISSTRTSGRIDSNFREALVAVCRELARMMARDGEGVTKSFQVDVVNAGTHEDAKMAARAIAGSSLVKTAIFGADPNWGRIVAAAGYS... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
Q6D9D2 | MRNSTKQEDLVKAFKALLKEEKFSSQSEIVHALQDEGFENINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTTSSPLKNLVLDVDYNDAVVVIHTSPGAAQLIARLLDSLGKSEGILGTIAGDDTIFTTPARGFSVKQLYEAILVLFEQEL | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 17162
Sequence Length: 156
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
|
A6KXY8 | MKSKNSRLDAIKIIISSKEVGSQEELLQELAKEGFRLTQATLSRDLKQLKVAKAASMNGNYVYVLPNNTMYKRMTEQHSASEMLMHNGFISIEFSANLAVIKTRPGYASSLAYDIDNRNFDEILGTIAGDDTIMLVIREGCTRAGVKNALSLIIPNIQ | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 17528
Sequence Length: 158
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
|
A9WQ89 | MSAESAAIVQPIALIPATKTARQARIAALLTAQSVRSQAELAALLADDGVQVTQATLSRDLVELGAVRVRADGGLVYAVPQAGVDRTPHAAVSKEYLDARMTRLCAELLVTAEASANLVVLRTPPGAANFLAMAIDHSVLPDILGTIAGDDTVLVIARDPFGGAAIAERFLQFAEEPGT | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 18566
Sequence Length: 179
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
|
Q5FWH6 | MSAQSLPAATPPTLKPPRIIRPRPPSRHRAPHSPGPLHNGSSPKALPQISNDASASVCTSIFWEPPTASLKPPALLPPSVSRTSLDSQTSPDSPSSTPSPSPVSRRSISPEPAPCSPVPPPKPSGSSRTPLPSGPTPLQDGSASAPGTVRRLAGKFEWGAEGKAQSSDSLERCSQGSTEVNGEKETPEAALSGNGSQENGTPDAALACPPCCPCVCHVAKPGLELRWVPVGSSEDILRIPCRASPLRASRSRINPPVISHPPVVLTSYRSTAERKLLPPLKPPKPTKVRQDISTSEELPQPDLKLPSEDGIQTATKAWEG... | Function: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2.
PTM: Phosphorylated on tyrosine residues upon EFNA1 stimulation. EPHB2-dependent phosph... |
Q5VV41 | MAQRHSDSSLEEKLLGHRFHSELRLDAGGNPASGLPMVRGSPRVRDDAAFQPQVPAPPQPRPPGHEEPWPIVLSTESPAALKLGTQQLIPKSLAVASKAKTPARHQSFGAAVLSREAARRDPKLLPAPSFSLDDMDVDKDPGGMLRRNLRNQSYRAAMKGLGKPGGQGDAIQLSPKLQALAEEPSQPHTRSPAKNKKTLGRKRGHKGSFKDDPQLYQEIQERGLNTSQESDDDILDESSSPEGTQKVDATIVVKSYRPAQVTWSQLPEVVELGILDQLSTEERKRQEAMFEILTSEFSYQHSLSILVEEFLQSKELRATV... | Function: Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6.
