ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9Y6M0 | MGARGALLLALLLARAGLRKPESQEAAPLSGPCGRRVITSRIVGGEDAELGRWPWQGSLRLWDSHVCGVSLLSHRWALTAAHCFETYSDLSDPSGWMVQFGQLTSMPSFWSLQAYYTRYFVSNIYLSPRYLGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEALPSPHTLQEVQVAIINNSMCNHLFLKYSFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQKLMAQSGMSQPDPSWPLLFFPLLWALPLLGPV | Function: Could regulate proteolytic events associated with testicular germ cell maturation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 34884
Sequence Length: 314
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q9JHJ7 | MGARGKTLVPLLVVVATAAMALQSTYLQVDPEKPELQEPDLLSGPCGHRTIPSRIVGGDDAELGRWPWQGSLRVWGNHLCGATLLNRRWVLTAAHCFQKDNDPFDWTVQFGELTSRPSLWNLQAYSNRYQIEDIFLSPKYSEQYPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIGEDESLPSPNTLQEVQVAIINNSMCNHMYKKPDFRTNIWGDMVCAGTPEGGKDACFGDSGGPLACDQDTVWYQVGVVSWGIGCGRPNRPGVYTNISHHYNWIQSTMIRNGLLRPDPVPLLLFLTLAWASSLLRPA | Function: Could regulate proteolytic events associated with testicular germ cell maturation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36175
Sequence Length: 324
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q90YH9 | MDLESKVKKMGLGHEQGFGAPCLKCKDKCEGFELHFWRKICRNCKCGQEEHDVLTSNEEDRKVGKLFEDTKYTTLIAKLKNDGIPMYKRNVMILTNPVPAKKNISINTVTYEWAPPVQNQTLARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPNEVKQMEQFVKKYKNEALGVGDVKLPGELETKATDKNNVNSGDRSTSAAVGAMEDKSADQKASQYSCYRCKLNMKEGDPAVYAERAGYDKLWHPACFVCCTCSELLVDMIYFWKNGNLYCGRHYCDSEKPRCAGCDELIFSNEYTQAEGQNWHLKHFCCFDCDCVLAGEIYVMVNDKPVCRPCYVKKHAAICQGCHNAIDPEVQRVTYNNFNWHATQECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKKMMS | Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. May play a role in the regulation of cell proliferation. May inhibit cell growth (By similarity).
Sequence Mass (Da): 47983
Sequence Length: 422
Domain: The N-terminal and the C-terminal halves of the protein can associate with each other, thereby hindering interactions with other proteins.
Subcellular Location: Cytoplasm
|
Q2TBQ0 | MASSRTLGTFRLPPLPTIREIIKLFRLQAVKQLSQNFLLDLRLTDKIVRKAGNLTNAYVYEVGPGPGGITRSILNAGVAELLVVEKDSRFIPGLQMLSDAAPGKLRIVHGDVLTFKIERAFPESLKRQWEDDPPNVHIIGNLPFSVSTPLIIKWLENVSQRNGPFAYGRTRMMLTFQKEVAERLTATTGSKQRSRLSIMAQYLCDVQHILTIPGQAFVPKPEVDSGVVHFTPLTRPRIKQPFKLVEKVVQNAFQFRRKYCHRGLGMLFPEARRLESTGKLLELADVDPTLRPTQLTVSHFKSLCDVYRKMCDEDPHLFAYNFREELRQKSKKEDDKQSCRL | Function: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity (By similarity).
Sequence Mass (Da): 38883
Sequence Length: 341
Subcellular Location: Mitochondrion
EC: 2.1.1.-
|
P91424 | MASASRLPPLPALRDFIHMYRLRAKKILSQNYLMDMNITRKIAKHAKVIEKDWVIEIGPGPGGITRAILEAGASRLDVVEIDNRFIPPLQHLAEAADSRMFIHHQDALRTEIGDIWKNETARPESVDWHDSNLPAMHVIGNLPFNIASPLIIKYLRDMSYRRGVWQYGRVPLTLTFQLEVAKRLCSPIACDTRSRISIMSQYVAEPKMVFQISGSCFVPRPQVDVGVVRFVPRKTPLVNTSFEVLEKVCRQVFHYRQKYVTKGLKTLYPEELEDELSDDLLKKCRIDPTTTSIRLGIEQFADLAEGYNEQCIRYPGLFLYDYTNKLHNLEDLSKEPNALPPPVPIFAPAPTIDSADNTWSLKNFNCS | Function: Probable S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA. Stimulates transcription independently of the methyltransferase activity (By similarity).
Sequence Mass (Da): 41893
Sequence Length: 367
Subcellular Location: Mitochondrion
EC: 2.1.1.-
|
Q9VTM5 | MAQPSARVLQSGMRLPPMPTIRELVKLYRLQARKQLSQNFLMDERLTDKIVKSAGRIDPRDLVLEVGPGPGGITRSILRRHPQRLLLVEKDPRFGETLQLLKECASPLNIQFDIHYDDILRFNIEQHIPDTSQRIHLIGNLPFAISTRLLINWLDDLAARRGAFRRIDTCMTLTFQQEVAERICAPVGGEQRCRLSVMSQVWTEPVMKFTIPGKAFVPKPQVDVGVVKLIPLKRPKTQLPFHLVERVVRHIFSMRQKYCRRGYGTLLPPEDREEVAEKLFQRAEVQDTLRPFELTVEQCLRLAEVYSEHLVTRPEVAAYDYRAPKNVEVL | Function: Probable S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. In contrast to mtTFB2, it does not have a critical role in either transcription or regulation of the copy number of mitochondrial DNA.
Sequence Mass (Da): 38101
Sequence Length: 330
Subcellular Location: Mitochondrion
EC: 2.1.1.-
|
Q8WVM0 | MAASGKLSTCRLPPLPTIREIIKLLRLQAAKQLSQNFLLDLRLTDKIVRKAGNLTNAYVYEVGPGPGGITRSILNADVAELLVVEKDTRFIPGLQMLSDAAPGKLRIVHGDVLTFKVEKAFSESLKRPWEDDPPNVHIIGNLPFSVSTPLIIKWLENISCRDGPFVYGRTQMTLTFQKEVAERLAANTGSKQRSRLSVMAQYLCNVRHIFTIPGQAFVPKPEVDVGVVHFTPLIQPKIEQPFKLVEKVVQNVFQFRRKYCHRGLRMLFPEAQRLESTGRLLELADIDPTLRPRQLSISHFKSLCDVYRKMCDEDPQLFAYNFREELKRRKSKNEEKEEDDAENYRL | Function: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity.
Sequence Mass (Da): 39543
Sequence Length: 346
Subcellular Location: Mitochondrion
EC: 2.1.1.-
|
Q8JZM0 | MAASGKLGTFRLPPLPTIREIIKLFGLRAVKQLSQNFLLDLRLTDKIVRKAGSLADVYVYEVGPGPGGITRSILNANVAELLVVEKDTRFIPGLQMLSDAAPGKLRIVHGDVLTYKIEKAFPGNIRRQWEDDPPNVHIIGNLPFSVSTPLIIKWLENISLKDGPFVYGRTKMTLTFQKEVAERLVATTGSKQHSRLSIMAQYLCNVEHLFTIPGKAFVPKPKVDVGVVHLTPLIEPKIKQPFKLVEKVVQNAFQFRRKYCHRGLGMLFPEAQRLESTGRLLQLADIDPTLRPTHLSLMHFKSLCDVYRKMCDEDPQLFTYNFREELKQKKSKGQEKDGDPESCGF | Function: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity (By similarity).
Sequence Mass (Da): 38962
Sequence Length: 345
Subcellular Location: Mitochondrion
EC: 2.1.1.-
|
Q1A705 | MTMRLPPLPTIGELIRLFGLSAKQQLSQNFLLDLNITDKIVRSSGDLTNKTVIEVGPGPGGLTRSILKAGAKKLVVIEKDRRFLPALEVLRHAAGNIDGSPWEEAFLTKSEMDAKRYMSYAPNKSRMQIVMNDVLRVDEQEILQHIHAPIDSNDKTQWENMAPITIIGNLPFAISTELTIKWLKQIQGRHGAFRFGRAEFILMFQKEVADRLIANPGTKQYSRLTVMTQQLCSVKKLSDIPGSAFVPKPDVDASLVSMVPRVTPLGVNVPTPTLEYVCRQVFGQRRKMINNSVKTLGPEAEILLARAHIDPTLRPEQLTVPQWCDLARAYQQWENKPQWAPAL | Function: Probable S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA. Stimulates transcription independently of the methyltransferase activity (By similarity).
Sequence Mass (Da): 38523
Sequence Length: 343
Subcellular Location: Mitochondrion
EC: 2.1.1.-
|
Q08315 | MVKSTVPTRPNKYWPGVVAIGLVSLFIFLSVSNQKHSTTSGDNIHKFSNGGTYRDGSKCITYNRNSPLAYNGSSSNNTLFWLCLLGLSMVWIAYCGYKSLSGQWHSCQHDKNERNFLFECFE | Function: Participates in the transport of viral genome to neighboring plant cells directly through plasmodesmata, without any budding . TGBp2 and TGBp3 are necessary for intracellular delivery of TGBp1-containing vRNPs to plasmodesmata (By similarity). Can gate plasmodesmata and increase their size exclusion limit (By similarity). To a lesser extent than TGB3, induces host actin cytoskeleton network thickening, which probably plays a major role in virus cell-to-cell movement (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13771
Sequence Length: 122
Subcellular Location: Host cell junction
|
Q9IV53 | MVRNNEIGARPNKYWPVVAAVVAICLFGFLTVTNQKHATQSGDNIHKFANGGQYRDGSKSIKYNCNNPRAYNGSSSNITFSQLFLPVLLIGAALYAYLWFTRPDCSVTCRGDCCRSYGG | Function: Participates in the transport of viral genome to neighboring plant cells directly through plasmodesmata, without any budding. TGBp2 and TGBp3 are necessary for intracellular delivery of TGBp1-containing vRNPs to plasmodesmata. Can gate plasmodesmata and increase their size exclusion limit. To a lesser extent than TGB3, induces host actin cytoskeleton network thickening, which probably plays a major role in virus cell-to-cell movement (By similarity). Binds ssRNA in a sequence non-specific manner .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13123
Sequence Length: 119
Subcellular Location: Host cell junction
|
Q05187 | MYGFGRGNMFRNRSTRYRRRPRYRAENYHSYMLDLLENMNEEFGRNWWGTPESHQPDSGPSSLQVESVELYTRDNAREHNTFMYDLVDGTKPVLILRRGQPFSIAIRFKRNYNPQQDRLKLEIGFGQQPLITKGTLIMLPVSGSDTFTKDKTQWDVRLRQHDGAVITLEIQIPAAVAVGVWKMKIVSQLTSEEQPNVSAVTHECKNKTYILFNPWCKQDSVYMEDEQWRKEYVLSDVGKIFTGSFKQPVGRRWIFGQFTDSVLPACMLILERSGLDYTARSNPIKVVRAISAMVNNIDDEGVLEGRWQEPYDDGVAPWMWTGSSAILEKYLKTRGVPVKYGQCWVFAGVANTVSRALGIPSRTVTNYDSAHDTDDTLTIDKWFDKNGDKIEDATSDSIWNFHVWNDCWMARPDLPTGYGGWQAYDSTPQETSEGVYQTGPASVLAVQRGEIGYMFDSPFVFSEVNADVVHWQEDDSSETGYKKLKIDSYRVGRLLLTKKIGVDDDFGDADAEDITDQYKNKEGTDEERMSVLNAARSSGFNYAFNLPSPEKEDVYFNLLDIEKIKIGQPFHVTVNIENQSSETRRVSAVLSASSIYYTGITGRKIKRENGNFSLQPHQKEVLSIEVTPDEYLEKLVDYAMIKLYAIATVKETQQTWSEEDDFMVEKPNLELEIRGNLQVGTAFVLAISLTNPLKRVLDNCFFTIEAPGVTGAFRVTNRDIQPEEVAVHTVRLIPQKPGPRKIVATFSSRQLIQVVGSKQVEVLD | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
Catalytic Activity: L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 86996
Sequence Length: 764
Subcellular Location: Membrane
EC: 2.3.2.13
|
Q6F9F5 | MSEMDAVNKIRELRDAFGSFMTGVTVVTTCKDDGTPLGFTANSFASVSLDPALLLVSIAKTSSNYHNFADASHFAINILAEEQKDVSNIFARPSDDRFAQLVWAKSEYQNPLIDGVSAWFDCTTYQVVDAGDHAILIGKVENFTSAGFAGLGYYRGAYFTPAKSSTDVISSMKVMMMALIGHENKILLEQTADHKWALPHLMVEKDGAEKALEKIFATYQPEASPSFIYSVYDDVTTQQQYIAFLCNTPVPTAHKGQFVDLNDLEKLTFTDSALQSMLMRYRKENYLKTYGVYYGNHTSGTVRQIVKEGV | Function: Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. TgnA catalyzes the reduction of flavin (FMN or FAD) by NADH and supplies the reduced flavin to the oxygenase component TgnB.
