ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O29277 | MKKFSRKTEETEVEVVLGEELKVDTGIAFLDHMLKTLSRHSGIKLRVKAKGDLEHHVIEDVAIALGKALAGVDKKGLERFGDAIVPMDDAVAICGLDFSGRGVLVVEGTFGDGEMREEDFLHFLDTLCRNAGLNVYLSVKGSNSHHKMEAAVKAVAISLKKALTKNGNDYRSAKGVLD | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 19335
Sequence Length: 178
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q75B47 | MSETQRAFVKRITHETQVQIALALNGGPLEIGQSILGGAKTTVAHQASSSQVINVQTGVGFLDHMIHALAKHSGWSLIVECVGDLHIDDHHTTEDCGLALGQALREAIGQVRGVKRFGTGFAPLDEALSRAVVDLSNRPYAVVDLGLRREKIGDLSTEMIPHFLQSFAESARVTLHVDCLRGTNDHHRSESAFKAVAVALRDALTRTGTDDVPSTKGVLM | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 23675
Sequence Length: 220
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
EC: 4.2.1.19
|
A1KAV7 | MRHADVTRDTLETRISVRIDLDGTGKSVLATGVPFFDHMLDQIARHGAIDLEVRAEGDTHIDDHHTVEDVGITLGQAFAKALGDKKGILRYGHAYVPLDEALSRVVVDFSGRPGLHYFVDYTRARIGNFDVDLAREFFQGFVNHAGVTLHVDNLRGDNAHHQCETIFKAFGRALRMAATRDERLAGAIPSTKGAL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21516
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q5ZW89 | MKKILFIDRDGTLVEEPFDFQVDSLDKIKLTSGVIPALLQLQKAGFTFIMVSNQNGIGTVAFPEEDFAVCHEFILDLFSSQGILFDEIFICPHTPENNCICRKPKTGLLEPYLKETVFAKQYSWVIGDRDTDKEFADNLGVNFLPISKTHTWEMVASAIINDARKASVQRKTKETTIDLSVQLDSDQTSVIDTPIPFFTHMLEQVAKHGGFDLRLQASGDLEVDEHHLIEDTAIALGEAIRTALGDKWGINRYGYTLPMDESLATIAIDISGRSFCDFKGQFTREFIGGMATEMIPHFFQSLSSALGATIHIEVTGTNHH... | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 39271
Sequence Length: 352
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
P61660 | MTDKLIGFYDPVRMKAERKTSETEIKLEMNLRGTGQYQFDTEIPFFEHMLSHISKHGLIDLNLWLRGDIEIDCHHSVEDTAILMGTTIHKQLGDKAGIFRYGHFTLTMDEVLTTVAVDLGGRYFFKYTGPELTGKFGIYDAELSLEFLQKLALNAKMNLHVVVHYGDNKHHVHESIFKALGKALRMAIAQDSAAAGAIPSTKGVLE | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 23168
Sequence Length: 206
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q2LVF5 | MIMRQASVQRSTSETDISVEIDLDGGGQAVVETSIPFFDHMLTLFSRHGLFNLTVKGRGDTEIDDHHLVEDMGICLGKVVKDAMGDKTGMVRYGSATIPMDETLCAVTLDVSGRPYLVYHVAFSAGARAGEFDLQLIREFFKAFSDHSGITLHINLFYGENNHHIAEAVFKAFARALSMAVSIDSRIQGVLSTKGCL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21560
Sequence Length: 197
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
A0LQG8 | MAGRRQGTVERITSETKIMADLTVDGEGKAELRTGVPFLDHMLSLFSVHGFFDLKLQAEGDLDVDAHHTVEDIGICLGGALAKALGDRKGIRRYGHAVVPMDEACASVTLDLSNRPFLVYRVPTLAARVGRFETELVPEFFRAFCQHGGATVHVQGLYGSNTHHILEAIFKALGRALDQATRFDERRSGIPSSKGTL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21504
Sequence Length: 197
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
Q2JNK3 | MTALDSSRLLQPRTASVHRRTGETDVQIHLNLDGSGRHEIDTGIPFLDHMLAQLSTHGLIDLQIKAIGDLHIDDHHTNEDVGITLGQALAQALQDRRGIHRFGHFWAPLDEALVQVVLDFSGRPHLSYGLELPTERIGRYETQLVREFYQAVVNHAQLTLHIRQAAGLNAHHIVEASFKAFARALRMAVERDPRRQEGIPSSKGVL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 23053
Sequence Length: 206
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplas... |
A5FVN2 | MSGLPTARPAVFSVPPYVGGESRLDGVNRVIKLSSNEGAFGPPPGAIAALTEVAAIAHRYPDGGATSLRAAIGRRFCLDPARIVCGNGSDDLIALLIQSYGGPGTELVMSRHGFLIYEIAARLAGMNVRKAPERNLTADIDAMLAEVTPATRLVFLANPNNPTGSLVPASDVSRLRAELPPDVLLVLDAAYAEYVERADYDPGVELVDSGQNTVMTRTFSKMFGLGGVRLGWAYAPLAIVDVLNRTRMPFNVSGPAAAAGIAALAEPGWVERCRNHNTRARTELAARIERAGFRVWPSEANFLLADLETADRAAAADTHL... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 38702
Sequence Length: 364
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
A1W431 | MTTPSAELPALARIRDDVRAMQAYVVADATGYLKMDAMENPFGLPPALQAALGQRLGQLALNRYPGTRQNDLKAALAAYAGAPAGSAVLLGNGSDELISLVALACARAQATVLAPVPGFVMYAMSAQLQGLGFVGVPLTADFELDEAAMLAAIAQHRPAITFLAYPNNPTATLWDEAVVQRIIDAAGAQGGIVVMDEAYQPFASRSWIERMRAQPERNGHVLLMRTLSKFGLAGVRLGYMIGPAALVAEVDKVRPPYNVSVLNTEAALFALEHADVFAAQADELRAARTELLAALRAMPGIERVWDSQANMVLVRVPDAA... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39090
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
A0KKB7 | MSIANLARRVVRALTPYQSARRIGGKGHVWLNANEAPLAYPFTIEGGRLNRYPECQPAEVVNGYAAYAGVNPDQVLVSRGADEAIELLIRTFCEAGEDQILICPPTYGMYAISAETCGVGIVEQPLTTSRQPDWPAIADRLSDVKLVFLCSPNNPTGDLVGRDGLIALLEKARDRAIVVVDEAYIEFCPEASVVDLLARFPNLVVTRTLSKAFALAGIRCGFTLASPEVIAMLAKVIAPYPIPEPIAQIAAQALSPMGLELMQERVVELNKQKAAFKAALATLHCVKEVFEDKGNFVLVRFVDGAAVFAAMKAAGIILRD... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 38432
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
B2UPR9 | MSIESFANQHVLELVAYQPGKPIEETARELGLNPHDIVKLASNENPLGPSPKAVEAIARAAAGVNIYPDGAAFRLRSAIAEFCGVEFGQTVVGTGSSEVIELICHALLNPRAEVVAAKHAFSMYPIMSKLFGAAYVEVPNKEDWTHDLDGFLAAITENTRVVFITNPTNPVGTVVGQQEIDDFMAKVPEHVLVVFDEAYREFSDNPPDTLKFVREGRNVVVLRTFSKAYGLAGLRVGYGIAPEPVCSMLHKARAPFNLHVLAQEAALAALEDREHVRRTVENNKEGMRFYEQAFREMGLEWIPSQGNFILVKVGRGKQVF... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39996
Sequence Length: 363
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
A8MEH2 | MTTNLFRKELEVLKPYVPGKPIEEVQKEYGIDQIEKLASNENPLGPSPKAVEAIMREVQHINIYPDAYAMKLKEEIAKRTNLTHENIITGNGGEQIIQLIAQTFINPGDEAIMADTTFGLYETSVLNMKGVPVILPLKDYKHDLDGFVEKINENTKIIYICNPNNPVGNILSKEEMEGFVARVPENVVIVLDEAYYDYAKVNPEYPESLDVLAKRPNTVILRTFSKVGGIAGVRVGYALTSKEIASQMSKVKDVFNVNILAQAAALGVLEDTEHIEKTVKLNYESLGMMEKYCEENDLEYIKSNANFMFMNIGTHSKPVF... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41765
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
A7HCR6 | MPLVPPHVASLTPYVPGKPIEEVEREYGVSNVAKLASNENALGPSPLALAAAREACAKVHLYPDGSAYLLRNAIAAKLGVPPEEVMVGNGSNELIELLVRTFVLDGEEVLTSAQSFVAYKLAAHEHGRTLVEAPMKGRFHYDLDALRKLLSRRTKLVFLANPDNPTGTWFTEAELTPFLDAVPKDTLVVLDEAYVEYVDAPGFQDGLALRRKYPNVVVLRTFSKIYGLAGMRLGYGLARPEVVEYVDRVRPPFNTNLVAQAAGAAALGDSAHVAKSRALVLEERPFLAKGLAALGAIVVPSQGNFVLADFPGRTGKDLFE... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39231
