ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9RW02 | MQTSSEPAASETAALLGKPLADRVMRGVRADLKAWAQLDPPFEPQLVSVLASDDEASQVYVQSKAKRAKKLGVAFRVVDLGAAATQEALEQTLRELSADPAVHGIVLELPLAAGLDADAALLHIAARKDIEGLSPANLALIAAGREPEALLPPTPRSVRFLLRHALGDDLRGLRVAVIGPGRTVGRPLLFMLNNKGATVTLCNEHTRDLAAVLAAQDAVVVAVGKAGLLRPEQVQPEHVVIDAGINVQESGDMVGDALPELPVRAQTPVPGGVGPLTSALMYQNLVRGVKLQRGEPVDD | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 31408
Sequence Length: 299
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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C0QAY0 | MAEVLKGKPVADALKAELTKNIEALKKDKGITPKLGIIRVGARPDDLFYEGGAKKTCAAVGMDCEIFEYPEDIDQASFEKAVTEVGAKKDVNGILMFSPLPKNLDERKIRTLIPVEKDVDCLTTGGAAKVFTDDATGFPPCTPTACMEMLHFYDIPIKGKKCVVVGRSLVVGKPLAMLLLREHGTVTICHSRTENLPGVCQDADILIAAVGRAKMVKADFVKKGQIVIDVGINADPDRPGKYCGDVDFETVEPVVTKITPVPAGVGSVTTSVLCKQTFMACQMQNA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30699
Sequence Length: 286
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q6ALZ5 | MSAKIISGTEIRKEILGEIKDAVTEMKDKYGTVPGLVTILVGESPASMSYVSLKIKTALSLGFYEVQESLSVETTEAELLALIEKYNNDDSIHGVLVQLPLPKHINEQNIITAIDPDKDVDAFHPVNIGRLMIGGDDVKFLPCTPAGIQEMLVRSGVETAGAEVVVVGRSNIVGKPIAMMMAQKGIGANATVTIVHTGSRDLATHCRRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVGTNSETGKAILRGDVDFEAVKEIAGKITPVPGGVGPMTIAMLMKNTLASALAHSS | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 31253
Sequence Length: 296
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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A4J3F5 | MTKILDGKKIASILREELKQDIITLKERGIEPKLAVVLVGEDPASVAYAKFLQKVSENAGVLFELHQLSKSTAEEEIICKIEDLNQIQAVHGILMMMPLPPHVNKQHIMEHISPLKDVDGLHPFNRGHLISGGICLHPATPTSCLEILKRSGITLAGKHIVVVGRGETVGKPLVFMALAENATVTVCHSRTVDLGKFTKQADIIISAVGKPGLITADMIKPGAVVVDAGIHEEAGNIIGDVDYEQVKEIAEAITPVPGGVGSLTTVLMLKNVLKGIQLQIGTQE | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30460
Sequence Length: 284
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q72F91 | MQLLDGKATAATIREELRAEIAALTPRARRAPGLAVILVGEDPASQVYVRNKERACHDTGIVSEAFRLAPTTTQEELERLIADLNVRPDIDGILLQLPLPRGLDAQRCLEAIDPAKDVDGFHPQNMGRLALGLPGFRPCTPAGVMTLLERYDLSPSGRKAVVVGRSNIVGKPLALMLGAPGKYANATVTVCHSGTPDLAAECRTADFLFLAIGRPRFVTADMVREGAVVVDVGINRTETGLAGDCDFEGVSRVASAITPVPGGVGPMTIAQLLVNTVQSWKVRCGL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30380
Sequence Length: 286
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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A5EX57 | MSAEIINGKEIAAEIRREIKQETAQFIAATGVRPGLAVILVGNDPASEVYVRNKGIQAEEVGFLSQIYRLPAQTTQAELLAKIVALNNDPQICGILVQLPLPAHLNAEIVLNTIDPNKDVDGFHPLNIGRLWAGEPCSVPCTPLGCSLILKRYFGDSLAGKKALIIGRSNIVGKPMAALLLQQHATVTIAHSKTPDVPALCRQADIVIAAVGQPELVKGDWIKSGAVVLDVGINRIAVGDKTKLVGDVAFESAKEVAAAITPVPGGIGPMTIACLLKNTLTLAKAIQQSGK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30659