Catalytic Activity: a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) + NADH
Sequence Mass (Da): 34415
Sequence Length: 310
EC: 1.5.1.36
|
Q6F9F6 | MRFSLFVHMERVSDQQTQKQLYDEMIELCQIADRGGMHAIWTGEHHAMNFTIAPNPFLNIADLANKTKHVRLGTGTVVAPFWHPIKLAGEAAMTDIISNGRLDIGIARGAYSFEYERMVPGMDAWSAGQRLREMIPAIKNLWKGDYEHNGEFWQFPKTTSAPQPLQQPNPPIWVAARDPNSHEFAVQNGCNVQVTPLHLGDEEVEKLMGHFNSACEKFQDIERPEIMLLRHTYVADSEEDAQVAANEMNVFYNYFGAWFKNEREINQGLIAPLSDEEIAAHPFYTPEAMRKNNVIGQAQEVIDRLKAYEAMGYDEYSFWIDTGMSFERKKASLERMINEVMPAFSESKVDRRHATISAVY | Function: Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. Catalyzes the insertion of two oxygens, followed by a ring cleavage of trigonelline to yield (Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone (MFMB). It is able to use reduced FMN or FAD.
Catalytic Activity: FMNH2 + N-methylnicotinate + O2 = (Z)-2-((N-methylformamido)methylene)-5-hydroxybutanolactone + FMN + H(+)
Sequence Mass (Da): 41152
Sequence Length: 360
EC: 1.14.14.-
|
Q6F9F7 | MQQFQLYINGKFEDGAAQFDSINPATGEIWAKMPEARTDQVNRAVDAAEQAFYDSSWSGLTASQRGKLLYKLADLVEKSAPRLAALETTDTGKIIRETSSQIAYVAEYYRYYAGLADKIEGSFIPVDKPDMQAWLVREPVGVVAAIVPWNSQLFLSAVKVGPALAAGCTVVLKASEEAPAPLLEFAKLIDEAGFPAGVVNVITGFGPECGAVLSAHPKVAHIAFTGGPETAKHIVRNSAENLAKVSLELGGKSPFIVFADTDINSALNAQIAAIFAATGQSCVAGSRLLIEESIKDEFLQRLAERVQSIKMGLPDDMQTEYGPLCTLKQREKIQQVVQRSVEQGAKLITGGQVCDGAGYYYPPTILDCSGVSDAQSIHTELFGPVLSVDTFSTEAEAIQKANSTPYGLASGVFTSNLTRAHRMTRAIRSGIVWLNTYRVVSPLAPFGGYGLSGHGREGGLSAALEYTTTKTVWLRMSDQPIDDPFVMR | Function: Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. Catalyzes the NAD(+)-dependent oxidation of (Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone (MFMB) to yield (E)-2-((N-methylformamido)methylene)succinate (MFMS).
Catalytic Activity: (Z)-2-((N-methylformamido)methylene)-5-hydroxybutanolactone + H2O + NAD(+) = (E)-2-((N-methylformamido) methylene)succinate + 3 H(+) + NADH
Sequence Mass (Da): 52515
Sequence Length: 488
EC: 1.2.1.-
|
Q6F9F4 | MISKTLQLSNNRTAHYFEQGEGEPLVLIHGVGMQAEAWYPQIEYFSKHYHVISLDMPGHGQSTALAADAQLQDFVDWAIECIHTLNLGPVNLAGHSMGSLITTGVSVTRPDLVKRMAVLNGVYKRTHAAREAVIQRAEALKQGHLDIETPLQRWFGQSEIEKIASERVKLWLENVNMSGYTTAYRAFAQGDLVYADGWSDIECPALVLTGTDDPNSTAEMTIQMAHQAKHGTAIVIENERHMVNLTAPEKVNQAMQAWLETTP | Function: Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. Catalyzes the hydrolysis of (E)-2-((N-methylformamido)methylene)succinate (MFMS) into formic acid, succinate semialdehyde (SSA), methylamine and carbon dioxide.
Catalytic Activity: (E)-2-((N-methylformamido) methylene)succinate + H(+) + 2 H2O = CO2 + formate + methylamine + succinate semialdehyde
Sequence Mass (Da): 29206
Sequence Length: 263
EC: 3.5.1.-
|
Q62313 | MRFQVALLLLSVAVARALPSVYKRDADSGDSQNPPNQPSKQSSTPLPSSNQVKTTRPTDGQGQKSDKKDQDKTTLAAVSSKAESGPRTAATDHSLGDSRRQPEKTDAELNETARPLSPVNPKLEKSDQSSTEDSGKPTGGNSGKPTGGDSGKPTEAGSNKATEDDSGKSTKVDLDKPTSKISPDTETSKTDKVQPTEKGQKPTLTSKTESGETLAGDSDFSLKPEKGDKSSEPTEDVETKEIEEGDTEPEEGSPLEEENEKVPGPSSSENQEGTLTDSMKNEKDDLYKDSSGNTSAESSHFFAYLVTAAVLVAVLYIAYHNKRKIIAFALEGKRSKVTRRPKASDYQRLNLKL | Function: May be involved in regulating membrane traffic to and from trans-Golgi network.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37848
Sequence Length: 353
Subcellular Location: Cell membrane
|
O43493 | MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAEDDDTGPEEGSPPKEEKEKMSGSASSENREGTLSDSTGSEKDDLYPNGSGNGSAESSHFFAYLVTAAILVAVLYIAHHNKRKIIAFVLEGKRSKVTRRPKASDYQRLDQKS | Function: May be involved in regulating membrane traffic to and from trans-Golgi network.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 45880
Sequence Length: 437
Subcellular Location: Cell membrane
|
O43952 | MTDQGVAKEQYITVGSLKEIADPVKKFLRKGNRKGRNQKELKFRAKVVNQQLADETGSINFTTEGVAVNNNQTYEFTGSLKVVDYKLNLAVTSATPAKDQIANLGSEQLSKADIDQHSGKHIVLIKDLINLRIGQSFFARPKDIVHNNEQRRMTATLADNTAAIQAEISVNKKSITQEVLESLNSDKVYLFSDVVLNFNESNKLVARFNYRSNIVEANDRQIQQLSNNNLSAKEYSDETEKKALTDVLQIHEKKERVHKQQNKNKNPRNAHKNHNRQRPNLQETEPVKISGLQQWNNNQTVIGKIVSLRTEDKSLPAKQDGTSTTMVYLKGTIGDETGVIDFDMAEKRDCPRFKENDVVKFTSVMNKGRQSAEGKVGGHYIEVKKFGQYIILSDHNINNVNLNNNLSNLELTARPKNPNPRFIKGEFVGVKEEEKDGNIQYTYTVRSKEGEEQSITIRNKITTLKVGEIHKIDRERKRSSSRPNHQGGQRGNRSHSQNNRNQRNRDKHHNSQNNQPNKYKNTSVQNNNNNKNQQRSQSQNQRPPRNYDNRQGGENRNNRQRNENNRNNFNGNGHRVNNQNNQRNRNSSYPRNNNYDHHHNQQTDISGLEPGKRGQNVTGQVIEVSEFSKQINDKTLHFVKGRIADENANIRFDIKKPQNLEIKVGEVYNFKDVNNKVDDNGYHYIDLNRFGRVFPSHKKFQSINDKRNCDADRSSIEYVKKTVPN | Function: Binds specifically to parallel G4-DNA, a four-stranded structure stabilized by tetrads of hydrogen-bonded guanines.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 83212
Sequence Length: 725
Subcellular Location: Nucleus
|
Q9HZX3 | MNAIPRVALVWLLVAQVLVILPHLAYMPLWIAAMWLGCAAWRVQVFRMRAGYPRAWVKLALALLAGAGVWLSRGSLVGLDAGAVLLIAAFILKLVEMKTRRDALVLVFLGFFAVVVGYLFDDGFLAALYSLLPVTALLAALIGLQQSAFASRPWPTLRLAGGLLLQALPLMLLLFLFFPRLGPLWSLPMPGNKGVTGLSESMAPGDIAELGRSAELAFRVRFEGALPPREQLYWRALTMERFDGRRWAQAPQWSGEDALHWQKRGPELRYDVIMQPSSQPWLFALDVAQTDQTDTRLMSDFHLQRRQPVEQRLFYRVSSWPQALRESSIDPRTRWRNLQLPMHGNPRARALADELRQAHAQPQALVAALLQRFNHEPFAYTLKPPATGADGVDDFLFDTRSGFCAHYAGAMAFVLRAAGIPARVVAGYQGGELNPAGNYLLVHQFDAHAWVEYWQPEQGWLSVDPTYQVAPERIEQGLEQALAGDSEYLADAPLSPLRYRGLPWLNDMRLAWDSLNYGWQRWVLAYQGEQQGAFLQRWFGGLDPTRLGLLLGAAAILSVGLLALFLLKPWQGRGDLRSRQLRRFERLLEMHGLRRSPGEGLRSYGERAARVLPAQAPAIAAFVGAFEAQRYGHGGADDPGLRLRALRRALPWRLVRTPTRDGRGEEQA | Function: Displays transglutaminase activity (TGase) in vitro. Plays a critical role in the viability of P.aeruginosa. Might contribute to an essential function linked to the cell wall.