Sequence Length: 364
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
B7GHJ8 | MKVKQQLKQLKPYQPGKPIEEVKREYQLETVIKLASNENPYGCSPLVRQAVMNELDDLALYPDGYSRTLREALAAHIGISEKQLIFGNGSDEVVQIICRAFLQKGTNTVMATPTFPQYRHNAIIEGAEVREIPLQDGHHHLEAMLEAIDDHTRVVWICSPNNPTGTYVNDASLRAFLNKVPQHVLVVVDEAYYEYVQAEDYPNTVSLLQQYENMMILRTFSKAYGLAALRIGYGIAHEHLLQAIEPAREPFNTSRLAQAAAFAALKDQTFIQQCAQKNKQGLDQFYAFCDEYGLRYYKSEGNFILIDFGFSGDEVFTYLL... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41993
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q12U08 | MARYELIKDEIGSIAKYVPGRSIEDIVKNYGLEPSSVIKLGSNENPLGPSPKAVEALIANAQGISIYPSADARELVDAISEYTDIPAANIVASGPGMDGLLDGLARLVIANGDEVVITTPTFSYYEIAARANGATTVYVQREKDFSINVDKLLAALTPNTKMIFLCSPNNPTGNVIPEEDILKIATATDALVFVDEAYVEFAEKNIAHLVLQHDNIIVGRTFSKAFGLAGMRMGYGIMPEWLREEYMKIATPFNVSTAAMAAGIAALSDTEHLNKSIELTVKGKKFLQEELPFKVYDTQANFVLVDVAPHKARDVTTELL... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39055
Sequence Length: 360
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
O07131 | MTRLYDFAPSNIRAIAPYQPGKPITELAREMGLKPGVIIKLASNENPLGVSPKAYAAMQDALEDIARYPDGNSFALRDCVCRKFKLQPDQLVFGNGSNDILELAARAFLTPGTEAVYAQHAFAVYALVTQATGASGISVPARDFGHDLDAMLAAITDKTRLFIANPNNPTGTLLSKPALRDFLAKVPRQVLVVLDEAYDEYLAAELKSEAFSWLAEFDNLLISRTLSKAYGLAGLRVGFGVTSPGVADLMNRVRQPFNVNSVAQAAAVAALEDDEFVERSYALNQAGMQQLTEGLARLGLSYIPSYGNFVSFHVAQAAEV... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 40134
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
B3DXN2 | MTNKILSQVKPSLQRLIPYEPGKPIEDLAREYGFSPSQIIKLASNENPLGPSPRALDALGRNLHKIHLYPDGYGYYLKEALSHHLDIDAENIVLGNGSNEIIELLFHVFATNEEDEVLFSKYAFAVYKLMAELFGVPFKEIADVSFNHDLKAMLEAIGPKTKLIFIANPNNPTGTRVSNEDLYLFLERVPDEVIVAIDEAYIDFVPDPPQTLSFVKKRDNIVILRTFSKMYGLAGLRIGYGVASKYVARYLERARQPFNTNSLAQIAATASLEDTQHRLLTLKITEEGKKRLEENFDRLGLPFIPSSANFILVHVGDGDF... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 42180
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q58365 | MGDWMIENKVRDVVKKLKPYVPGKSKEEIARAYGIKPEDIIKLGSNENPWGPSPKIKEKILDEIDKIHQYPEPVNPILMKELSKFLNVDEENIIVGGDGADEIIDTIFRTFVDDGDEVIIPIPTFTQYRVSATIHNAKIKYAKYDKEKDFKLNVESVLNNITDKTKVIFLCTPNNPTGNIIENRDVERVINETDALVVIDHAYIEYAKKEYDWTQKAPEYDNVIVLRTFSKVFGLAGMRVGYGVANKKIIDYMMRVKPIFSLTRLSQVCAITALRDREFFERCVRDGIKSREMLYNGLKKFKDIKVYPSEANYLLVELKT... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 42962
Sequence Length: 373
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
A2SSJ1 | MKPRVRSEFVKSGYVFAKSPADIAKEYGFTEVAMLGSNENPYPPSDKVLRAAEAELSGVNRYPDPKAAAFHAALRTYICDCPVVTSGLGMDGVIETVIRTIVEPGDKVVISTPTFSMYGLAAKAASARVVNVSRSADFSVDLDTFLNEAKDARLSFLCTPNNPTGTVTPVEDIEYILDRIEGVLFLDCAYVEFSDINYLPLLSRDNLIIGRTMSKVYGLAGLRIGYAFVPEWLEAPYNIAATPFTMNRLSEAAASVAVSDAAYRESFIAHVQKWRDVFMQEIPFPVYPSGSNFILINVAPQKGDAAAESLAKHGVLVRSC... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 38283
Sequence Length: 351
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
P61003 | MSIDDKVRSIVKEFKAYVPGKSKEEIARNYGIDPERIIKLGSNENPWGCSPKIEEKLLNEVSNLHQYPQPINPELMDEISKFTKMPVENIIVGGDGADEVIDNIMRILIDEGDEVIIPIPTFTQYAISAKIHGANIKWAKFDEENGFKLDVESVLNNITEKTKAIFLCTPNNPTGNVIPTEDIKKIVESTDALVMIDHAYIEYSKEEYDLTSWALKYDNVLVLRTFSKVFGLAGQRVGYGVTSKKVVDYMMRIKPIFSLTRASQVSAITALQDKEFFEKCLKEGIESREEIYNGLKKFKQLEVYPTEANYMLVKVKNGMN... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 42246
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
P36605 | MFDLNTCLRKNILELQPYRCARDDFSEGVLLDANECAYGSVISVDGVEFNRYPDPRQIEVKQRLCDLRNKELSITKPLTPDNICMGVGSDEIIDSLIRISCIPGKDKILMCPPSYGMYTVSAKINDVEVVKVLLEPDFNLNVDAICETLSKDSAIKVFFACSPGNPTAKALKLEDIKKILEHPTWNGIVVVDEAYIDFSAPDMSALTLVNEYPNLAVCQTLSKSFGLAGIRIGFCLTSKPIATIMNSLKAPYNISEPTSRLALDALSPQSIDKMHTYRDAIIQQRVRLCKELTTIKGMGKIIGGYDANFILIQVLDRPEG... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 42734
Sequence Length: 384
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
A1S6Z2 | MTSQVNAVPTDSLAARLARPELLSLEPYQSARRIGGSGEIWVNANESPFNRTGIDGANRYPECQPPGLIAAYAAYAGVAAHELVCGRGADEAIELLIRTFCVPGQDSIGIFSPTYGMYAISAATFNVAVNTLPLAEDFSLPDDISALTGSKLVFVCNPNNPTGTLLPLGEIARVAKTFPNALVVVDEAYIEFAHNADGSPAQSATSLMAEFENLVILRTLSKAFGLAGARCGFLLAKPSVCELVMRVIAPYPVPVPVSVIAEKALSVMGIAQMRADVVLLNKQGARLALALTEAGLSVLPSGGNYVLAFSNDVEVLARAL... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 38291
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q8EFB2 | MSQEPICQEPMSNVTVRSVPSDNSASNPLDKIVIESATLAARLARPELLELTPYQSARRLGGKGDIWINANESPFNNVAVGELDLTKLNRYPECQPPALINAYSQYSGVVESKIVASRGADEAIELLIRAFCIPGIDSIATFGPTYGMYAISAQTFNVGVKALSLSAEYGLPADFATAARGAKLVFICNPNNPTGTVIDKARIEQAIQALPDSIVVVDEAYIEFCPEYSVADLLETYPNLVVLRTLSKAFALAGARCGFLLANEEIIEIIMRVIAPYPVPLPVSEVAEQALSPAGIARMKTQVKELNTQGERLAAALNLY... | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 42350
Sequence Length: 391
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
P59397 | MPVRLDRSSADFDQRFAAFLAAKREVSADVEAAARAIVDDVARRGDAALLEATAKFDRLTLDASGLRVSAAEIEAAVKACDAATLDALSLARDRIETYHRRQLPKDERFTDPLGVELGWRYTAIESAGLYVPGGTAAYPSSVLMNAVPAKVAGVSRLVMVVPSPDGKLNPLVLAAARLGGVTEIYRVGGAQAVAALAHGTATIAPVAKIVGPGNAYVAAAKRLVFGKVGIDMIAGPSEVLVIADDTGNADWIAADLLAQAEHDTSAQSILITDSARLAADVEKAVEAQLKTLPRTAIASASWADFGAIIMVKNLNDAIPL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 44907
Sequence Length: 431
Pathway: Amino-acid biosynth... |
Q9RQ85 | MHNILEVIYWNKCSYERKKKILSRPIISNRFLIRNKVKEIISNVKSFGDRALYNYTNVFDNINLKNIRVSEEDIVSSHLHVSKELKLAVEVAFKNIKKFHSKQNVGSFNLKVQDNIYCQQIIRPIESIGLYIPNGSAPLLSTVLMLAIPANIAGCKRIMLCSPPPIMNEILYACKICEIKDVFQIGGAQAIAALGCGTETI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 22668