Sequence Mass (Da): 8... |
Q86VW2 | MRGGHKGGRCACPRVIRKVLAKCGCCFARGGRESYSIAGSEGSISASAASGLAAPSGPSSGLSSGPCSPGPPGPVSGLRRWLDHSKHCLSVETEADSGQAGPYENWMLEPALATGEELPELTLLTTLLEGPGDKTQPPEEETLSQAPESEEEQKKKALERSMYVLSELVETEKMYVDDLGQIVEGYMATMAAQGVPESLRGRDRIVFGNIQQIYEWHRDYFLQELQRCLKDPDWLAQLFIKHERRLHMYVVYCQNKPKSEHVVSEFGDSYFEELRQQLGHRLQLNDLLIKPVQRIMKYQLLLKDFLKYYNRAGMDTADLE... | Function: May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. It works as a guanine nucleotide exchange factor for Rho family of small GTPases. Links specifically G alpha q/11-coupled receptors to RHOA activation. May be an important r... |
C1F4E8 | MKMWSGRFREPLDPAFDHWQRSLQFDWQLLPEEVAASKAHALALEAAGVLTAGEREALHNALDLVTSRFHAPDGSGPSWVMSNQEAEDIHHFVELQLVATVGDLGLKLHTGRSRNEQIATDLRLFVRSRAQMLQAYLGTWAEILVARAQQMGNAAMPAYTHLQRAEPVLVAHWLLAYAEMLLRDASRLEDCVRRLNYCPLGSGAVAGATLALDRGIASQALNFAAPTANSMDATSDRDFVLEFLQALTGIALHASRFAEEITLYATAEFGFVDLPEAYSTGSSAMPQKKNPDLTELVRAKVGRINGAAQAVTLLLKGLPL... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 53046
Sequence Length: 486
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subcellular Location: Cytoplasm
EC: 4.3.2.1
|
Q46104 | MKNEMWSGRFSGASDELLKEFNASLNVDKTLFNEDIQGSIAHATMLESCGILKKEELDAIIKGLEQVRSEIEQGKFIFDIKDEDIHMAVEKRLSEIIGSEIGGRLHTARSRNDQVATDFKLFVKKSHIELIKLLKELIQTMLEHAKVHKKTIMPSFTHLQHAQPVSFSFYILAYAFMLMRDIKRLQNSLELADFSPLGSCACAGTSYAINRELSAKILGFKDIMPNAMDGVSDRDFALDLLYDIAVIFTHTSRLCEEMILFSSSEFSFITISDSFSTGSSIMPQKKNPDVCELIRGKTGRVYGNLISLLTIMKALPLAYN... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 51660
Sequence Length: 460
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subcellular Location: Cytoplasm
EC: 4.3.2.1
|
A9WJR8 | MEHRLWGGRFSEPTAAEMRRFNDSFHFDVRLAEVDIAGSIAWAGALLQAGLINETEHADLVRGLELVRAEFANGSFVAAAGDEDIHTAVERRLRELIGDAALKLHTGRSRNDQVATDMRLYTIGIARQLDRRLRDLQLALLAQAEQHTATVMPGYTHLQRAQPITFGHWCLAYVEMFARDRSRLNDAIRRMRVLPLGAGALAGNSLGVERERLTELLDEFDELSANSLDAVSDRDFVAEVLFACALIGVHLSRLAEDVILYASAEFGFLELADAYSTGSSLMPQKKNPDSMELLRGKSGRLLGNLVALLTVLKGLPLTYN... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 51005
Sequence Length: 461
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subcellular Location: Cytoplasm
EC: 4.3.2.1
|
P51464 | MASEGDKLWGGRFVGSIDPIMEMFNSSVSYDQRMWSADIRGSQAYVKALEKAGLVSPTEMEHILTGLDQIHEEWSKGTFVLTKADEDIHTANERRLKELIGEPAGKLHTGRSRNDQVVTDMRLWLRDSCSALHLHLTRLIRTMVDRAAIEIDILFPGYTHMQRAQPIRWSHWILSHAVALCRDAERLGELRKRINVLPLGSGAIAGNPLGVDRELLRKELEFDSVSLNSMDATSERDFIAEFLFWASLCMTHLSKMSEDLIIYSTKEFSFVTLSDSYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCSGFLMTLKGLPST... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 52258
Sequence Length: 467
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
EC: 4.3.2.1
|
Q8TR65 | MSNILRRGRLEAAPDEEILRYASSMETDRWIFSADIAVDLAHTVMLKEQGIISAEDCSKILAGLLKIREEGMEKLDFSYEDIHISLESRLIDMVGEDVGGRMHSGRSRNDEVATCIRLTLREELLGLLEEIFALRKTLVSLAEKHTETLMPGFTHLQHAQPTTLAHHLCAHEAALGRDFDRVQDAFSRVNLCPLGAAAFASTGFNLNRKRTQELLGFEGLLENSMDAVSSRDFLIECASVFSNLMINLSRMAEELVIWSSSEFNFIELDDTYASTSSIMPQKKNPDTAELMRGKTGVAVGALMSLLTICKGLPLSYNRDL... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 54705
Sequence Length: 491
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subcellular Location: Cytoplasm
EC: 4.3.2.1
|
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