Catalytic Activity: L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74807
Sequence Length: 668
Domain: The transglutaminase activity is contained within the periplasmic domain (180-544).
Subcellular Location: Cell inner membrane
EC: 2.3.2.13
|
H3BV60 | MLGTVLLLALLPGITTLPSGPPAPPFPAAPGPWLRRPLFSLKLSDTEDVFPRRAGPLEVPADSRVFVQAALARPSPRWGLALHRCSVTPSSRPAPGPALALLREGCPADTSVAFPPPPPPSPGAARPARFSFRLRPVFNASVQFLHCQLSRCRRLRGVRRAPAPLTPPPPPPPSRCLPQDEACADTGSGSAEGLAADGPHLHTLTQPIVVTVPRPPPRPPKSVPGRAVRPEPPAPAPAALEPAPVVALVLAAFVLGAALAAGLGLVCAHSAPHAPGPPARASPSGPQPRRSQ | Function: Expressed in gonadotrope cells, acts as an inhibin B coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility.
PTM: Glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30175
Sequence Length: 292
Subcellular Location: Cell membrane
|
Q54V07 | MKVIYIYLLLLLVCKFLFVKSSCSLKVGKIECTKELETFLLYNETVVNVKMDTNGVKYYFNALEFPYKNLLCDLNIDIKFTPEIPSFPNIPTTGGDFGFTFNFPCDYRRRVKRIEIERTILSLSFDTSKNQFVTYLNPGCGPFNISSSGIQILSTTYETGAIPNVPILDDDKGILTIQGSNLYNTSIKIYSNNILKDTNPSGALDASHSSVTFSAEEFLTPNNWTIEVSICGSFYKSYSFPYFPKLDKMEGVLNDNGGNMVFTGKHLRPKHNVTGTFGNKTIECLTSNSSKSITCTIPSRKNYGFLGYDIPVTITIDGEYKSNTIKISYDLPLIQSVSQRGNSQIFDVTGVYFSGVKNMTVITGKNMKTDIIQKKTATLEEPGFFIESNYTIFIFLPNNTQPGFMNLVVGDGGSETFTSPRYNFKITPTITAGQTFNSTTSGNDLEIKGIFMRTVDSDGRDVPLTVNSGSGGLVCNPLKDGDGLLFTCVLGPGFGSSHTMNVYYNLIPIGSFTVSYNPPYLGTSEQEKDGTIKMNGKDLGESVKDSIMTVVYSDGNTVNGTVIKSSHTSLIFRYPIGNRNTASYIFQLGDQKSNKAGPFTLKPIIENTDPAVPCGGGVVTINGHYFFNYTKDTTTITIGKVPCNISSISETTIECVIVPNLRSLSPYYTSGTKPLVISSSNPGTEKVYQLTPAGLNYKFAPPTITNTSAIDQTALITIYGTSFGDANLEILINDKPCTQPEINIHTYSSLTCNVTNYDEMKIYNYSNTKFNISISVDGQYFIADIFQFKYESGIIYSENKSTGFPNEMYLGFVVFVIFIALISFAAKNQIEKYFEERKSRKAFRSLDNLRLKLRQKHATEIAKHYTFGEQSAPKPDKSTFYDIRKKLSRLPLIRRCFKEHTD | Function: tgrB1 and tgrC1 are involved in kin discrimination. They play an essential role in aggregation and subsequent development.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 100319
Sequence Length: 902
Subcellular Location: Cell membrane
|
P42523 | MEKKIILLILFLFFISGYSMNPPTPIDAIYDDKSFTLIFNSNLPYSTRLILYKNEKEPRTEMAPNYFNCSLVDGERHCLFHSDEPFSRLWGSIDSKVCVRDKSNTVEDCTFDASGLVYYPKVYNLKYSKKPKTSGEDIVITGSYLRLFGGPNFLINSIDVNKPFVVKGNFSDPSFDCNNITVTFPPGSGKFRLYYDETGDNPVPFSYESPIISSSVSDSSKQIITINGDNFFTDKDLVKVSFDGIDQPNFIISVNHKQIQVNNYNRVDPGPMSVNITVDEVSIEKNYIHCFPAIITSISSVSNHLDGIVTIKGEKLSSTLNSSLTPSITIGDKVCKFIKSTTTELECKLDANELGGKNLPVNVNFGGCDSTSPNGVSFTYNIPTLSSGSYSNGIVTLIGTNLGTNNESSIQLYGDGIKNTNISQFNVSSSDEKSVTFELPHLRCRSFNINFTRSGITAKTLSISASLSVNVINRPTVSNGILNIEIYYMDCTISSSAPSITVGDSSSASPCSIPSSNSSYYETTCPTPYGTGINKQFIFKLNSETVSDQFSYAPPEVENRTISDDGTNIELHGNNFGNSTSLIKVYLNGSDISSEIQELEDHQLTIKILDSYENGPINITVDGNYMDSLFYLTLPPVIYRITNKDNKTLACGGLITVSGKNLLTSDKEFKVNVKSNNKNTTVFAQDEKILIVRDESRESSLFVTTFIGVRSGPSTTLTYIKPMISEIPTIENKIEKGILAIIRGYSFTDILNASLTVSSETVPLSCNLECSLSPNEILDDSDSSETNITNSNTDCLSCHSGSSVKNTSGVLYLLFNSTSFQYNVTIEEIKLSPSPNVSQRDVETKSSKPSNGLIIGSTIGSVGGALAIGALAYYFKIPFRVKKFIGKKF | Function: tgrB1 and tgrC1 are involved in kin discrimination. They play an essential role in aggregation and subsequent development. Could function as a non-diffusible cell-cell signaling molecule that is required for multicellular development. Has both cell-autonomous and non-cell-autonomous functions. Terminal node, epistatic both to comC and tgrD1. Activates tgrD1.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 97443
Sequence Length: 889
Subcellular Location: Cell membrane
|
P84026 | EKFPAVNQKPQAAXL | Function: Binds to thrombin and inhibits blood coagulant activity. Does not inhibit the serine protease activity of thrombin or platelet aggregation activity. May bind to the heparin recognition exosite.
PTM: Glycosylated.
Sequence Mass (Da): 1652
Sequence Length: 15
Subcellular Location: Secreted
|
P82354 | ECENTECPRACPGEYEFDEDGCNTCVCKGCDDAQCRCSSDANGCESFCTCNTRCSAADECNPRCTCK | Function: Potent thrombin-specific inhibitor.
PTM: Eight disulfide bonds are present.
Sequence Mass (Da): 7257
Sequence Length: 67
Subcellular Location: Secreted
|
P10828 | MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED | Function: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.
Sequence Mass (Da): 52788
Sequence Length: 461
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
|
Q24FB1 | MKKILIGLIIGLFLFSSVNASVNLTEVQNAISIQQGINWAEVHNNTWYYPPYLGEMFISEYYFELLVLNWTHKSAFNATYFTERLLQTQFEDGSWEQVREQNLETGQLDATVFNYWYLKSINNNPKIEAALQKARKWIVAQGGIEATQTMTKFKLAAFGQYSWEDLWYVPLFIFKQNGIFKYTYVKDIVAQWVYPHLTALAYLRYQRTVFNVPVADLRELWINYPKNGIKISPREYSTLNPDSDLLILMDEIFKLKQPLGSFGAYTISTLLTLMSFKDFQSKHPHLYQNEIQKAYEDGYYFVEFNYFNFREAYHGSLDDGRWWDTILISWAMLESGQDKERIFPIVQNMVKEGLQPKKGIGYGYDFEYAPDTDDTGLLLVVMSYYKEAFQKQIPETIEWLFSMQNDDGGYPAFDKGKNEDNLLFKFAFNMAGIANSAEIFDPSCPDITGHIMEGLGEFGYQANHPQIQNMIKYQRKTQNKWGSWQARWGVNYIMAVGAVVPGLARVNYDLNEQWVQNSINYLLNKQNKDGGFGECVLSYNDPEKWNGIGKSTVTQTSWGLLALLEVYNQNEQIKHAADRAAQYLLDQFKRDDNTFYDHSTIGTGHRGLLYLQYPSYAQSFPLVALNRYQKISQGQYHFSKNLYNGNGEPVQKQNI | Function: Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into tetrahymanol, a triterpenoid sterol with five cyclohexyl rings that is involved in membrane integrity, permeability and fluidity.