Sequence Length: 201
Pathway: Amino-acid biosynth... |
Q0AB56 | MSDSAFSKDNRWLLPEGVDELLPPRAAQMETLRRQLLDQFGAWGYELVMPPFIEYLDSLLTGTGHDLDVQTFKLTDQLTGRLMGVRADITPQVARIDAHRLRREAPSRLCYIGSVLHARPEGISRSRNPVQVGAELFGHAGVESDIEIISLAVASLRTAGVAQPHLDLGHVGIFRGLARAAGCTPAQEGALLEALQRKAVAEIDELLDEAAIDPHLRRMLRALPQLNGGLEALDHAGEVLAEAPQGVRQALRTLWGVAAGLERRLPDLPLHFDLAELRGYGYHTGIVFAALVPGYGSEVARGGRYDDIGRVFGNPRPATG... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 43257
Sequence Length: 401
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
A6TKS9 | MVLEKVFLPEGVQDLLMKDCHHRRLIEGRLMEEWVKQGYMEVSSPTLEYYDLFRQGEQMLRGNKMFKLIDAKGDLLVLRPDGTLPIARMVATKMKDMVYPLKICYIQDIFRLDQEQAGKQREFRQAGVEVFGVESYEADGQVIITAIESLKALGLSDFQIEIGQTKILQSILDSMAVTTDEKDEIIMLIHNKNFSTLESLLEKLDIDPKTRLILKEIPNLFGTPQGVMESVAALPINDNIKRALEELQQICHMIQAYGFGQYISVDLGMTAPLGYYTGIIFKGFTKDLGTILCSGGRYDRLLMSFGMNCPATGFALLIDQ... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 44829
Sequence Length: 396
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
B4UGX0 | MLDLSLPSGLRDLLPDHSAHLAELSSKLHDVFSRFGYRRVFLPTLERLDVVERGLSPAALADVMKFVEPGSGEVVAIRPDITPQIARLYAARPDALPSPARLCYDGPVLRAREARAGRPREVYQAGVELLGAGGASADAEALVLLARSLERVGLKAPRVEVGHARFAEAVMEAARLPERLRSAAWEALSRKDRAALAAAAAKGRGSAEAREAVPQLAGLFGDGALDRARAIARAVPEAAAPLAETEAALRIARRRGVREVAVDLGEARGLGYYTGITFAGYAPGAGAAVARGGRYDGLLARFGRPGPAIGFAVDLEFATQ... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 36976
Sequence Length: 349
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
O67223 | MKTSLISGERFYSLEESNLVKEIFKKAVKIFEAFGYDYINLSHFEPYEFQELTFGEGSKEAITFKDSYTKESFGLRLDFTTQVVRTISHLRNVKLPERVYYFGKVFSLDRRGFEKLQTGVELIGEKSILADFEVIQVLTEFLKSLGLKDLKVILSHAGIVRKVADEREELLRAFSERNLEALKEVLGNDIKFFVEVSKNPEVLNFLEKYDLEKEKEELLELGKLLEEFGIDYAYDLGEVRNFPYYTGVIFEIYELKSGKALAGGGRYDNLSKIYGKEYPATGGAVYLERLLDILPKNVEKKDYFVIDKTKKRLGLKLADV... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
Sequence Mass (Da): 44349
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose ... |
Q5P7C3 | MRWVLPDHIQDALPAEADKIERLRRRLLDAFRSHGYQLVVPPLLEYLDSLTTGAGQDLKLRTFKLVDQLSGRTMGVRADMTPQVARIDAHLLNRRGVSRLCYCGSVLHTLPSTLTATREPLQLGAELYGHAGLDADIEIIRLLAEVMRLAEVPASRIDLGHVGLFRVLAARAGMVPGREEELFDLLQAKDLPDLHALVAGVAEPVRSALLALPGLYGGAEVLDKARVCLPDDAEIREALDDLSRLAAALGDLPVSFDLADLRGYHYHSGVVFAAYGGGSPAALALGGRYDRVGEAFGRGRPATGFSLDLRELAVRLADVG... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 41427
Sequence Length: 384
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q8CTV2 | MNNTIISMKEKELRFLKFFHQQKYNVVDFNLIEELDWRRLTHEDLQQMDERSFWQQNKSIYALRNDFTDQLFRYYSNYPTHLKKVAYAGDIIRDNRVIKQVGIENYEPQFDNITQNFLDFQYFIQNVLHDDIQFVILGHYQLIDALLEKNHQTREVMEMIEERNLSGLIQKLTFNHPIIQILKENTLNQLKILSHYLPERHPAMVAIQSWAQWFTDHGITEIHLDVTAQAPRSYYKGIFIKCHLKNTTHSVLTGGYYHGSLEGFGLGLTL | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
Sequence Mass (Da): 32171
Sequence Length: 270
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose ... |
Q8DTQ5 | MKKTSLPVGMHDKLFKRARVMYEIERDISNLLIKQGFNRIETPTLEHFEVFADDVSSEHYHLFDKKGNLLSLRPDITSQIGRVIASTRVETPIKFSYSGKVFKYNEELRGLANEHTQAGIEIVGYKTQDAIKDALLSAKDALKASGLKDYKFEFSHAHILQTIFANLDIPETAKKELTTFIQDKNITGLNEFTHRYPSEFNALIRQLPFLFGESHQVLKKARQLTNHQTILSALTDLEDLLQELAVSLAEITLDLAQIASMPYYTGLMFKVFGDKIPDAFVSGGRYDKLFERFGAKELTAIGWALDIDSVYQAIHDHIRF | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 36449
Sequence Length: 320
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q03K76 | MKKTTLALGMHDKLFKRARTMYQIEHCICDLLMTKGFLRIETPTLEHFEVFSDVVDNGNYNFFDKNGDLISLRPDITSQIGRVIASTQVHTPIKFSYSGKVFNYNEEMRGLSNEHTQAGVEIIGFPVHQALEEAVISAKEALDVAGVRNYKFEFSHAQLLQLIFEELNLPAVKEAELATYIRDKSITGLKEFTKENPSQYDKVLEQLPSLFGETTAVLTEARQLTDNESFLTALDSLEVLTSRLADNLPETTLDLAQLPAVPYYTGIMFKVFGDKVPDAFVSGGRYDKLFERFGATELTAVGWAIDIDSVYQAVHDDVEF... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 36634
Sequence Length: 326
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
O30548 | MATVDRWLLPDGIEEVLPPEAARIETARRRVLDLFQRWGYELVITPHVEFLESLLSGSGQDLDLKTFKVIDPLSGRQMGLRADITPQVARVDAHTLRREGPSRLCYAGSVLHAKPRALATSRSPIQLGAELYGDSSTSSDIEVISLMLEMLELAMVPDVHMDLGHVGIYRGLARAAGLSGEAEQRLFDAMQRKAMDEIAELTATVEPSLAAMLQALARLCGGRETLDAARRVLAEAPAPVTEALEALIRIADQLALRYPDLPLYFDLGELRGYHYHTGVVFAVFVPGVGQSIAQGGRYDDIGADFGRARPATGFSTDLKT... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 43071
Sequence Length: 395
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q67KH4 | MSTPVTRTQVPDGVRDRLPSEAAAMRRLSARLDNVFRAWGYREVSTPVIEYLEAVAAGAANWGRREDLYQFFDRKGRTLALRPDMTTPIARLMATRLADEPLPLRLSYFAPVFRHRELRAGATSEIWQAGVELVGAPGEAADAEVISLACAAVRAADLTGFRIGLGHVGVVEGLFESAGVDPQAAAVLKEAMVARDLVAFEQGVARAGLSGERAERLLALVHFHGSYAEAVARFGGVGGRVAEALQHLGRVLEVLEALGVAEQVNLDLGLVRSLGYYTGVVFEGYLPGIGAPVLGGGRYDNLVAEFGRPLAATGFALEVD... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 42441
Sequence Length: 399
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q2JMG5 | MYGRGSGAEHSRGSGAEHFWDPRPEASSTVSSSLRPPSGARDLLPREVQRREKLEAQLTRVFRRHGYQRIITPTLERLETLLAGGSIRAESVLQLRDGEGTMLGLRPEFTASIVRAAATRLAGGPLPLRLYYHGSVFRNSRREEGSYSSQEFFQSGVELIGAGGWLADAEILLLLADCIRSVGISSCEFSWTLLLGDVSLTESLLSAVAPTAQAAVRRAIAQLDYVYLESAPLPEAARQIGLQILGLRGQPGSVLSDLAQLPVPPERLRDLRQLCQVLEEHGVRVVLDLSLLQTLAYYTGIVFQAVASGEIIALGGRYDR... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 47515
Sequence Length: 434
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
A5GL51 | MALQPASGVRDLNPQQVQRNHELREALAAVYRLWGYEEVAPPRIERMDTLKAGGAIDSRDIVRLVADEPLGLRPEMTASIARAACTRFQNRRRPLRLWSHGTVFEGRQADEGGLCIEEKLHCGVELFGARGVEAELELLSLLMASFKALALPLSEPPQLLIGHTGLMQLLLKNVDEQDHPAYRNCLTQLDRLALRELINTQPQHAHLQQWLDRRGAPDAVISQLKDAFPDAPVLQQLTRLINHLSPLAETTGISLQLDPTFQPMYALYDGIVFQLVCRGTSSPVVVARGGRYDTVVQRLGARGKDATGLGFSFCVDDLRD... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 43509