Sequence Length: 291
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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B8E335 | MGVILEGKPVAEKLEKEIKEKIQFYKSQGVIPTLCIVKVGKNAEAEAYAKSIEKFFSKIGINIERKNFNEEISLVDFKKIMKELEEDSAIHGVLILRPLPEELERGKAFQFLPTKKDVEGVTYENLGRLLVGEDSFHPCTPQAVLELLDFYQIPVEGKNVVVVGRSISVGKPLSLLLLNRNATITVCHSKTKNLVEFTKKAEILIVAIGKPYFVGKDMVGEGQVIIDVGTNVVDGKLVGDVNFEEVKDKVEYITPVPGGIGVITTRVLAMNLLKAVKKVEA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 31034
Sequence Length: 281
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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A9M068 | MSAQLINGKEVSQKRLQAVAEAVAQRQQDNLHMPCLAVVLVGGDPASAVYVRNKKTACQKCGIKSLSYELPESTSQEELLALVDRLNADSEVDGILVQLPLPKHLDSQAVLERISPDKDVDGFHPYNVGRLAVKMPLMRPCTPKGVMTLLEAYGIDPKGKKAVVVGASNIVGRPQALELLLARATVTVCHSATENLADEVAGADILVVGVGIPNFVKGEWIKPGAVVIDVGINRLDDGSLCGDVEFETAKERAAMITPVPGGVGPMTIATLMENTLHAASLHDA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30110
Sequence Length: 284
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q2GCV3 | MTQLIDGFRIAAGICESIATSVAHLRKNNGLVPSLRVIIVGENPASQVYVRSKQKKAESLGIDAETIALPKDTSEVELIRLVNSLNDDTSINAILVQLPLPPHINPTRIIESIDSKKDVDCFHPENVGRLALSKDALLKPCTPAGSLYLIKSALGDNLSGMDAVVIGRSNIVGKPMAMLLLHENCTITLTHSKTRNIQEKTRQADIVISAVGIPHFVKKDFIKPGATVIDVGMNKVDGKLVGDVDFEDVLQKVKFITPVPRGVGPMTIAFLMLNTVITTCLQNKLEHQEVIGTVIQKL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 32304
Sequence Length: 298
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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A9A4N5 | MTGTKIDGKVISQSVKDRVKKAVEELKNQGINPCLATVLVGDNPASATYVRNKHRACEEVGITTKDHKLDASTTQAQLNEIIENLNNDNSVHGILVQLPLPEQLDEFTTTSRISPLKDVDGLTPHNAGLLAMKKAALVACTPSGVMEMFDYHGIELEGKNIVLINRSNLVGKPLYHLLLDKNATVITCHSRTKNLVELCQSADIIITAVGDRNKFTLTSDMIKEGAIVIDVAISRFQEKLVGDADYEDIIQKASFATPVPGGVGPMTVAMLLKNTITAASLSSQIGK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30956
Sequence Length: 287
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q05213 | MKILRGEEIAEKKAENLHGIIERSGLEPSLKLIQIGDNEAASIYARAKIRRGKKIGIAVDLEKYDDISMKDLLKRIDDLAKDPQINGIMIENPLPKGFDYYEIVRNIPYYKDVDALSPYNQGLIALNREFLVPATPRAVIDIMDYYGYHENTVTIVNRSPVVGRPLSMMLLNRNYTVSVCHSKTKDIGSMTRSSKIVVVAVGRPGFLNREMVTPGSVVIDVGINYVNDKVVGDANFEDLSEYVEAITPVPGGVGPITATNILENVVKAAEFQKNNL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30622
Sequence Length: 276
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q9X288 | MWIDCKTIARSIEERTKERVEKLGFTPKLVSVACTDDPSALSYLKSQRKKAEKLGIAFEIMNVSPEEIVSTLKKLGSDESVNGVFVARPFPLGLDEKEILSSVPVEKDVEGVNPANLGLLLYDEEIFPPCTAEAAVRILERETNLSGKRVTVVGRSVTVGKPLALMLLKKGRDATVTVCHSRTVNLEEITKNSDIVVVAVGRAHFLKKNMVKEGAIVIDVGINYVDGKLQGDVDPSVEEIARVTPVPGGVGQVTTALLFEHVVRAAERQRK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 29557