Catalytic Activity: tetrahymanol = H2O + squalene
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76021
Sequence Length: 655
Subcellular Location: Membrane
EC: 4.2.1.123
|
Q9UT18 | MPSSQISHQDPELGQTSSGSSSIKEKAEPQLYAGPIDPARRPDVFQEGFEDVSVTDDDNDNELLRKMGYQPVLHRSFEFFESFAASFASLDVVSGVRLTFSWGISFGGPAAYWSAMLVTGFCSIVTAACLAEICSALPAAGSIYLWAAESAGPRFGRFVSFLVAWWSTTAWTTFVASITQSTANFIFAEVSTFNNPWPTNDSDVKFRAVQWIVAEVLLVFTILLNQVPPRYYKWIFKASMLLMFIDYVMNIIWVPVATSKKPDGFRSAKWVFTETIYDQAGYIKEVDDANGNPIASLSKIVPKGWQWCLSYFATAGVIVGYDASGHIAEETKDASIKAARGIFYSTVTSFIVAFSLAILYLFCCPDLDTFTAILYNDNSPQPFVNFYSYLLGRGGHVVMNVVIILEIFLNGVVSVLACSRLVFAVSRDGVLPFSNWISQVSKTGQPKNAITVIYIVSALLLCTILPSAVAFTSLVSAAGAPSFAAYAVLAFCRLFITRDKFPKGRWSLGWLSKPCLVITLVYNLFALVVNVSPYTYPVTGPSFNYAVVIMGGVSIFAIICTIVIPKSRWVANRYRYESDSEHSASVKELKV | Function: Thiamine transporter involved in the cellular uptake of thiamine. Pyrithiamine, oxythiamine, amprolium, and the thiazole part of thiamine have been shown to be also substrates of thi9.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65070
Sequence Length: 591
Subcellular Location: Endoplasmic reticulum membrane
|
Q8Q0F4 | MTLMEDAKKGVITPEIEAVAKAEGIDAEIVRSCVAKGLVAIPKNARRDTLPVGIGKYMSTKINANVGTSRDCIDIDAEIEKAKAAEAFGAHAVMDLSTGGDLDEIRTRILKAVNIPVGTVPIYQAAASRKIVVEMSSDDMFNAVRKHAEQGVDFVTVHAGVNLNSLERLRQSDRIMNVVSRGGSFTLAWMLHNGEDNPFYAEFDYLLEIAKEYDMTLSLGDGMRPGCIADASDRPKFMEFITLGELVKRSREANVQTFVEGPGHVPLNEIELSVRGMKELCDGAPLYLLGPLVTDIAPGFDHITGAIGGAVAGMHGTDFLCMVTPSEHLALPSIEDIKEGLLVTKLAAHTIDLIKEGPRERAWKQDTAMAYARRDLDWEKQFELAIDGDRARKIRDARKTESDACSMCGELCAVKIVKEAFGEKKEEE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 46739
Sequence Length: 428
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
|
B1I672 | MNQMLAAWQGTVTPEMEQVARDEGYPVEPVLQGVAAGTIVIPANMRRKNLKAVGIGTGLRTKVNANIGTSPKQSALDDHRVKLRVALDAGADAVMDLSTGGDLDRCRREILASCPVPVGTVPIYQAAIEAKERYGAIVAMREDELFEVVERQAKDGVDFFTIHAGVTLESLDRLRKQGRLTDIVSRGGSFLTGWMLHNDRENPFYKEFDRLLEICLAYDVALSLGDGMRPGCQADATDRAQVQELLILGELVDRCREAGVQVFVEGPGHVPLDQIIMNVQLQKRLCKGAPFYVLGPLVTDVAPGYDHITAAIGGAVAAMAGADFLCYVTPAEHLGLPTVEDVREGVIATRIAGHAADLVKRVPGAREWDERMSRARKALDWEKQIELAIDPEKARRYHTERNPEKFAGCTMCGEFCAMKLVGEYLGKDYENC | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 47335
Sequence Length: 432
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
|
A8ZVP4 | MTQVARAKQGVVTEQMAAVAKSEGLSPEAVRDGVAAGRIVIPGNVNRRFAPVGIGSGLRTKVNANIGTSPEHHDVAEEERKLQTAVAAGAHSVMDLSTGGDLFAVRKMVLEKSPVMVGAVPIYEVAARLSAESRAFYEMTPDMLFDAIERQCAEGLDYITVHCGVTRQAAALAGADRRVTGIVSRGGSLLAAWMHDHRKENPLYEEFDRLLGIAAAYDVTLSLGDGLRPGAVADASDGAQLQELVVLGDLARRARDADVQVMIEGPGHVPIDQIGANVQMQKALCGGAPFYVLGPLTTDCAPGYDHITGAIGGAVAAAAGADFLCYVTPSEHLCLPDIDDVRVGVIAARIAAHSGDIAKKVPGALDRDMQMSACRKALDWRGMYQAAIDPCLPRQRREASHPEEESVCTMCGELCAVKTHNRMTNP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 45112
Sequence Length: 426
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
|
Q6AK99 | MTRNLEKKMSIREDAQQGKVTPLFEQCAAVESMSVERLMAGVSDGTIAITKNKNHAFSKVIAIGAGTSTKVNANLGSSKDINSLEEELKKLAVAIKAGADTIMDLSMGGDLQKIRQEILKNCSVPLGTVPIYQVAAEVVAAGKEIVDMTVERMFEVIEQQAKDGVDFMTIHCGINRHLQERLKNQPRTMGVVSRGGSFTLDWMNHHKRENPMYEYFDDLLAILKEHEVTLSLGDGIRPGCLADATDRNQIQELITLGELTERAWAAGVQVIVEGPGHMPLNQIKANVLLQKQMCKGAPFYVLGPLVTDIAPGYDHITGAIGGAIAASAGADYLCYVTPAEHLKLPNCSDVHEGVIASKIAAHAADIVKGLPGAIEKDNAMAKCRKELDWKGQIELSIDPAKSAQYRHEGGGDATDACSMCGEFCALKVFERSQK | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 46957
Sequence Length: 434
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
|
A8F821 | MTQMEIAQKGTSSEEMKRVAEYEEMNLEVIRQKLAYGKAVLPKNKLHKIEKPMIVGEGFTVKVNANIGTSQAFFSLEEEKEKARVAIEYGADSLMVLSTWGDLKEIRKAIIDLSAVPVGSVPIYDSAMKSYQLKKNVVDFSEKDFLNMVISHAEDGIDFMTIHAGITKKVLEHVKNSGRILKVVSRGGAIIAGWMIKNNKENPFYEYFDELLDIAKDYDITLSLGDGMRPGTVLDASDVQQFEELFVMRELVEKAREKGVQVMLEGPGHIPLNEVELNVKLMKKIGEDAPIFLLGPLPTDRAMGYDHIACAIGGALAGYYGADFLCYVTPSEHISLPTIEDVREGVIASKIAAAIADLARGNRKAWWLEKQMALSRKNFNWEEMFKLSLGKDLARKKYKERPYLHEGCSMCGPFCAIKIVEEFF | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 47521
Sequence Length: 424
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
|
Q4FVJ8 | MTISDIGSQASTTTSSKATAKADALKTPAHRSETDARFEEDARDLHRILPASRKVYIEGSRPDIQVPMREITLDPTPIQGVPESEWEQNPPFYVYDTSGVYTDPNTTIDLTKGLPKLREEWIKERGDTEQLSGLSSDYGQARARDISTANLRFAHIDKPRRAKAVDGKVGNVTQMHYARRGIITPEMEYIAIRETQKQHELTDMRQHEGETFGAHTPAIITPEFVRSEVAAGRAIIPNNINHPESEPMIIGRNFLVKINANIGNSALGSSIDEEVSKMTWATRWGADNIMDLSTGNHIHETREWLIRNSPVPIGTVPIYQALEKVDGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTANRLTGIVSRGGSIMAQWCLAHHKESFLYTHFEDICEIMKQYDVAFSLGDGLRPGCLQDANDEAQFGELRTLGELTQVAWKHDVQVMIEGPGHVAMNRIKENMDLQLETCADAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPNKKDVKDGIITYKIAAHAADLAKGHPGAQARDNALSKARFEFRWDDQFNLALDPDTAREFHDETLPKDAHKSAHFCSMCGPKFCSMKITQNVRDYAAGLKTLADTKNSVSPQSGALNDAEHLIKKVDTQLVEQVGSASAEEIHQGMAEMTEKYHKEGRQLYKEV | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 76921
Sequence Length: 691
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
|
Q5XI22 | MNAGSDPVVIISAARTAIGSFNGALSTVPVHNLGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLAHLRSGVKMGEVPLADSILCDGLTDAFHNYHMGITAENVAKKWQVSREAQDKVAVVSQNRAEHAQKAGHFDKEIVPVHVSSRKGLTEVKIDEFPRHGSNLEAMSKLKPYFLTDGTGTVTPANASGMNDGAAAVVLMKKTEAESRMLKPLAQVVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDVFEINEAFAAVSAAIAKELGLSPEKVNIDGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGIAMCVQRG | Function: Involved in the biosynthetic pathway of cholesterol.
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 41108
Sequence Length: 397
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
|
P39594 | MTRISREMMKELLSVYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDALTGEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQEDANAKEVRAAIGDMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQTYKTGR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP.
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 23681
Sequence Length: 222
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q8AA13 | MVSLQFITHQTDRYTYFESALMALEGGCKWIQLRMKEAPCEEVEAVALQLKPLCKEKEAILLLDDHVELAKKLEVDGVHLGKKDMPIDQARQLLGEAFIIGGTANTFEDVVQHYRAGADYLGIGPFRFTTTKKNLSPVLGLEGYTAILSQMKEANIELPVVAIGGITREDIPAILETGVNGIALSGTILRAEDPAAETRKILNMKRIIK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 23050
Sequence Length: 209
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q2KUS6 | MNTLRFPAGLYGVTPEWDDTSRLLAAVRDAAAGGMRALQLRRKHLSREQRLLQARALAPLCRELGVTFIVNDDWRTALEAGADGAHIGRDDATLAEVRAAAPGLLLGVSCYADLNRARELLAQGADYIAFGAVFPSPTKPQAAHAPLALLGEAAAQVRACGEPRPAVVAIGGITPANAGLVAAAGADSIAVITGLFEAPDIRAAAQACAAPFPLTD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22339
Sequence Length: 216
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q7WF72 | MKTLRFPAGLYGITPEWDDTDRLLAAVRAAAAGGMTALQLRRKLADERLRAAQARALAPLCRELGVVFLVNDHWKLALDVGADGAHLGRDDADPATVRAQAGAGLLLGVSCYNDLRRADALLAAGADYVAFGTVFASPTKPEAVHAPLQTLTEARARLLACPAPRPAVVAIGGITPANVSQVAQAGADSAAVISGLFEAPDIQAAARACAAAFSVNP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22357
Sequence Length: 217
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
A8M9N4 | MRLPKGIYGITDDSYNVKNHVDAAKVFLEGGVRIIQYRRKEGSIRQMLNEAKEIRKLCNQYGAVMIVDDRVDIAVLSDADGVHVGLEDAPVDEVKRRFSGIIIGASASTVDEAKEGEKAGADYLGAGSIFPSPTKPDYRILGLEGLRRVVQSVSIPVYAIGGVTLESIPAIKATGAWGAAVISGILAAKDPLEMAKRFVKAWDEA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22057
Sequence Length: 205
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q8R806 | MKRIDFTLYAITDRSFIKGMDIAEAVEIAIKNGVTVVQLREKDISSREFYEIALKVKEVTRKYNVPLIINDRVDIALAVDAEGVHVGPDDLPVGVVRRILGPDKIVGGSAYSVEEALKAEKEGADYIGAGSVFAQPVKPEAEVIGIEGVRKIKEAVNIPVVAIGGVNKTNAYEVILHSGVDGISAIAGIFDGDIEANTKDMLREIRRAFKERGK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 23218
Sequence Length: 214