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q8RIA5 | MIIVTGGAGMIGSAFVWKLNEMGIKDILIVDKLRKEDKWLNIRKREYYDWIDKDNLKEWLVCKENADNIEAVIHMGACSATTETDADFLMDNNFGYTKFLWNFCAEKNIKYIYASSAATYGMGELGYNDDVSPEELQKLMPLNKYGYSKKFFDDWAFKQKNQPKQWNGLKFFNVYGPQEYHKGRMASMVFHTYNQYKENGYVKLFKSYKEGFKDGEQLRDFVYVKDVVDIMYFMLVNDVKSGIYNIGTGKARSFMDLSMATMRAASHNDNLDKNEVVKLIEMPEDLQGRYQYFTEAKINKLREIGYTKEMHSLEEGVKDY... | Cofactor: Binds 1 NADP(+) per subunit.
Function: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Catalytic Activity: ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose
Sequence Mass (Da)... |
C4K8I6 | MIIVTGGAGFIGSNIVRALNKIGYQDILVVDNLEKGAKFVNLVDLKIADYRDKDDFITSVRAKEVLGNIEAIFHLGACSSTMEWDGQFMMKNNYEYSKTLLHFCLKACIPFLYASSAAVYGGRTDCFIEEPQYEKPLNIYGYSKFLFDQYVRKIWPKARAPICGFRYFNVYGPRETHKGSMASVVFHLDKQIKAGKPPQLFLGSEQFKRDFIFVDDVAQINLWCWQNQISGIFNCGTGHAASFQTLADTVVAYHNSKPVQYVDFPENLKGCYQTFTQADITKLRTIGYDKPFKPLDEGVTHYLDWLNHQ | Cofactor: Binds 1 NADP(+) per subunit.
Function: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Catalytic Activity: ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose
Sequence Mass (Da)... |
Q9XCA1 | MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLNIADYMDKEDFLIQIMAGEEFGEIEAIFHEGACSSTTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATYGGRTSDFIESREYEQPLNVYGYSKFLFDEYVRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKLFEGSDGFKRDFVYVGDVADVNLWFWENGVSGIFNLGTGRAESFQPVADATLAYHKKGSIEYIPFPDKLKGRYQAFTQADLTNLRKAGYDKPFKTVAEGVTEYMAWLNRDA | Cofactor: Binds 1 NADP(+) per subunit.
Function: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Catalytic Activity: ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose
Sequence Mass (Da)... |
O05074 | MAQYSAEFKQAKVLVLGDVMLDRYWFGATNRISPEAPVPVVRVQENEERAGGAANVAMNIASLNVPVQLMGLIGQDETGSALSLLLEKQKIDCNFVALETHPTITKLRILSRHQQLLRLDFEEDFNNVDCKDLLAKLESAVKNYGALILSDYGKGTLKDVQKMIQIARKANVPVLIDPKGTDFERYRGATLLTPNMSEFEAVVGKCNTEEEIIEKGLKLISDIELTALLVTRSEKGMTLLRPNQEPYHLPTVAKEVFDVTGAGDTVISVLATALADGRSFEESCYLANVAAGIVVGKLGTSTVSTVELENAIHARPETGF... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
O25529 | MKKILVIGDLIADYYLWGKSERLSPEAPVPVLEVQRESKNLGGAANVANNLISLKAKVFLCGVVGDDLEGEHFISALKARGIDASGILIDKTRCTTLKTRIIAQNQQIARVDKEIKDPLNADLRKKLLDFFTEKIQEIDGVILSDYNKGVLDFELTQAMIALANQHHKLILCDPKGKDYSKYSHASLITPNRTELEHALHLKLDSHANLSKALQILKETYHIAMPLVTLSEQGIAFLEKGELVNCPTIAKEVYDVTGAGDTVIASLTLSLLESMSLKDACEFANAAAAVVVGKMGSALASLEEIALILNQTHPKILSLEK... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
Q0C190 | MSSRLSGLLDRAAGKRVLCIGDVMLDRFIYGVVDRISPEAPVPVLRHSREASMPGGAANVARNLASLGLEPVLIGACGDDDAGRELLSIFDQDLSLSVRLVTAKGRPTTLKCRFVAGGHQLLRVDTENVAPVSEATEEELIGILSREAPGSAAILISDYAKGLLTDRLLKAVTKLAADLNIPLIADPKGRDFARYGAVDILKPNAFELSAAVHRSISTDEEAALALREALDTLPAKAIIVTRAARGISYIGQDGNVHHEAGRAREVFDVSGAGDTSLAALATAIAGGGTLSDAVHLAIAASGIAVGKAGTATVSAEEIKA... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
Q93NH4 | MYDAIVVGGGFSGLKAARDLTNAGKKVLLLEGGERLGGRAYSRESRNVPGLRVEIGGAYLHRKHHPRLAAELDRYGIPTAAASEFTSFRHRLGPTAVDQAFPIPGSEAVAVEAATYTLLRDAHRIDLEKGLENQDLEDLDIPLNEYVDKLDLPPVSRQFLLAWAWNMLGQPADQASALWMLQLVAAHHYSILGVVLSLDEVFSNGSADLVDAMSQEIPEIRLQTVVTGIDQSGDVVNVTVKDGHAFQAHSVIVATPMNTWRRIVFTPALPERRRSVIEEGHGGQGLKILIHVRGAEAGIECVGDGIFPTLYDYCEVSESE... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in the degradation of L-nicotine . Catalyzes the oxidation of (S)-6-hydroxynicotine (6-hydroxy-L-nicotine) to 6-hydroxypseudooxynicotine . Oxidation of the pyrrolidine ring of (S)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylm... |
A0A075BSX9 | MTEKIYDAIVVGAGFSGLVAARELSAQGRSVLIIEARHRLGGRTHVVNFLGRPVEIGGAGVHWCQPHVFAEMQRYGFGFKEAPLADLDKAYMVFADGQKIDVPPATFDEEYTTAFEKFCSRSRELFPRPYSPLDNHEVSNLDGVSARDHLESLGLNELQLASMNAELTLYGGAPTTELSYPSFVKFHALASWDTITFTDSEKRYHVQGGTNALCQAIFDDCRADSEFGVPVEAVAQTDNGVTVTLADKRVFRALTCVLTLPTKVYADVRFEPPLPPEKRAFIEHAEMADGAELYVHVRQNLGNTFTFCDDPNPFNAVQTY... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in the degradation of L-nicotine . Catalyzes the oxidation of (S)-6-hydroxynicotine (6-hydroxy-L-nicotine) to 6-hydroxypseudooxynicotine . Oxidation of the pyrrolidine ring of (S)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylm... |
Q9Y5L2 | MKHVLNLYLLGVVLTLLSIFVRVMESLEGLLESPSPGTSWTTRSQLANTEPTKGLPDHPSRSM | Function: Increases intracellular lipid accumulation. Stimulates expression of cytokines including IL6, MIF and VEGFA. Enhances cell growth and proliferation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6950
Sequence Length: 63
Subcellular Location: Lipid droplet
|
Q9JLS0 | MKFMLNLYVLGIMLTLLSIFVRVMESLGGLLESPLPGSSWITRGQLANTQPPKGLPDHPSRGVQ | Function: Increases intracellular lipid accumulation. Stimulates expression of cytokines including IL6, MIF and VEGFA. Enhances cell growth and proliferation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7007
Sequence Length: 64
Subcellular Location: Lipid droplet
|
P33389 | MDRRRFLTLLGSAGLTATVATAGTAKAASTGTFPGYKDSYGVLHDTTRCIGCRKCEQACNEVNKLPAPKAKFDDLTVLEKTRRTDADSWTVVNRYNAAGLDHPVFRKQQCNHCLEPACASACFVKAFTKNPDGSVTYDGSLCVGCRYCMVACPFNVPAFQYAEAFDPLIQKCTMCHPRLAEGKLPGCVEICPKEALTFGRRKDLVRIAHDRIRQNPGRYIDHVYGEQEMGGTAWMYLSGVPFSATGMNEELGTKSAPEYTAGALGAVPMVVGIWPILLTGAYAITKRKEKIAAEEQAEAVKQAVAASRAEADDKLKAALA... | Function: HMWC (high-molecular-weight cytochrome c precursor), ORF2, ORF3, ORF4, ORF5, ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates. ORF2 is a transmembrane redox protein.