Sequence Length: 271
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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B9KZ23 | MAAHILSGRPVVESLHARIQQVLARRAPHQGPPTLTVLLPNDPSAQAYARAIRKQFTTLSLNYRTEEIDDTLDESRFAILLKRLAEDESVTGILALQPLPKGVSRRSLARLMPPTKDVDGVSFEQQGRLAIGSPWIAPSTPLGGLILLQHYGIEVAGRHAVVIGRSPVVGRPLALLLLARDATVTICHRRTPDLAKLTRQADLLFVAAGQPHLVKPDMVAPGAVVIDFGVSVRDGRLIGDVDPAVAEVASALTPVPGGTGPVTTAVLALNLLRLAGLLEENDLFPGAP | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30631
Sequence Length: 288
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q5WE80 | MVNGINHMTFSVSNMDKAVSFYKHVFMEAPLVLGEKTAYFTIGGTWLALNLQPDIDRKEIRQSYTHIAFSIEESQLDAFYTRLLEAGADILPGRKRQVETEGKSIYFRDPDGHLLEVHTGTLAERLAHYEKTAPDMLVNIDEQNKK | Function: Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
Sequence Mass (Da): 16647
Sequence Length: 146
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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O31817 | MEIKGINHLLFSVSHLDTSIDFYQKVFGAKLLVKGRTTAYFDMNGIWLALNEEPDIPRNDIKLSYTHIAFTIEDHEFEEMSAKLKRLHVNILPGRERDERDRKSIYFTDPDGHKFEFHTGTLQDRLRYYKQEKTHMHFYDETAF | Function: Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
Sequence Mass (Da): 17172
Sequence Length: 144
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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Q99958 | MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYSAGMGRSYAPYHHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKEKEERAHLKEPPPAASKGAPATPHLADAPKEAEKKVVIKSEAASPALPVITKVETLSPESALQGSPRSAASTPAGSPDGSLPEHHAAAPNGLPGFSVENIMTLRTSPPGGELSPGAGRAGLVVPPLALPYAAAPPAAYGQPCAQGLEAGAAGGYQCSMRAMSLYTGAERPAHMCVPPALDEALSDHPSGPTSPLSALNLAAGQEGALAATGHHHQHHGHHHPQAPPPPPAPQPQPTPQPGAAAAQAASWYLNHSGDLNHLPGHTFAAQQQTFPNVREMFNSHRLGIENSTLGESQVSGNASCQLPYRSTPPLYRHAAPYSYDCTKY | Function: Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.
PTM: Phosphorylation regulates FOXC2 transcriptional activity by promoting its recruitment to chromatin.
Sequence Mass (Da): 53719
Sequence Length: 501
Subcellular Location: Nucleus
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Q61850 | MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYGAGMGRSYAPYHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVPKDKEERAHLKEPPSTTAKGAPTGTPVADGPKEAEKKVVVKSEAASPALPVITKVETLSPEGALQASPRSASSTPAGSPDGSLPEHHAAAPNGLPGFSVETIMTLRTSPPGGDLSPAAARAGLVVPPLALPYAAAPPAAYTQPCAQGLEAAGSAGYQCSMRAMSLYTGAERPAHVCVPPALDEALSDHPSGPGSPLGALNLAAGQEGALGASGHHHQHHGHLHPQAPPPAPQPPPAPQPATQATSWYLNHGGDLSHLPGHTFATQQQTFPNVREMFNSHRLGLDNSSLGESQVSNASCQLPYRATPSLYRHAAPYSYDCTKY | Function: Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.