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q9PNL3 | MKNKLDLSLYLVATKGSKSEECFLNTLENAIKGGVSIIQLREKELNAREFYKLGLKVQKLCKSYKIPFLINDRVDIALALDADGVHLGQEDLEAKLARKLLGDEKIIGLSLKKLEQLEFIQGVNYLGCGAIKATPTKESSLLSLELLSQICDKSPIGVVAIGGIDKEALVELKGINLSGVAVVRAIMDAKDAFLAAKELKRKIYENLSLK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 23001
Sequence Length: 210
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
B0SUK3 | MTDCRLYLITPPALDDLAAFGHDLAAALDGGDVAALQIRLKDAPDDIIAAAVQVLSPIARARDVAVILNDRPDLAARLGCDGVHLGQDDMPLAQARKLMGPGAMIGVTCHDSRHLAMEAAEAGADYVAFGAFFPTTTKDAPTTADPEILSIWQETMEIPSVAIGGITADNAAGLAAAGADFLAVSAGVWKHPQGPAAGVAAINAAIAQGLEARLAARGG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22280
Sequence Length: 219
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
A9WDL8 | MSIAHIVDWRLYVVTDAGLSRGRSHRAVIEAAIVGGATVVQYREKHASTRQMIEEALELRDLTRRAGVPLIVNDRVDVALAVDADGVHVGQDDMPVALARRLIGNKLLGVSAHNLSEALQAVRDGADYLGVGPIFATTTKPDAAAPIGLDGLRAIRQHVSIPIVAIGGINQANAADVMRAGADGIAVVSAVVAADDVTAAARQLRALVSVTQEKAL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22596
Sequence Length: 216
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q824E9 | MEEDFFKLILITDRQNIPMEEYLDFVSACVQSGVTAVQLREKGLSHRELLSFGGALKSILDPLDIPLIVSDSVSVCLDLDASGVHLGQTDGDVIEARELLGPDKIIGWNVHTLDQLLNANTLPIDYLGLSALFATENKPEATDLWGFSGLEQAVSLCEHPIVAVGGIDESNAGNVVEAGAAGIAAIGAFHSAHNPGLATKALREIVDRGLRC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22571
Sequence Length: 212
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
A5WDP0 | MNKHNKSADALSLYLVTDSALCADKGLIETVLAAIDGGVTLVQLRDKHASDEALYTTACELKEAIAGRVPLVINDKVQIAHKAKLDGAHIGQGDLSVKQARNILGHDAWLGLSINTLAQLQQTHHHHLDLLDYVGLGPVFATATKQDHAEPIGLEGLSTLSKASVLPTVAIGGINHANARQVYQTGCHGIAVVSAICAADDPKQAAELLIAQR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22462
Sequence Length: 213
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q8U192 | MNLRNKLKLYVITDRRLKPEVESVREALEGGATAIQMRIKNAPTREMYEIGKTLRQLTREYDALFFVDDRVDVALAVDADGVQLGPEDMPIEVAKEIAPNLIIGASVYSLEEALEAEKKGADYLGAGSVFPTKTKEDARVIGLEGLRKIVESVKIPVVAIGGINKDNAREVLKTGVDGIAVISAVMGAEDVRKATEELRKIVEEVLG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22590
Sequence Length: 207
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
O34294 | MRLDPFYLIVDSADWVERLVPLGVKLVQLRIKDRPEPVLREEIRRAKAACAAAACQLIINDYWRLAIDEGCDFIHLGQEDLMAADLAAIRRAGLKLGLSTHDPSELETALAAAPDYVALGPVWPTILKEMKWAPQGVERLADWRRRVGPMPLVAIGGITAERAPLVLENGADSAAVVTDITRNPDPEARTRQWLAATAPWRSVG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22488
Sequence Length: 204
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q7UQH1 | MTNAESRTVLRILDANANRAGEGLRTLEESARFILNDLSLTERLKTHRHDLAVAMRRWNRFQLIGSRDTPGDVGTGVQTASEQSRADLSSVIAAATTRTQQALRCLEEYGKTADSEFAACIESIRYQCYATFRELELKMAGLNARSRKLVEARLYALIACEPNADYLKARIAELVDAGVDVIQLRDSSVDDRTLFEQAKLGAAIAAERDVLWIINDRADIAVASGADGVHVGQEELPVDAVREVVGPERLIGLSTHSIEQVRLATRTTANYIGCGPTFPGKTKSFDRYPGCEFLTQVSDAERSGELTLPAFAIGGIGLGNVEQVAQSGIGRVAVTGALAPHDGLHQTAMGMREILERVPLRITPDSSDVCPLPND | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 40704
Sequence Length: 375
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
B6INN5 | MTDCRLYLITPPAFDPQAFAPTLAAALDAGDVACVQLRLKDAPDEAILRAVEVLRPLVQARDVAFILNDRPDLAARSGCDGVHVGQEDTPYREARRLVGADAIVGVTCHDSRHLAMVAGEEGADYVAFGAFFPTGTKEPKTTADPEILTWWQEMMEVPCVAIGGITVETAPLLVQAGADFLAVCGGVWNHPAGPAAAVADFNRVMRG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 21998
Sequence Length: 207
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
Q21MI9 | MPHNKHTVYAITDATLMPTTASLCHRVELALRSGVTWLQYRDKSSNTSKRSEQAQALKALCQTYNAKLIINDDTALAKQVGADGVHLGQTDGCIVSARELLGPQAIIGSTCHASLELAERALAQGSSYVAFGRFFASNTKPNAAPAQLSLLAHAQQKFTCPIVAIGGITPSNGAQLLHAGATTLAVCHSLFADDNVEYRAKCLLGLTPNAEDALVTS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22930
Sequence Length: 217
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
A8M4E6 | MSSLGRLHLITDNRPGQDPLAVVRAALSVARAELVVQVRVTDETTDRQAYDLARRVTVLCARYGATCLVNDRLHVALAVGADGGHVGADDLPVGAARAVLGSAAVLGATAREADTAVEAVAAGASYLGVGSVHPTTSKDGLPPPIGAAGLRAVAAAVSVPVIAIGGVTAADVPDLRAAGAYGVAVIAALSHAADPARATAAFVEALTC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 20611
Sequence Length: 208
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
|
A7MQQ2 | MLRIADKTFQSRLFTGTGKFASSSLMLEAIRESGSEMATLAMKRVDLLRRDDALLAPLQASGVALLPNTSGAKTAEEAVFAAQLAREALGTHWIKLEIHPDARWLLPDPIETLRAAEKLVAQGFVVLPYCGADPVLCKRLEEAGCAAVMPLGAPIGSNQGLQTRALLEIIIAQASVPVVVDAGIGAPSHAAEALEMGADAVLVNTAIAVARDPVAMARAFRQAVEAGRTGFEAGLGARVFQAQATSPLTGFLEAQA | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 26794
Sequence Length: 256
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.10
|
Q6AAE4 | MSCDEKAATSSDEPLRIGGLRLTSRLIMGTGGSTSMDTLERALVASGTQLTTVAMRRFAAGPRQSVFEILQRHRITALPNTAGCYTARDAILTANLAREALDTNLVKLEVIADEDTLLPDPVELVNAAEQLVANDFVVLAYTNDDPAIAKRLEDLGCAAVMPAGAPIGTGLGILNPHNIELIVDRANVPVILDAGIGTASEATLAMELGCDAVLLASAVTRAHNPVGMAQAMKMAVVAGRMARTSGRIPRRRLARASSPFDGIITGRVRGPRENDSL | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 29163
Sequence Length: 277
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.10
|
Q85G31 | MDSFCLHHYQFSSRLILGTGRYSSPSLAQQSIEASGCEIVTVAVRRFHALHAFTPLINWNRYWLLPNTAGCRTCSEAVRVALLARQLLQHLQQPHQCLIKLEVIPDPLYLLPDPLGTLKAAEILVRKGFAVLPYIYPDPVLALQLEQIGCAAVMPLASPIGSGQGIQHVHSLQLILQNARIPVIIDAGLALPSDASRVMEMGASAVLINSAIALSPSPVSMAHAMKLAVQAGRLAFLAGRMPLSSSAHASSASFGSFL | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 27715
Sequence Length: 258
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Plastid
EC: 2.8.1.10
|
P58263 | MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIFAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLAPQSGPGSRSYFAHATSPLTGFLEASV | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 26865
Sequence Length: 256
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.10
|
B9DKG1 | MLKIGPYEMESRLLLGTGKFDNEEIQTKAIEASGTDVLTFAVRRMNLYDKNLPNPLANVNLKDFVTFPNTAGAKTVDEAIRIAEIAKHAGVCDMIKVEIIGDDETLLPDPIATYEACEILLERGYIVCPYIAEDVVLAKRLEELGVHAVMPLASPIGTGRGINNPLNLSYIVKNANVPIIVDAGIGSAKDAAEAMELGADAVLLNSAVSRAKDPVKMAEAMKLGIEAGRLSYEAGRIPVKYTAQASSPSEGLGFL | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 27287
Sequence Length: 255
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.10
|
A0R980 | MNMKEISKVVDLVRESNPLVHNITNVVVTNFTANGLLALGASPVMAYAKEEVAEMASIAGALVLNMGTLRPDEVEAMLLAGKSANRNDVPVLFDPVGAGATSYRTEVARHIPAEIELAIIRGNAAEIANVINEKWEIKGVDAGAGNGNVVSIAKQAADELNTVAVITGKEDVVTDGERTIVIRNGHSILTKITGTGCLLTSVIGAFVAVEKDYVKAAVAALTFYGVAAELAAAKTVEKGPGSFQIEFLNQLANTTSGDIEKYGKIEVI | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28089
Sequence Length: 268
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
Q65DJ9 | MNMEDAARGIELVRKQKPLVHNMTNNVVTNFTANGLLALGASPVMAYAREEAADMAKIAGALVLNIGTLSRESVEAMIIAGKSANEHGVPVIFDPVGAGATPFRTESAQAIMRKVKVSAVRGNAAEIANTLGEDWLIKGVDAGEESGDRTELAKKAAKLWDTAVIITGAEDVITDGTKTYTVGNGHQLLTKVTGTGCLFTSVIGAFCAVEKDVCRAAVSAAAFYGTAAELAAAKTESRGPGSFQIEFLNQLAAVEAMDIKERGRIREVE | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28240
Sequence Length: 269
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
A8FIR7 | MKTSIASHLLEKVRAENPLVHNITNQVVTNFTANGLLALGASPVMANAKEEVAEMAQLADALVLNIGTLTKETVESMILAGQSANKKGIPVLLDPVGVGATTFRLKAAKQLLEQVNITVVRGNAAEIAHLLEVDGWESKGVDAKAANGDVSALVKQAAKTLQTVVVITGEVDVVSDGEDVLSIHNGHEWLTKVTGTGCLLTSVIGAFCAAGERPLHASAAALLFYGVAAEKAAQYTQNKGPGTFQMELLNALSHTTGNDVLTLGKIGRNVT | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28236
Sequence Length: 271
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
P39593 | MDAQSAAKCLTAVRRHSPLVHSITNNVVTNFTANGLLALGASPVMAYAKEEVADMAKIAGALVLNIGTLSKESVEAMIIAGKSANEHGVPVILDPVGAGATPFRTESARDIIREVRLAAIRGNAAEIAHTVGVTDWLIKGVDAGEGGGDIIRLAQQAAQKLNTVIAITGEVDVIADTSHVYTLHNGHKLLTKVTGAGCLLTSVVGAFCAVEENPLFAAIAAISSYGVAAQLAAQQTADKGPGSFQIELLNKLSTVTEQDVQEWATIERVTVS | Cofactor: Binds 2 magnesium ions per subunit. The first is coordinated via water, the second is coordinated to ATP but its significance is unclear.
Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28213
Sequence Length: 272
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
B8DSX7 | MTTASTTPNSDTSNLHEVAPDDPIRERIRQAAQNVREQTPLAQSFTNFVTINLVANAQLAAGGTAAMSFLPNDVTSLASSCGATYINVGTLLPFYRDALQEISEHLSRHGCKWVLDPVAAGVGVARTEILKGFKDYPPTVIRANASEALVLHDMWQLGDAAGTDEHNGPAGVEAADSVDAAITAATDLAAYLALHSPTHTGAVAVSGEVDLVTDGRLVYRLPGGSAMMTKITGAGCSLGGVTATYLAVADALVASLAASMLYNVSSGAAERASHGPGSFQTAFLDALWNVTPEEIASAPLYLA | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 31354
Sequence Length: 303
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
A7IA08 | MDNQVFSGIFARAREQHPLVHHITNYVTVNDCANITIGAGGAPVMADAREEAGEMTGFAGALVLNIGTLNSGIIESMILAGKVANERKIPIILDPVGAGATRLRTDSTRRLLDELTISIIKGNAGEIGVLAGAEAKVRGVDSAGISGDPVTITRTFARETGITVVMSGATDIISDGNKVLLVDNGHPLMGRISGTGCMASAVTGVIAAVEKDRLIAAATALAAFGLAGERAAAASRGPGSFKPALFDAMAELGPQDLAADARVRSA | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 27142
Sequence Length: 266
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
A3CS46 | MPDNTREGSSARFVDGAIPAGLLAAVRSQRPLVHHITNGVTINDCANITICAGAAPVMAEAPEEVAGMVAAAGALVLNIGTLSAAQVEAMLIAGRRANELGIPVVLDPVGVGATEFRTATARKLLDTLDIAVLKGNAGEIGVLAGTGGSVRGVDSGGVAGDPVETARECARSTGTVVSMTGAVDVVTDGSRVFLVGNGNPAMDRLSGTGCMASSVTAAFVAVAEDYAVASAAALAAFGLAGEWGAAGARGPYTFRTALFDELAGLSPDDLAGHARIEER | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 27828
Sequence Length: 279
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
A5ULP3 | MTNKEKLLQKIPELLNEVKSKNPLTHCITNFVTVNDCANAVLAIGASPIMSEDIEEVAEVVSIADALVINIGKLSHEQVEAMKISSAQANKINTPVILDPVGVGISQLRNKVTLEIIENYKLAAIRGNITEIKTIAKLTGIISESNTAKGVDVSESDIITQDNLNENADVISKLAAKLDTVILASGPIDILSDGETTIAIDNGDEMMPYITGSGCMLSSIVGSCIGATNPLEGTMVAALLMTIAGEKARSKVDSENAGTGSFRAYLIDYLYKLDGQTLINKSNIEIL | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 30488
Sequence Length: 287
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
Q2RGX6 | MNWGEQVASRRQRVHEQRPLVHHITNLVVTNLTANVTLAIGASPVMAYAREEVADMARLAQAVVLNMGTLTGDVVEAMLLAGKAANNAGIPVVFDPVGAGATPFRTRTAQKIIKELHIDILRGNASEIASIGGFGGHTKGVDAAGAPARVAEMVKQVARDLNTVVAVTGATDYISDGERLIAVDNGHPLLTFVTGTGCSATSIIAAFRAVEEDGVTASTAALAYYGLAAERAAAVSQGPASFQVALLDTLYNLAGEELARGVKIRLL | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 27779
Sequence Length: 267
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
Q3IP35 | MSDVDAAVDLAAALGDIDTATPLVNSVTNNVTVNDVANITLHWGGLPVMSDDAREVDDMVATADGCLINMGTVDEDGEESMVVAGTAANEGDKPLVVDPVGVGATPTRTRVANRLLDELDVTILNGNHGEITALAGDDADVRGVESVGEYADIAETALSCARTHDTVVVASGETDIVASPEEAYEITAGHPLMAQIVGTGCMLGVTLATFAAGMENATPLDAALAGTVGFGLAGEKAAEEGEYNGPASYKTAFLDTVAGLEAAPDDPAGRIERVLSVT | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28228
Sequence Length: 278
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
B2A1A8 | MSTFNSNFKLGTYLTQVRQENPLVHAITNYVTMNDCANITLAAGASPAMCESRDEVSDFVPLAKALYINIGTINQEHKDSIYLAAEKASELEIPIVLDPVGAVAIKSRLDLVKDLLTNYNVSCIKGNNAEIKCLAGRKGHGKGMDSLDLGEDIQMVNSELSEKYNTMVLATGKTDLITKGNITVKVSNGTPLLGRITGSGCMLGILISAFIGASDNDWEAGIAATVSMGVVGEMAEESISSSTDLGSFRVKIFDHMAALTSKELQERGNVSEL | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 29157
Sequence Length: 273
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
O97680 | MVKQIESKYAFQEALNSAGEKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVVFLEVDVDDCQDVAAECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELI | Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity).
PTM: In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins (By similarity).
Sequence Mass (Da): 11813
Sequence Length: 105
Subcellular Location: Nucleus
|
Q9BDJ3 | MVKQIDSKDAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVVFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINEFV | Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity).
PTM: In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins (By similarity).
Sequence Mass (Da): 11757
Sequence Length: 105
Subcellular Location: Nucleus
|
P45855 | MRKTVIVSAARTPFGKFGGVLKEVKAAELGGIVMKEALQQAGVSGDDVEGNVMGMVVQAGSGQIPSRQAARLAGMPWSVPSETLNKVCASGLRAVTLCDQMIRAQDADILVAGGMESMSNIPYAVPAGRWGARMGDGELRDLMVYDGLTCAFDEVHMAVHGNTAAKEYAISRREQDEWALRSHARAAKAADEGKFQDEIVPVNWIGRKGKPNVVDKDEAIRRDTSLDQLAKLAPIYASDGSITAGNAPGVNDGAGAFVLMSEEKAAELGKRPLATILGFSTTGMPAHELAAAPGFAINKLLKKNGLTVQDIDLFEVNEAFASVVLTCEKIVGFDLEKVNVNGGAIALGHPIGASGARILMTLVYELKRRGGGLGVAAICSGAAQGDAVLVQVH | Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 41179
Sequence Length: 393
Subcellular Location: Cytoplasm
EC: 2.3.1.9
|
Q8BGW0 | MALSLEEFVYSLDLRTLPRVLEIQSGIYFEGSVYEMFGNECCLSTGEVIKITGLKIKKMMAEICEGAIGGCESQKPFELPMNFPGLFKVMADKTPYLSIEEITRTVNIGPSRLGHPCFYHLKDIKLENLIIKQGEPIRFNSVEEINGETLVNCGVVRNHQSHSFTLPLSQEGEFYECEDEHIYTLKEIVEWKIPKNRTRTVKLTDFSNKWDSTNPFPEDFYGTLILKPVYEIQGVLKFQKDIVRILPSLDVEVKDITDSYDANWFLQLLSTDDLFEMTSKEFPVVAEVVEISQGNHLPQSILQREKTIVIHKKYQASRILASEIRSNFPKRHFLIPISYKGKFKRRPREFPTAYDLQIAKSRKETLHVVATKAFHTLHKELSPVSVGDQFLVHHSETTEVVFEGTRKVNVLTCEKVLNKTREDAQLPLYMEGGFVEVIHDKKQYQISELCTQFCWPFNVKVAVRDLSIKDDILAATPGLQLEEDITDSYLLISDFANPEECWEIPMSRLNMTVRLVNGSSLPADAGLLQVRSFVEEITEEQYYMMRRYESSLSHPPPRPPKHPSAEEMKLTLLSLAEERTINLPKSLKSHHVDRPKKLPSDESGQDSRAPVGFQNDVADVERQKSKHGPLQPQAPL | Function: Plays a central role in late thymocyte development by controlling both positive and negative T-cell selection. Required to sustain and/or integrate signals required for proper lineage commitment and maturation of T-cells. Regulates T-cell development through T-cell antigen receptor (TCR) signaling and in particular through the regulation of calcium influx and phosphorylation of Erk.
PTM: Phosphorylated on Tyr residues quickly after TCR stimulation.
Sequence Mass (Da): 72780
Sequence Length: 636
Subcellular Location: Cytoplasm
|
Q5TEJ8 | MEPVPLQDFVRALDPASLPRVLRVCSGVYFEGSIYEISGNECCLSTGDLIKVTQVRLQKVVCENPKTSQTMELAPNFQGYFTPLNTPQSYETLEELVSATTQSSKQLPTCFMSTHRIVTEGRVVTEDQLLMLEAVVMHLGIRSARCVLGMEGQQVILHLPLSQKGPFWTWEPSAPRTLLQVLQDPALKDLVLTCPTLPWHSLILRPQYEIQAIMHMRRTIVKIPSTLEVDVEDVTASSRHVHFIKPLLLSEVLAWEGPFPLSMEILEVPEGRPIFLSPWVGSLQKGQRLCVYGLASPPWRVLASSKGRKVPRHFLVSGGYQGKLRRRPREFPTAYDLLGAFQPGRPLRVVATKDCEGEREENPEFTSLAVGDRLEVLGPGQAHGAQGSDVDVLVCQRLSDQAGEDEEEECKEEAESPERVLLPFHFPGSFVEEMSDSRRYSLADLTAQFSLPCEVKVVAKDTSHPTDPLTSFLGLRLEEKITEPFLVVSLDSEPGMCFEIPPRWLDLTVVKAKGQPDLPEGSLPIATVEELTDTFYYRLRKLPACEIQAPPPRPPKNQGLSKQRRHSSEGGVKSSQVLGLQQHARLPKPKAKTLPEFIKDGSSTYSKIPAHRKGHRPAKPQRQDLDDDEHDYEEILEQFQKTI | Function: May constitute a control point in macrophage inflammatory response, promoting LPS-induced TLR4-mediated TNF production . Determines the threshold for activation of B cells by low-affinity and low-avidity ligands via PLCG2 activation and its downstream pathways (By similarity).
PTM: Phosphorylation at Tyr-632 is induced by LPS. Phosphorylated by Src kinases (Lck or Fyn) following BCR engagement.