Location To... |
P33390 | MQHANTNKSLMTPGNIITGIILVMGLVLTVLRFTKGIGAVSNLDDNNPWGIWIGFDLLCGVALAAGGYVTSASCYLFGMKRYHSAVRPAITTAFLGYFFVVVALNYDLGHPLRLPYPLVYSQGTTSLLFEVGLCVATYLTVLFVEWSPAALEWLGLRKIRNVVVKLTLVLTIFGVVLSTLHQSSLGALFLIAPSKLHPLWYSSFLPVFFFISSMVAGLSMVIFEGSLAHKGMHHMMDETHLKEADGVVFGFGKAASFVLAGYFMIKVIDVTMDNDWHYLATGYGAWWLVEMLGFVALPSFLYALGVREKRIGVIRFASVL... | Function: HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates.
Location Topology: Multi-pass membrane protein
Sequence M... |
P33391 | MDQAIYTLHEFMLHTKNWTYILMGVTLLVYVGYWLFLTGRDEKIRKY | Function: HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates.
Location Topology: Single-pass membrane protein
Sequence ... |
P33392 | MYAFLTGPMLWASLLVFFGGLLARVIWYIRGLDWRLDRVAYKPHLAIGLQGAVQSALKWLVPFGTYSWRQQPFFTVAFFLFHIGAVLVPLFLAGHNVILEERFGFSLPALPMGVADTLTVLAIIGLVMIALRRIALTEVRILTTGYDWFILAVSAAPFVTGFLARLHVGDYDTWLLAHIITGELFLIVAPFTKLSHIVLFFMSRGQLGMDYAIKRGGATRGPAFPW | Function: HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates.
Location Topology: Multi-pass membrane protein
Sequence M... |
Q96FZ2 | MCGRTSCHLPRDVLTRACAYQDRRGQQRLPEWRDPDKYCPSYNKSPQSNSPVLLSRLHFEKDADSSERIIAPMRWGLVPSWFKESDPSKLQFNTTNCRSDTVMEKRSFKVPLGKGRRCVVLADGFYEWQRCQGTNQRQPYFIYFPQIKTEKSGSIGAADSPENWEKVWDNWRLLTMAGIFDCWEPPEGGDVLYSYTIITVDSCKGLSDIHHRMPAILDGEEAVSKWLDFGEVSTQEALKLIHPTENITFHAVSSVVNNSRNNTPECLAPVDLVVKKELRASGSSQRMLQWLATKSPKKEDSKTPQKEESDVPQWSSQFLQ... | Function: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites . Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: form... |
Q8R1M0 | MCGRTSCHLPREVLTRACAYQDRQGRRRLPQWRDPDKYCPSYNKSPQSSSPVLLSRLHFEKDADSSDRIIIPMRWGLVPSWFKESDPSKLQFNTTNCRSDTIMEKQSFKVPLGKGRRCVVLADGFYEWQRCQGTNQRQPYFIYFPQIKTEKSGGNDASDSSDNKEKVWDNWRLLTMAGIFDCWEAPGGECLYSYSIITVDSCRGLSDIHSRMPAILDGEEAVSKWLDFGEVATQEALKLIHPIDNITFHPVSPVVNNSRNNTPECLAPADLLVKKEPKANGSSQRMMQWLATKSPKKEVPDSPKKDASGLPQWSSQFLQK... | Function: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites (By similarity). Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link... |
Q6IND6 | MCGRTACTLAPDDVSKACSYQDKQGRQKCPKWRDGDTDKYQPSYNKSPQSNNPVLLSLKHFQKDADSSERVLAAMRWGLIPSWFNELDPSKMQYKTNNCRSDTITEKALYKAPLFKGRRCVVLADGFYEWKRQDGEKQPYYIYFPQIKSEKFPEEQDMMDWNGQRLLTMAGLFDCWEPPSGGEPLYSYTVITVDSSKTMNCIHDRMPAILDGDEAIRKWLDFGEVSTQDALKLIHPIENITYHPVSTVVNNSRNNSTECIAAVILTQKKGPALSASSKKMLEWLQNKSPKKEESRSIIQSPKLSQFGAPPKKTSAGLMQQ... | Function: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms... |
P54961 | MWPSDVGIVALELIFPSQYVDQVDLEVYDNVSAGKYTVGLGQARMGFCTDREDINSLCLTVVSRLMERWSIPYSQIGRLEVGTETLLDKSKSVKTVLMQLFKDNTDIEGVDTVNACYGGTSALFNAISWVESSSWDGRYALVVAGDIAVYAKGSARPTGGAGAVAMLVGANAPLVFDRGVRSSHMQHAYDFYKPDLSSLYPTVDGKLSIQCYLSALDHCYQLYCSKIQKQLGEKFDIERLDAVLFHAPYCKLVQKSLARLVLNDFVRASEEERTTKYSSLEALKGVKLEDTYFDREVEKAVMTYSKNMFEEKTKPSLLLA... | Function: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+)
Sequence Mass (Da): 50332
Sequence Length: 453
Pathway: Metabolic intermediate biosynthes... |
P05114 | MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD | Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6K... |
P18608 | MPKRKVSADGAAKAEPKRRSARLSAKPAPAKVDAKPKKAAGKDKASDKKVQIKGKRGAKGKQADVADQQTTELPAENGETENQSPASEEEKEAKSD | Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6K... |
P02313 | MPKRKAEGDAEGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKDGNNPAENGDAKTDQAQKAEGAGDAK | Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
PTM: Phosphorylation favors cytoplasmic localization.
Sequence Mass (Da):... |
P05204 | MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK | Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
PTM: Phosphorylation favors cytoplasmic localization.
Sequence Mass (Da):... |
P09602 | MPKRKAEGDAKGDKTKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKDANNPAENGDAKTDQAQKAEGAGDAK | Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
PTM: Phosphorylation favors cytoplasmic localization.
Sequence Mass (Da):... |
Q5RAA0 | MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADADKEGNNPAENGDAKTDQAQKAEGAGDAK | Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
PTM: Phosphorylation favors cytoplasmic localization.
Sequence Mass (Da):... |
P18437 | MPKRNAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKDANNPAEDGDAKTDQAQKADGAGDAK | Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
PTM: Phosphorylation favors cytoplasmic localization.