PTM: Phosphorylation regulates FOXC2 transcriptional activity by promoting its recruitment to chromatin.
Sequence Mass (Da): 52874
Sequence Length: 494
Subcellular Location: Nucleus
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Q89WC9 | MPELPEVETVRRGLQPVMEGAKIVVAEARRPDLRFPFQPDFVARLQGQVVTGLGRRAKYLMADLASGDVLLMHLGMSGSFRVIKPDNDAAPGEFHYPRGKDTTHDHVLFRMSSGADIVFNDPRRFGYMKVIARNALEDEPLLRGLGPEPLGNEFDAAMLARSCEGKATSLKAALLDQRVVAGLGNIYVCEALHRSHLSPRRIAATLATRKGEPTDHAKRLVGAIHTVLNDAIKAGGSSLRDHRQTTGELGYFQHSFKVYDREGETCKTPACGGTIKRFTQNGRSTFWCPKCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 32309
Sequence Length: 293
EC: 3.2.2.23
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A9HI30 | MPELPEVETVMRGMRLHLDGKTIARVAVRRADLRFPFPADLVARLEGATITGFARRAKYILIRLDTGDTLLLHLGMSGRVLLSLPGDAPVPDRHEHFFFETTDGTRCGLIDPRRFGAVDLMPTAEERAHRLLARLGPEPLGNQFSQHWLQEVLARRRTSIKAALLDQTVVAGLGNIYVSEALFRAGIHPARLACTLDAAEDARLVQAIRAVLREAIAAGGSSLRDYVQPDGELGYFQHAWRVYGRAGQGCPDCPGPPACHGVERLEQAGRSSFFCPLCQPPPGKVS | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 31343
Sequence Length: 286
EC: 3.2.2.23
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Q7VN67 | MPELPEVETCLRGIEPYLAGQTIQQIVIRTPKLRWPISAELCAMSGAKILALSRRAKYLIIHTERGDILVHLGMSGSLTLLNSSQPTKASKHDHVDLITEAGIILRYNDPRKFGAWLWAKQAENYPLITKLGPEPLSDTFTSDYLFKKSRNKTVAVKNFIMNNDIVVGVGNIYASESLFMAGVHPELAAQNLTEKQCVQLRNVIQAVLTKAIIQGGTTLKDFTQPDGKPGYFAQVLQVYGRKGEECRECGTLIQAKVIGQRNSYFCPDCQPLPK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 30443
Sequence Length: 274
EC: 3.2.2.23
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A1WZG2 | MPELPEVETTRRGLQVHLVGRTLQRVVVRQRQLRYPVPARVEAAVVGEEVVALERRAKYLLIRLGGGAWLLLHLGMSGSLRLVAETDAPGRHDHVDLVLNDGRAVRLTDPRRFGCLLLGDGDPQDHRLLRRLGPEPLGSAFDGAVLHRAARGRRVAVKALLMDATVVVGVGNIYANEALFRAGIRPDRAAGRIARARYDRLAGAVRAVLEAALAAGGTTLRDFTDGSGEPGYFAVNLSVYGASVCPVCGGALRQIRLAQRGTWFCPRCQR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 29314
Sequence Length: 270
EC: 3.2.2.23
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B0TER7 | MPELPEVETVRRSLAGRITGLTIEKVELRLPKIAFALPGTLFTDALRGRRIIELGRRGKYLLLHLDGDETLVIHLRMTGRLIHLRPEEREEPEAAHTHAVFFLDDGSLLRYTDVRQFGTLTLMTREAALRQPGKGRLGPEPLGQDFSFVDFRNALVKRKTKLKPLLLDQSFLAGLGNIYADEALARARLHPDRTADSLDDEESRRLYDCIRTVLQEGIDAKGTSFRDYVDGEGRKGEFQEKLWVYGRGGNPCRRCGGEILREKRAGRSTHFCPRCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 31478