Sequence Mass (Da): 72049
Sequence Length: 643
Subcellular Location: Nucleus
|
Q91YX0 | MEPVPLQDFVSGLDPTSLPRVLRVCSGVYFEGSVYELFGNECCLSTGDLIKVTHVQLQKVVCEYPETGQTLELNPNFTGLFSPLTSLRSYRTLEDLVSAMPQNSTRWPIYFKSTQRIVTKASVVPEDQPLRLEAVEIHHGIRYARCVQVSKTKELLHLPLSQKGPFWRCKPSAPQTLHQILQDPALKDLTLSCPSLPWNSVILKPQYMLQAIMHMRSSIVKIPSTLEVEVEDVTASSQHIHFFKPLRLSEVLAGGGPFPLTTEILEVPEGPPVFLSPWVSFLRKGQRLCIYGPASPSWRVVASSKSRKVPRYFMLSGAYQGKLKRRPREFSTAYDLLGALQPGRPLRVVATKDCDGNEEENPDFSFLAVGDRLEVLRSGQVCGTKGQDIDVLVCQRLSEQSGEEEEDLEEIEDEAEDKEQILLPLYLSGSFVEEVNDSRRYNLVDLTAQYSLPCEVKVVTKDTRHPTDPLASFPGLRLEEKLTEPFLVVSLDSQPEMCFEIPPRWLDLTVVEAEGQPAQVARPLSIAPVEELSEAFYYSLRKLPASESQAPPPRPPKSQGINKKQQNIQSCKESSVKPQVVEPQKSCPQPQLKAKTLEALPKNKSNVYSKISVHKKDRKPNPQTQNSVLSMKPKTSSSLGKHSTMESHLLPDPDMDDHDYEEI | Function: May constitute a control point in macrophage inflammatory response, promoting LPS-induced TLR4-mediated TNF production . Determines the threshold for activation of B cells by low-affinity and low-avidity ligands via PLCG2 activation and its downstream pathways .
PTM: Phosphorylation at Tyr-660 is induced by LPS . Phosphorylated by Src kinases (Lck or Fyn) following BCR engagement .
Sequence Mass (Da): 74378
Sequence Length: 663
Subcellular Location: Nucleus
|
P9WHF4 | MQARGQVLITAAELAGMIQAGDPVSILDVRWRLDEPDGHAAYLQGHLPGAVFVSLEDELSDHTIAGRGRHPLPSGASLQATVRRCGIRHDVPVVVYDDWNRAGSARAWWVLTAAGIANVRILDGGLPAWRSAGGSIETGQVSPQLGNVTVLHDDLYAGQRLTLTAQQAGAGGVTLLDARVPERFRGDVEPVDAVAGHIPGAINVPSGSVLADDGTFLGNGALNALLSDHGIDHGGRVGVYCGSGVSAAVIVAALAVIGQDAELFPGSWSEWSSDPTRPVGRGTA | Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 29400
Sequence Length: 284
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
EC: 2.8.1.1
|
P31142 | MSTTWFVGADWLAEHIDDPEIQIIDARMASPGQEDRNVAQEYLNGHIPGAVFFDIEALSDHTSPLPHMLPRPETFAVAMRELGVNQDKHLIVYDEGNLFSAPRAWWMLRTFGVEKVSILGGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVKVTDVLLASHENTAQIIDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTELVREGELKTTDELDAIFFGRGVSYDKPIIVSCGSGVTAAVVLLALATLDVPNVKLYDGAWSEWGARADLPVEPVK | Function: Catalyzes the transfer of sulfur from 3-mercaptopyruvate to a thiol-containing acceptor to form an intramolecular disulfide releasing hydrogen sulfide and pyruvate (Probable). May be involved in the enhancement of bacterial growth inhibition by serine .
Catalytic Activity: 2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate
Sequence Mass (Da): 30812
Sequence Length: 281
Domain: The N-terminal region is the non-catalytic domain; the C-terminus contains the active-site cysteine residue and the CGSGVTA motif probably responsible for substrate specificity.
Subcellular Location: Cytoplasm
EC: 2.8.1.2
|
P25325 | MASPQLCRALVSAQWVAEALRAPRAGQPLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRARPEDVISEGRGKTH | Function: Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.
Catalytic Activity: 2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate
Sequence Mass (Da): 33178
Sequence Length: 297
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
Subcellular Location: Cytoplasm
EC: 2.8.1.2
|
Q9I452 | MSSAQLLTAQQLAARLSEPDLLVLDCRFALEDPSYGARVYQENHIPGAHFADLERDLSAPVRKGVTGRHPLPDPAELALKLQAWGLRQDSQVVLYDDGPGAFAARAWWLLHWLGKRDGVYLLDGGLAAWKAAGLALTNGESSLRPGDFQGQPDASLLIDAATLQAQLGQPGLALLDARAQPRFRGEVEPIDPVAGHIPGAQCAAFTDNLGSDGRFLPPEQLHQRFSALLRGRPVDELVAYCGSGVTACHNLFALSLAGFPLPRLYAGSWSEWITDPRRPVATGD | Function: Catalyzes the transfer of sulfur from 3-mercaptopyruvate to a thiol-containing acceptor to form an intramolecular disulfide releasing hydrogen sulfide and pyruvate.
Catalytic Activity: 2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate
Sequence Mass (Da): 30598
Sequence Length: 284
Domain: The N-terminal region is the non-catalytic domain; the C-terminus contains the active-site cysteine residue and the CGSGVTA motif probably responsible for substrate specificity.
Subcellular Location: Cytoplasm
EC: 2.8.1.2
|
P97532 | MAAPQLFRALVSAQWVAEALKSPRASQPLKLLDASWYLPKLGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSLGVSAATHVVIYDGSDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDILENLDARRFQVVDARAAGRFQGTQPEPRDGIEPGHIPGSVNIPFTEFLTSEGLEKSPEEIQRLFQEKKVDLSKPLVATCGSGVTACHVVLGAFLCGKPDVPVYDGSWVEWYMRAQPEHVISQGRGKTL | Function: Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.
PTM: The N-terminus is blocked.
Catalytic Activity: 2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate
Sequence Mass (Da): 32940
Sequence Length: 297
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
Subcellular Location: Cytoplasm
EC: 2.8.1.2
|
Q9USJ1 | MFSVGKKISFILPIKGVLQKLKDNAQKTVLLDATWYLPTDTKNGKKEYLESRLPGAQYFDIDEAKDHKNPLPHMLPPADEFASYVGKLGIDRNTNVIIYDRKGFFSSPRVFWTFKVFGHEHVFLFPNAFNAWKTEGLELETGEPRTPKPVVYEGAKLNKDLVASFDDIVKVIESPDAAGVHIVDARAHERFLGNVPESRPGLASGHIPTSINIPFTETTAAGITAPKPEEDLEKVFSSHGLTDKSVPIITSCGSGVTASVLFAALKECGFKDVRVYDESWSGYGKRANEDSSLLATGP | Function: Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.
Catalytic Activity: 2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate
Sequence Mass (Da): 32800
Sequence Length: 298
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
Subcellular Location: Mitochondrion
EC: 2.8.1.2
|
Q9BU02 | MAQGLIEVERKFLPGPGTEERLQELGGTLEYRVTFRDTYYDTPELSLMQADHWLRRREDSGWELKCPGAAGVLGPHTEYKELTAEPTIVAQLCKVLRADGLGAGDVAAVLGPLGLQEVASFVTKRSAWKLVLLGADEEEPQLRVDLDTADFGYAVGEVEALVHEEAEVPTALEKIHRLSSMLGVPAQETAPAKLIVYLQRFRPQDYQRLLEVNSSRERPQETEDPDHCLG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Sequence Mass (Da): 25566
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 3.6.1.28
|
Q8JZL3 | MAQGLIEVERKFAPGPDTEERLQELGATLEHRVTFRDTYYDTSELSLMLSDHWLRQREGSGWELKCPGVTGVSGPHNEYVEVTSEAAIVAQLFELLGSGEQKPAGVAAVLGSLKLQEVASFITTRSSWKLALSGAHGQEPQLTIDLDSADFGYAVGEVEAMVHEKAEVPAALEKIITVSSMLGVPAQEEAPAKLMVYLQRFRPLDYQRLLEAASSGEATGDSAS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Sequence Mass (Da): 24264
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 3.6.1.28
|
Q8CGV7 | MAQGLIEVERKFTPGPDTEERLQKLGATLEHRVTFRDTYYDTSELSLMLSDHWLRQREGSGWEFKCPGVTGVSGPHNEYVEVTSESAIVTQLFELLGSGEQETAGVAAVLGRLKLQEVASFITTRSSWKLALSGAHEEESLLTVDLDSTDFGYAVGEVEAVVHEKAEVPAALEKIISVSSMLGVPAQEKAPAKLLVYLQRFRPQDYQRLLEADSSGEATGDSVP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Sequence Mass (Da): 24544
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 3.6.1.28
|
Q7TX80 | MARCDVLVSADWAESNLHAPKVVFVEVDEDTSAYDRDHIAGAIKLDWRTDLQDPVKRDFVDAQQFSKLLSERGIANEDTVILYGGNNNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPLSSDPVSRPVTSYTASPPDNTIRAFRDEVLAAINVKNLIDVRSPDEFSGKILAPAHLPQEQSQRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGLDNSKETIAYCRIGERSSHTWFVLRELLGHQNVNIAFGYGPHACPASAYSRMCLTTFFTSLTQRFPQLQLARPFEDLERRGKGLHSVGIKELLVTWPT | Function: May be a sulfotransferase involved in the formation of thiosulfate.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 35999
Sequence Length: 320
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
EC: 2.8.1.1
|
P00586 | MVHQVLYRALVSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAVGLDSGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIATCRKGVTACHIALAAYLCGKPDVAIYDGSWFEWFHRAPPETWVSQGKGGKA | Function: Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification. Binds molecular oxygen and sulfur.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 33296
Sequence Length: 297
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue .
Subcellular Location: Mitochondrion matrix
EC: 2.8.1.1
|
A2RVP7 | MADSSAAEPTTGASSPPVASDENSTQIQPIRMPTIEEIRAQEVWNNCAVRAVTSGVMGGGLGLMMGLFLGALDNPITHDTMTARQQFVFTAKQMGQRSWNSCKTFAVMGLVFSAAECIVEKARAKHDTVNTAIAGCVTGGSMSARGGPKAACIGCAGFATFSVLIEKFFDRHT | Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18183
Sequence Length: 173
Subcellular Location: Mitochondrion inner membrane
|
Q94EH2 | MAANDSSNAIDIDGNLDSDSNLNTDGDEATDNDSSKALVTIPAPAVCLFRFAGDAAGGAVMGSIFGYGSGLFKKKGFKGSFADAGQSAKTFAVLSGVHSLVVCLLKQIRGKDDAINVGVAGCCTGLALSFPGAPQALLQSCLTFGAFSFILEGLNKRQTALAHSVSLRHQTGLFQDHHRALPLSLALPIPEEIKGAFSSFCKSLAKPRKF | Function: Together with HP30-1 and HP30-2, triggers the import and insertion of transit sequence-less multi-pass transmembrane proteins (e.g. CEQORH) into the chloroplastic inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21811
Sequence Length: 210
Subcellular Location: Plastid
|
F4J469 | MNSNIFPPSKQQNELNNIQQSFSNLQSQCSNLLLNVSQTLNPLFNANTNNNKPNIFSALNSFRDQAKQALDSRISRFNSGKAPVWARISDDGGGARAQVTVPIRGSGKGLSADAIEERLAGVPVYALSNSNEEFVLVSGTSSGKSLGLLFCKEEDAETLLKEMKSMDPRMRKEGSKVVALALSKVFQLKVNGVAFRLIPESTQVKNALKERKTAGIDDDDFHGVPVFQSKSLILRSENMSYRPVFFRKEDLEKSLIRASSQQNRLNPALKPGDIQVAVFEDIVKGMRESTTSNWDDIVFIPPGFEVSTEQTQE | Function: Involved in protein precursor import into chloroplasts.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34575
Sequence Length: 313
Subcellular Location: Plastid
|
Q9LNQ1 | MAINRSSDHESDENTRLYHPYQNYQVPIKSQYLYKLPTSPEFLFTEESLKQRRSWGENLTFYTGTGYLAGSVAGASAGIFSGIKSFENGDTTKLKINRILNSSGQAGRTWGNRVGIVGLIYAGIESGVVAVTDKDDVWTSVVAGLGTGAVFRAARGVRSAAVAGAFGGIAAGAVVAGKQVFKRYAHI | Function: Essential component of the TIM17:23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Links the inner and outer membranes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19974
Sequence Length: 187
Subcellular Location: Mitochondrion inner membrane
|
Q38820 | MAANNRSDHGSDENTRLYNPYQNYEVPINKSQYLYKLPTSPEFLFTEEALRQRRSWGENLTFYTGTAYLGGSVAGASVGVITGVKSFESGDTTKLKINRILNSSGQTGRTWGNRIGIIGLVYAGIESGIVAATDRDDVWTSVVAGLGTGAVCRAARGVRSAAVAGALGGLAAGAVVAGKQIVKRYVPI | Function: Essential component of the TIM17:23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Links the inner and outer membranes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19878
Sequence Length: 188
Domain: The C-terminal part (143-188) is required for insertion in the mitochondrial inner membrane.