Sequence Mass (Da):... |
P82970 | MPKRKAAGQGDMRQEPKRRSARLSAMLVPVTPEVKPKRTSSSRKMKTKSDMMEENIDTSAQAVAETKQEAVVEEDYNENAKNGEAKITEAPASEKEIVEVKEENIEDATEKGGEKKEAVAAEVKNEEEDQKEDEEDQNEEKGEAGKEDKDEKGEEDGKEDKNGNEKGEDAKEKEDGKKGEDGKGNGEDGKEKGEDEKEEEDRKETGDGKENEDGKEKGDKKEGKDVKVKEDEKEREDGKEDEGGNEEEAGKEKEDLKEEEEGKEEDEIKEDDGKKEEPQSIV | Function: Preferentially binds to euchromatin and modulates cellular transcription by counteracting linker histone-mediated chromatin compaction.
Sequence Mass (Da): 31525
Sequence Length: 282
Domain: Specifically targeted by its C-terminus to nucleosomes in euchromatin.
Subcellular Location: Nucleus
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Q9XXQ9 | MVAVEFKVSESGRPRPEKNPKLGFFVYLLGSAAIIGGFLFGYDTSVVSAAMLYVPEAPGLKPMGTVWKEVIVSITPGMAAVGAWFSGAGSDRYGRKPIIIGSTLIFVCGAVICAVAWTKIVMLIGRIFLGVGIGFASMVVPVYLGEASPTHVRGTLVSAFAMMISFGQVVANIMGGVFSYWEPYTIGWRLMFAFAGIPALIQFVCFIFLPETPRWLYENGHTEQAEQVLEKIYGGNTEWIEYELAEIKTYAEERQKQMEEEKKSGPVIWRILKTPHVLKACFIGSMLQAFQQLAGINTILYYTADIIRSAGIENYHTIIW... | Function: H(+)-myo-inositol cotransporter (By similarity). Probably by promoting the transport of myo-inositol regulates intracellular osmosis in response to hyperosmotic stress .
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass... |
Q21455 | MVQVAPVAAGAGSGQTRPSSDPKTGWFVYMLAFSAVIGGFLFGYDTGIVSAAMLYVPNASGIKPLDSVWQEIIVSITPGVAAIGSLCSGPGSDFLGRKKIIIGASVTFTIGAIICAAAWTKIILLIGRILLGLAIGFASMIVPIYVSEASPSHIRGKLVTGFQLMITVGLVIANIIGGAFSYVDPDQVGWRLMFAFAAVPAIIQFVCFLFLPESPRWLYEHGRTVEAREVLTRIYNGHTEWVDYEINEISFSYEEELRAKAEHAGNGPTIIRILKTPHVRKAMIIGSLLQMFQQLSGINTVMYYTGNIIRSAGVKDNHTT... | Function: H(+)-myo-inositol cotransporter.
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66562
Sequence Length: 604
Subcellular Location: Cell membrane
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Q9SDL7 | MVLEKKSALLEDLIKKCGGCAVVDGGFATQLEIHGAAINDPLWSAVSLIKNPELIKRVHMEYLEAGADIVVTSSYQATIPGFLSRGLSIEESESLLQKSVELAVEARDRFWEKVSKVSGHSYNRALVAASIGSYGAYLADGSEYSGHYGENVSLDKLKDFHRRRLQVLVEAGPDLLAFETIPNKLEAQACVELLEEEKVQIPAWICFTSVDGEKAPSGESFEECLEPLNKSNNIYAVGINCAPPQFIENLIRKFAKLTKKAIVVYPNSGEVWDGKAKQWLPSQCFGDDEFEMFATKWRDLGAKLIGGCCRTTPSTINAIS... | Function: Catalyzes methyl transfer from S-methylmethionine (SMM) to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level.
Catalytic Activity: L-homocysteine +... |
G5EFD4 | MGFSPFLDECRAEGLWPIGPSCNKIISFGVYTFFIVVNFIVLCIPNSNSANNNYRRMTDDDASSTSKLTISKILSICTIFAVICQSIFYFCFTFYFHPYTHLLLAFCVSKLFFWILSLCSFSKWRNQPSTPISLAFAFSAALLIHCIPLTDWKKYFEPTSKNRGDLTFYIIELALVTVVFFFTIVTGLFNFSGCSSRESAWNNLSKKVVTVAPYIWPTKSISLQLRVVFCLFLLIIGRLINVSLPILSKWIVDELATPDTFQYSLLFLATFLKFLQGNGAMGGFLNTVRTYLWIPIQQYTTRELEVELFKHLHSLSLRWH... | Function: May play a pivotal role in the detoxification of heavy metals such as cadmium but do not depend exclusively on phytochelatins (PC) synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90575
Sequence Length: 801
Subcellular Location: Vacuole membrane
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Q02592 | MVLRYNSPRLNILELVLLYVGFFSIGSLNLLQKRKATSDPYRRKNRFGKEPIGIISWWILGIALTYVVDISNLVIYALRVPNWWPCKTTVVCLILFLLFWIIVLISCADSKALPKNADSILKAYRLSVLYVWAIDIVFETIFIVYSPHPNETFQGIVLADHVARLVLCVFATAIYLTYRRKRHTHDPLDFEERQLTEESNVNENAISQNPSTVQLGVSASTSNFGTLKSTSKKPSDKSWAEYFRSFSTLLPYLWPTKDYRLQFQIFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQGNMGV... | Function: Involved in metal tolerance. Probably involved in the transport of metal-bound phytochelatins. Compartmentalizes cadmium within vacuoles, thereby protecting cells from cadmium toxicity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93994
Sequence Length: 830
Subcellular Location: Vacuole ... |
P38074 | MSKTAVKDSATEKTKLSESEQHYFNSYDHYGIHEEMLQDTVRTLSYRNAIIQNKDLFKDKIVLDVGCGTGILSMFAAKHGAKHVIGVDMSSIIEMAKELVELNGFSDKITLLRGKLEDVHLPFPKVDIIISEWMGYFLLYESMMDTVLYARDHYLVEGGLIFPDKCSIHLAGLEDSQYKDEKLNYWQDVYGFDYSPFVPLVLHEPIVDTVERNNVNTTSDKLIEFDLNTVKISDLAFKSNFKLTAKRQDMINGIVTWFDIVFPAPKGKRPVEFSTGPHAPYTHWKQTIFYFPDDLDAETGDTIEGELVCSPNEKNNRDLN... | Function: S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that catalyzes both the mono- and asymmetric (type I) dimethylation of the guanidino nitrogens of arginine residues in a variety of RNA-binding proteins such as heterogeneous nuclear ribonucleoproteins (hnRNPs) and small nuclear ribonucleo... |
Q9M1W4 | MTGNSFNSMKDFLKQTGGYAVIDGGLATEFERHGADLNDPLWSAKCLVTSPHLIHTVHLDYLEAGADIISSASYQATIQGFEAKGFSREESESLLKKSVEIATEARNSYYDKCGTSSSMDDKILKKRPILVAASVGSYGAYLADGSEYSGIYGDSITLEKLKDFHRRRLQVLAESGADLIAFETIPNKIEAQAFADLLEEGDVKIPGWFSFNSKDGVNVVSGDSIKECISIAENCEKVVAVGINCTPPRFIEGLVLEIEKVTSKPILVYPNSGESYDADRKEWVENTGVGDEDFVSYVEKWMDAGVSLLGGCCRTTPTTI... | Function: Catalyzes methyl transfer from S-methylmethionine (SMM) to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level.
Catalytic Activity: L-homocysteine +... |
Q9FUM9 | MVVTAAGSAEEAVRRWVDAAGGRLVLDGGLATELEANGADLNDPLWSAKCLLSSPHLIRKVHMDYLEAGANIIITASYQATIQGFESKGFSKEQSENLLTKSVEIALEAREMFLKEHLEKSTPIQHPVLVAASLGSYGAYLADGSEYSGDYGEAGTKEFLKDFHRRRLQVLAEAGPDLIAFETIPNKLEAEAYVELLEECNINIPAWFSFNSKDGVHIVSGDSLIECTTIADKCAKVGAVGINCTPPRFIHGLILSIRKVTDKPILIYPNSGERYDGEKKEWVESTGVSDGDFVSYVNEWCKDGAVLIGGCCRTTPNTIR... | Function: Catalyzes methyl transfer from S-methylmethionine (SMM) to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2, HMT-3 and HMT-4) and biosynthesis (by MMT1) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level (By similarity).
Catalytic Act... |
O94284 | MLTLNSTIKSVTGSFQSASMLARFASTHHKVLVVGGGSAGISVAHQIYNKFSKYRFANDQGKDTSLKPGEIGIVDGAKYHYYQPGWTLTGAGLSSVAKTRRELASLVPADKFKLHPEFVKSLHPRENKIVTQSGQEISYDYLVMAAGIYTDFGRIKGLTEALDDPNTPVVTIYSEKYADAVYPWIEKTKSGNAIFTQPSGVLKCAGAPQKIMWMAEDYWRRHKVRSNIDVSFYTGMPTLFSVKRYSDALLRQNEQLHRNVKINYKDELVEVKGSERKAVFKNLNDGSLFERPFDLLHAVPSMRSHEFIAKSDLADKSGFV... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone.
Sequence Mass (Da): 51575
Sequence Length: 459
Subcellular Location: Mitochondrion
EC: 1.8.5.-
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Q8LAX0 | MGSFVKEETSSLMTDFLEKCGGYAVVDGGFATELQRHGADINDPLWSAKCLITSPHLVTKVHLDYLESGANIIITASYQATIQGFVAKGLSVGEAENLLRRSVEITYEAREIFYNRCTKGSWDFAYAGKASRRPILVAASVGSYGAYLADGSEYSGIYGDSVSKETLKDFHRRRVQILAKSGADLIAFETIPNKLEAEAYADLLEEEDIDIPAWFSFTSKDGVSVPRGDSVVECAKVADSCKNVVAIGINCTAPRYIHALIISLRQMTRKPIVVYPNSGEVYDGLNKKWIKSEGESEEDFVSYVSKWRDAGASLFGGCCR... | Function: Catalyzes methyl transfer from S-methylmethionine (SMM) to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level.
Catalytic Activity: L-homocysteine +... |
Q9FUM7 | MWFGGGPIDAAGALRGFVREAGGCAVVDGGLGTELEAHGADLHDALWSAKCLASAPHLIRKVHLDYLEAGADVIISASYQATIEGFQSRGFSRDESEELLRRSVHVAQEARRVFAAEGDRSSRRGRPPALVAASVGSYGAYRADGSEYSGDYGKSMTKEDLKNFHRRRLQVLAGAGPDLIAFETIPNKLEAQVYAELLEENGIRIPAWFSFTSKDGVNAASGDPINECAAVADSCPRVDAVGVNCTAPRFIHGLILSIKKVTSKPIVVYPNSGETYVAETNEWVDSDGATGTDDFVSRVGEWRRAGAALIGGCCRTSPAT... | Function: Catalyzes methyl transfer from S-methylmethionine (SMM) to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2, HMT-3 and HMT-4) and biosynthesis (by MMT1) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level (By similarity).
Catalytic Act... |
Q9EST2 | MASSMRSLFSDHGRYFEAFRRFLNNSTEYQCMREFMDKQLPGIIARIGGSKSEIKVLSIGGGAGEMDLHILSKVKAQYPGVHIINEVVEPSAEQITKYKELVAKTSNLENIKFAWHKETSSEYQNRVMEQKEIQKWDFIHMIQMLYYVDDIPATLKFFHSLLATNAKILIILVSGKSGWLKFWKKYRSRLPQNDLCQYVTSFDIIQMLDSLGIKYQCYDLLSTMDITDCFIDGNENGELLWDFLTETCNFLTTAPPDLRAEIMKDLQGPEFIVRKEGKILFDNSLSFITIEA | Function: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
Catalytic Activity: histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33712
Sequence Length: 292
Subcellu... |
Q6DC37 | MAAPFKTLVEDYPRYLKSFELFLERSSEHQCMQDFIHNTLPDILASIGGGRSVFNVMGVGSGAGDIDLEMLAQLHLKHPHVKVDNEVVEPSNDMLYKYKARVSTSPDLAYINFTWNKMTASEFEKQWQEKTPEKKMDFIHMIQMLYYVKDPNATVSFFRSLLEKDGKLLIILVSGESGWGKLWTTFRKQLCYTEMSQCVTIGEIKSFLDSEGVPYRKYVLLSQMDITECFTEGDQEGELLLDFLTEVKEFSKNAPERLKKEVLDVLRHPDCSKEVDGRIIFNNNLEVLVIEP | Function: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
Catalytic Activity: histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33619
Sequence Length: 292
Subcellu... |
P50135 | MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRIGDTKSEIKILSIGGGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTSNLENVKFAWHKETSSEYQSRMLEKKELQKWDFIHMIQMLYYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWDKLWKKYGSRFPQDDLCQYITSDDLTQMLDNLGLKYECYDLLSTMDISDCFIDGNENGDLLWDFLTETCNFNATAPPDLRAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA | Function: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
Catalytic Activity: histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33295
Sequence Length: 292
Subcellu... |
Q4SBY6 | MASAMRSLIEDDSRYLKSFKLFLERSTEHQCVQEFIHNVLPDILGSVGKGKTHLNVIGVGSGAGEVDLEILSELHSRHPGASVDNEVVEPSAQQLQDYKALVLQKKDLDYISFNWNKMTATEFEERWRANKMSKEADFIHMIQMLYYVKDPEATTSFFQSLLSKTGKLLIILVSGNSGWGKLWKTYKNQFCNPEISQCVTTADIQSFLDSKGARYQSFELPSQMDITECFTQGDEKGELLLDFLTEVLEFSKTASPELRAEVMELLRHPDCSVESNGRVMFNNNLGVIVLD | Function: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
Catalytic Activity: histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32938
Sequence Length: 291
Subcellu... |
O14979 | MEVPPRLSHVPPPLFPSAPATLASRSLSHWRPRPPRQLAPLLPSLAPSSARQGARRAQRHVTAQQPSRLAGGAAIKGGRRRRPDLFRRHFKSSSIQRSAAAAAATRTARQHPPADSSVTMEDMNEYSNIEEFAEGSKINASKNQQDDGKMFIGGLSWDTSKKDLTEYLSRFGEVVDCTIKTDPVTGRSRGFGFVLFKDAASVDKVLELKEHKLDGKLIDPKRAKALKGKEPPKKVFVGGLSPDTSEEQIKEYFGAFGEIENIELPMDTKTNERRGFCFITYTDEEPVKKLLESRYHQIGSGKCEIKVAQPKEVYRQQQQQ... | Function: Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high a... |
P31943 | MMLGTEGGEGFVVKVRGLPWSCSADEVQRFFSDCKIQNGAQGIRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNNVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYNGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSTFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPVRVHIE... | Function: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with ... |
Q51983 | MFDTRKKIYVSDVTLRDGMHAVRHQYSLADAERIARALDEAGVDSIEVAHGDGLQGSSFNYGFGAHTDLEWIERVAATVRRAKIATLLLPGIGTVHDLKNANAAGASVVRVATHCTEADISQQHIEYARKLGMDTVGFLMMSHMTTPTALAVEAKKMESYGAQCIYVVDSGGAMNMYDIADRFKALKDVLDPSTQTGMHAHHNLSLGVANSIVALEYGCDRIDASLTGMGAGAGNAPLEVFIAAVDRMGLKHGCDVRKLIDAAEEIVRPLQERPVRVDRETLALGYAGVYSSFLRHTEAAAHKYGLDAFEILVELGRRRM... | Function: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of p-cumate.
Catalytic Activity: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
Sequence Mass (Da): 38059
Sequence Length: 350
Pathway: Aromatic c... |
Q9X9Q0 | MSQEAARDAAAGRPVQIHDPTLRDGQHAVRHSLGAEQFRAYLKAADAAAVPVVEVGHGNGLAASSLQVGRARLSDDEMMSIARETLTTSKLGVLMFPGWATTQDIKNALAYEVDLVRIATHCTEASVAERHLGFLRDEGVEAHGMVVMTHMASPDQLAEECARLVGYGATGVGILDSSGHFLPSDVTARIGAICAAVDVPVMFHGHNNLGMAVANSIAAAQAGAGILDACARGFGAGAGNTQLEVLVPVLERLGFRTGIDLYRLLDAADIAGRELMPAPPTIDSVSIVSGLAGVFSGFKKPVLDIAAREGVDPRDIFFEL... | Function: Involved in the biosynthesis of the peptidyl nucleoside antibiotic nikkomycin.