Subcellular Location: Mitochondrion inner membrane
|
Q9S837 | MADPMNHSTGHQQQQKYRQYNPYQQVNLPYRKLYELPTSPEFLFEEEATKKRLTWGENLTFFTGWGYCTGSVLGAFKGTIAGMRAAERGESLKIRTNRILNSGGLVARRGGNCLGSVGLMFAAMESGVTYMRDGDDGSLTTVIAGLATGVLYRAASGPRSAVVAGAVGGVAALAAVAGRRIVKRFVPI | Function: Essential component of the TIM17:23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Links the inner and outer membranes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20213
Sequence Length: 188
Subcellular Location: Mitochondrion inner membrane
|
Q5SRD1 | MEGGGGSGDKTTGVLAGFFGAGEAGYSHADLAGVPLTGMNPLCPYLNVDPRYLVQDTDEFILPTGANKTWGRFELAFFTIGGCCMTGAAFGAMNGLRLGLKETQNMAWSKPGNVQILNMVTRQGALWANTLGSLALLYSAFGVIIEKTRGAEDDLNTVAAGTMTGMLYKCTVSEMALDSPFCVLLSGS | Function: May participate in the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. the PAM complex (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19670
Sequence Length: 188
Subcellular Location: Mitochondrion inner membrane
|
Q9V9P3 | MHKIVWFGTLNKSIGYIGKKKTCLLSPCEKICLNSARKTVQRCDKNYSPPKLRRIKNFYTYSVVLGSLFSIVMWAIYKLGKPEEDHRGPIEDEFSQLPWFRQYIMRMWHTLQYYEKMMEEPQMARLLPNVVPPPYIQPPYSLVLEIKDVLVHPDWTYQTGWRFKKRPGVDYFLQQCSRNFEIVIYTSEQGMTAFPLLDALDPYGYIKYRLVRGATDLVEGQHTKNLDYLNRDLSRVIVVDCDPYTTPLHPDNSLVLTKWLGNDDDVQLFDLTAFLQLIAEHQVNDVREVLRYYRQFEDPMEQFKDNQRRLQEQSQESIQNLPTSERQWNLTLLGRSLRGSSIK | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40580
Sequence Length: 343
Subcellular Location: Mitochondrion inner membrane
|
Q9W0S3 | MSLIAIERVLCGWPKICRKLIVTSRSLTSGLRRALVKQPRKGGDVGKPGMELGRCSCFGLRVNLSNASVVYVGHRRYSTYEKTSTQILTKLFPQTSEESNDEESRERRKLEEEEEQKELERAFRRMKLGFGLFGIGSMLFSFWAIYFYGRPSLDEHGNEVIDEFSCLPQMQQLMWRTWKSVNRFQRFFKEPSRKKLLPDPLQPPYVQPPYTLVLEIKDVLVHPDWTYETGWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDALDPNGCIMYRLVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDTTLFELTSFLSVLGTSEIDDVREVLQYYNQFSDSLSQFRENQRKLGELMHAEEVEKTSKSRPVVKNWTRGFINH | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47706
Sequence Length: 409
Subcellular Location: Mitochondrion inner membrane
|
Q5P162 | MQTTQETQGALERRIDMSVPMAEIDKEVDSRLKRMARTVKMPGFRPGKVPMKIVAQTYGSQARSEAIGAAVEKAFGDKVREQNLRVAGYPRIEPREAAVEGALEFSAVFEVYPQVPLGDLSGQKVERPVLTVGDAEVDKTIEVLRKQRTTFEAVDRPAQDGDRVVIDFAGRKDGELFEGGKAQDFPFVIGAGSMLKDFESAVGGLKVGETKTFEMTFPEDYHAADLAGQKVEFEITVKGVEAPILPAVDADLARALGVADGDVTKLRDEVRANLEREVKRRIQGKVKEQVMEALLVANPIEVPKALVEAESRQLAENAKRDLEMRGMNTKDIPVEPTWFADQAVRRVKLGLIMAELVNAKELYAKPEQVRAMIDEMAQSYEDPAELVRWYYAQPERLGQAEAVVIEDNVVAWVLSQTQTEDKTVTFDELMGNAA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48083
Sequence Length: 434
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q2NJE2 | MKIKKINNQKVQYFFKVSSKELETQLSSAYEKIKSKVEIKGFRKGHVPRKIFENHFGKNNLYSDALENIVQTKYQEILQKKDFESMGMPQVIDLNEKKLKDNQNFTFGLEFIVKPKVILKKYLGLEITKDELEVKDCEVEEKINSLLEKQATLESKTQNNSLELTDTAVFDFEGFVDEKPFEGGTAKNFSLKIGSGQFLPGFEDQMLGMKQGQNKDINITFPSDYHQKKLANKKVIFKVTLHQIKTKKIPQLTDNLVKLLKLANVSTVEELKNNTKKTLLDQKKHKEKENIKKQVIEQLVKNSELQIPQEIISQEKTHLQKEFEKQLKQQNLTLEQYKQYLGIGDEKMEKEFNQQAQKNLQYRLIIEQVAFQEKLTISKEKIEQQYKNLSNHYKVPVNQIKQNLPEKNLQHSLLMDEALDLVINKAVVVTK | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50267
Sequence Length: 431
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q9X6W7 | MNITETSADGLKREYKVVISAQDIEQKVQGRLEELRRTVQLPGFRPGKVPVAVIKQRYGGSVLAEALEDAIADSSRQALNERGLRIAMQPKINVEKYEDGGDLSYTMGVELLPDIEPGDLSGLELEKPVATVEDSAVDEALTRLASAHSVQAPVTEDRAAEKGDIAVIDSPVRSTGEALPGMDGKDYPLELGANQFVPGFEDQLVGAKAGEHRTVKVTFPADYPHDRLKGADTVFEVDVKELRKNVPAEVNDDLAKEFGMESLEKLREAVGRPHQGRIRQRVALRVKRQLLDKLAEAHSFEVPPGMVDVEFEGIWQRLQQELQNGTAGEDAGKPEEELKTEYRGIAERRVRLGLLLSEIGRRNDIQVTQDEINRALIAEARRFPGQERQVFEFFKQNREALENLRAPIFEDKVVDYILDQAKVSEKPVSAEELMKDPDEEAEAA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49408
Sequence Length: 444
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
A1K784 | MQTTQEIQTSQNPLERRIDMSLAVADIDKAVEARLKQMARSVKMPGFRPGKVPLKIVEQTYGPQARSEAIGAAVERAFGEKVREQNLRVAGYPRIEPKEAGSEGALEFSAVFEVYPEVVVGDLSAQSIEQPTLVVGDAEVDKTIDVLRKQRTTFEAAARPTQDGDRVTIDFAGRKDGELFEGGQATDFPFVIGAGSMLKDFETAVVGLGVGETKTFDMTFPEDYHAKHLAGQPVQFEVTLKSVEAPKLPEVDSDFAKALGVADGNVDKLREEVKGNLEREVKRRIQAKVKEQAMDALLAVTPIEVPKALVESEATQLAENAKRDLAARGMNTKDIPVQPAWFGDQAMRRVKLGLIMAEVVKGNELHAKPEQIRGLVEEMAQSYEDPSELVRWYYAQPDRLAQAEAVVIEDNVVAWVLSKAQTSEKSIAFDDLMGNAA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 47981
Sequence Length: 437
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
B9MQ31 | MEFKIEKKGTNKAIIEVEVEAEKFEEGLQKSYLKNAKYFKIPGFRPGKAPRSLIERAYGEEVFYDDAIDYVLNETYPKVIEESKLEVVSRPEVDIVQVGKGKSFIYKAEVYVKPEFELGQYKGVEITKIEYPVAEEEVEHELEHLREENARFVPVERPVENGDIVTIDFEGFVDGEPINGGSAKDYELTIGSNTFIPGFEEQLIGMNKGEEKEIEVTFPEDYQEPSLAGKKATFKVKVKDIKVKELPELDDEFAKDVSEFETLEELKANIRNRIREKNDKRAKDEMIDAILEKIAQNTSIDIPEPMIENQINYYVEDVARNLQYFGMTYERYLQAIGKTDKEFRSQFRERAEKAVRNNLILEKIAKVENIQATEEELQKELERLAKMYNLEVDKLKERLSEDDIEYIKEGIILNKAIDFIYENAKIISEDNQGENQEN | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50844
Sequence Length: 438
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q8RC26 | MGASLKKIEKSVATLELTIPKEKFEEGLDYAFKKNASKFNVPGFRKGKAPRFLVERYYGEGVLYEDAIEYVFHEAYQEALKTFNLEPVDYPDINILQIGKGKDLVLEATVAVMPEVELGEYKGIEIEKIEYDVYDGDVEYELEKLRQQNARIIPVEGRPAEQGDIAVIDFEGYIDDKPFEGGKGENYELELGSNTFVPGFEDQIISHNVGETFDVTVTFPEDYRVEELKGKTAVFKVTLKALNKKELPELDDEFAKDVSEFETLEELKQDIRKKLEEKNKREAENEMKEKAVMKVVENAKVDIPDVMVERQIDLSLRDLDYNLRLQGLDLNTYLSITGKTIQDLRKEMWEGALNRVKTQLVIDKIAKVENIEATEEELENKLKELAESYRVNLEEFKKSLTESQINGIKEDIAYYKTIDFIFNQCKIVSKEE | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49762
Sequence Length: 432
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.