Catalytic Activity: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
Sequence Mass (Da): 37146
Sequence Length: 357
EC: 4.1.3.39
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Q53WI0 | MSWDLSTAKPPVVVDTTLRDGSHAHRHQYTVEEARAIAQALDEAGVYAIEVSHGDGLGGSSLQYGFSRTDEMELIRAVRETVRRAKVAALLLPGIGTRKELKEAVEAGIQMVRIATQCTEADISEQHFGMAKEMGLEAVGFLMMSHMRPPEFLAEQARLMEGYGADVVYIVDSAGAMLPEDAYARVKALKEALSRAKVGFHAHNNLGLAIGNTLAALAAGADWVDATLRGYGAGAGNAPLEVLAAVLDKAGLNPGLDVFKLLDAAEYVMGPILHFQPYPDRDSVAIGYAGVYSTFLLHAKRIGKELGVDPLAILLELGRR... | Cofactor: Divalent metal cation. Has the highest activity with Co(2+) as cofactor, followed by Ni(2+) and Mn(2+). Mg(2+) and Ca(2+) are very poor metal cofactors.
Function: Catalyzes the retro-aldol cleavage of both 4-hydroxy-2-oxopentanoate (HOPA) and 4-hydroxy-2-oxohexanoate (HOHA) to pyruvate and acetaldehyde or pro... |
Q38134 | MKTFFKDMAERAIKTFAQAMIGALGAGATGLIGVDWLQALSIAGFATVVSILTSLASGIPGDNTASLVNNKKEGE | Function: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis. Participates with the ... |
Q6XQ99 | MKEFLTAATSSTGGASLVGAATGQLYIAGATFICFLLFGAWGAYWKYRDSKAIQEALNDGDLNKALKIRGR | Function: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of nanometer-scale pores (pinholes) causing host cell membrane depolarization and endolysin refolding and release into the periplasmic space (By similarity). Once the pinholin has permeabil... |
P10307 | MLSLDFNNELIKAAPIVGTGVADVSARRFFGLSLNEWFYVARIAYTVVXIGAKVVDKIIDWKKATKE | Function: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Participates in determining the precise timing of host cell lysis. Parti... |
P06808 | MAAPRISFSPSDILFGVLDRLFKDNATGKVLASRVAVVILLFIMAIVWYRGDSFFEYYKQSKYETYSEIIEKERTARFESVALEQLQIVHISSEADFSAVYSFRPKNLNYFVDIIAYEGKLPSTISEKSLGGYPVDKTMDEYTVHLNGRHYYSNSKFAFLPTKKPTPEINYMYSCPYFNLDNIYAGTITMYWYRNDHISNDRLESICAQAARILGRAK | Function: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space . Determines the precise timing of host cell lysis . Regulated by specifi... |
Q6R6U4 | MVLVRGGYKLEKFLQLLTVLLQEAKDPASLLKRLLTILVAVIIFLFVSNTSEVMSFLKTFSTSAVLQDVQTQRIDNFPNVAREKSMVLFSQTGADAVFVVKYKPDAINDYSNIIAWESNAQLDRADLADKAVNKTSELYRRHLEGFNYASDLTVKVNKYMGKNIPSFKNVIFNYIYTCPYFNLNNIYAGYIGIAWRDKPVDIADSEQFKEYLTKLCSPQQRSLGRSI | Function: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis. Regulated by specific ... |
P03705 | MKMPEKHDLLAAILAAKEQGIGAILAFAMAYLRGRYNGGAFTKTVIDATMCAIIAWFIRDLLDFAGLSSNLAYITSVFIGYIGTDSIGSLIKRFAAKKAGVEDGRNQ | Function: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space . Determines the precise timing of host cell lysis . Participates with th... |
Q9Z2Y3 | MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPTQNALPFPHSAGDRTQALSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELNQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDL... | Function: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM... |
Q9Z214 | MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPAQNALPFSHSAGDRTQGLSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELSQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSEL... | Function: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM... |
Q9NSB8 | MGEQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRANTVFGLGFSSEQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR... | Function: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM... |
Q9NSC5 | MSTAREQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQHLTQFAEKFQEVKEAARLAREKSQDGGELTSPALGLASHQVPPSPLVSANGPGEEKLFRSQSADAPGPTERERLKKMLSEGSVGEVQWEAEFFALQDSNNKLAGALREANAAAAQWRQQLEAQRAEAERLRQRVAELEAQAASEVTPTGEKEGLGQGQSLEQLEALVQTKDQEIQTLKSQTGGPREALEAAEREETQQKVQDLETRNAELEHQLRAMERSLEE... | Function: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. Isoforms can be dif... |
Q2FIN9 | MIRFEIHGDNLTITDAIRNYIEEKIGKLERYFNDVPNAVAHVKVKTYSNSATKIEVTIPLKNVTLRAEERNDDLYAGIDLINNKLERQVRKYKTRINRKSRDRGDQEVFVAELQEMQETQVDNDAYDDNEIEIIRSKEFSLKPMDSEEAVLQMNLLGHDFFVFTDRETDGTSIVYRRKDGKYGLIQTSEQ | Function: Required and sufficient for dimerization of active 70S ribosomes into 100S ribosomes. 110S ribosomes are probably translationally inactive and may serve as a reservoir of easily reactivated ribosomes when necessary in the cell. Also reduces the translation efficiency of a small number of genes. Unlike E.coli,... |
Q4WPV8 | MTVSKKVEENIFASKLGPEYVGFDHITWYVGNAKQAASYYVTRMGFKQIAYRGPETGSRSVVSHVISNGQAIFVLTSPIRSMAGTGAYDDDPDVTKADRRLLEEIHNHLIKHGDGVKDVAFRIEGDIEAVWKRAVDHGAAPVAAPTTLKDDRHGSITLATIGTYEDTVHSLINRHDYSGPFLPGYEVVTDDDPINRLLPSIDFIEIDHCVGNQPWNGVDPIVKYYEDCLNFHRYWTVDDLNMCGEYSAMRSIVVASPNEVIKMPMNEPAQGKKKSQIEEFVNYYNGAGVQHIAFRTHDIVTAVTRLRERGVSFLEVPSAY... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 45776
Sequence Length: 406
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
P93836 | MGHQNAAVSENQNHDDGAASSPGFKLVGFSKFVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTL... | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 48816
Sequence Length: 445
Pathway: Amino-acid degradat... |
Q22633 | MTTFDKGAKPDIGTFVAFDHVRFVVGNAKQAAYWYCANFGFEPFAYKGLETGSRITAQHAIRQDKIVFIFESALLPDNSELGNHLVQHGDGVKDVCFEVEDLDSIIAHAKAAGATIVHDITEESDADGSIRYATLRTYGETDHTLLERKNYRGAFLPGFKAHPMPATFFKTLPRVGLNFLDHCVGNQPDLQMDSAVQWYEKVLKFHRFWSVDDSMIHTEYSALRSIVVTNFEETIKMPINEPATSDKKAISQIQEYVDYYGGSGVQHIALNTSDIITAIEALRARGCEFLSIPSSYYDNLKERLAASSMVVKEDMDRLQK... | Cofactor: Binds 1 Fe cation per subunit.
Function: Key enzyme in the degradation of tyrosine.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 44383
Sequence Length: 393
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylala... |
Q1E803 | MAPAADSPTLQPAQPSDLNQYRGYDHVHWYVGNAKQAATYYVTRMGFERVAYRGLETGSKAVASHVVRNGNITFILTSPLRSVEQASRFPEDEALLKEIHAHLERHGDGVKDVAFEVDCVESVFSAAVRNGAEVVSDVRTVEDEDGQIKMATIRTYGETTHTLIERSGYRGGFMPGYRMESNVDATSKFLPKVVLERIDHCVGNQDWDEMERVCDYYEKILGFHRFWSVDDKDICTEFSALKSIVMASPNDIVKMPINEPAKGKKQSQIEEYVDFYNGAGVQHIALRTNNIIDAITNLKARGTEFIKVPETYYEDMKIRL... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 45290
Sequence Length: 399
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
Q6TGZ5 | MTSYTDKGEKPERGKFLNFHHIKFWVGNAKQAAVFYCDKFGFEPLAYKGLETGSREVVSHAVRQDKIIFVFESALNPGNEEMGEHMIKHGDGVKDVAFLVEDCDFLVKKAKERGAAVLKEPWVEQDAGGKVKYAIVQTYGDTTHTFVEYLGPYKGLFLPGYKEPLFRDPLLPKLPSGHLSFIDHIVGNQPDDEMVPVSDWYQKCLLFHRFWSIDDKQIHTEYSALRSIVVTNYEETIKMPINEPAMGKKKSQIQEYIDYNGGPGVQHIALNTSNIIQAIVNLRARGLEFLSAPDNYYESLREKLKTAKIKVKEDLKTLQE... | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45211
Se... |
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