Sequence Length: 277
EC: 3.2.2.23
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P23900 | MSNPQKALNDFLSSESVHTHDSSRKQSNKQSSDEGRSSSQPSHHHSGGTNNNNNNNNNNNNSNNNNNGNDGGNDDDYDYEMQDYRPSPQSARPTPTYVPQYSVESGTAFPIQEVIPSAYINTQDINHKDNGPPSASSNRAFRPRGQTTVSANVLNIEDFYKNADDAHTIPESHLSRRRSRSRATSNAGHSANTGATNGRTTGAQTNMESNESPRNVPIMVKPKTLYQNPQTPTVLPSTYHPINKWSSVKNTYLKEFLAEFMGTMVMIIFGSAVVCQVNVAGKIQQDNFNVALDNLNVTGSSAETIDAMKSLTSLVSSVAGGTFDDVALGWAAAVVMGYFCAGGSAISGAHLNPSITLANLVYRGFPLKKVPYYFAGQLIGAFTGALILFIWYKRVLQEAYSDWWMNESVAGMFCVFPKPYLSSGRQFFSEFLCGAMLQAGTFALTDPYTCLSSDVFPLMMFILIFIINASMAYQTGTAMNLARDLGPRLALYAVGFDHKMLWVHHHHFFWVPMVGPFIGALMGGLVYDVCIYQGHESPVNWSLPVYKEMIMRAWFRRPGWKKRNRARRTSDLSDFSYNNDDDEEFGERMALQKTKTKSSISDNENEAGEKKVQFKSVQRGKRTFGGIPTILEEEDSIETASLGATTTDSIGLSDTSSEDSHYGNAKKVT | Function: Channel protein for glycerol. Has a role in both glycerol influx and efflux. Plays a role in osmoregulation: under osmotic stress the channel is apparently closed to allow accumulation of glycerol in the cell under hyperosmotic conditions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73877
Sequence Length: 669
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Leu-Ala/Ser (NPA).
Subcellular Location: Membrane
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P00541 | ASGQLHRPQPQEHTSTSAAAGTWRHTQASESRHRLPHCSAAPSHQDHSAMGFGPELWCPKGHSELLRLQDSELRLLELMKKWMSERAKSDREYAGMLHHMFSQLGSEEPPPALPLQEDRQSVCSTDQERSGVTALETIKNHISGIFSPRFSLPPPVPLIPEVQKPLCQQAWYHGAIPRSEVQELLKCSGDFLVRESQGKQEYVLSVLWDGQPRHFIIQAADNLYRLEGDGFPTIPLLIDHLLQSQQPITRKSGIVLTRAVLKDKWVLNHEDVLLGERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPELKAKFLQEARILKQYNHPNIVRLIGVCTQKQPIYIVMELVQGGDFLSFLRSKGPHLKMKELIKMMENAAAGMEYLESKHCIHRDLAARNCLVTEKNTLKISDFGMSRQEEDGVYASTGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWEAFSLGAVPYANLSNQQTREAIEQGVRLEPPEQCPEDVYRLMQRCWEYDPRRRPSFGAVHQDLIAIRKRHR | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 60506
Sequence Length: 533
Domain: The F-BAR domain is truncated and contains only the FCH region (the coiled-coil region is missing).
EC: 2.7.10.2
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Q9NH03 | MNNQSLQRAAMISEHLAPTSELNMNQTSAPIKTAKEELADFVEIFPILTNEILKELPGMDMPPQTIAWVEKMINVNVSGGKMNRGLTVLHSLQLLVEGRQLSRSEIFLANVLGWCVEWLQAFFLVADDIMDQSITRRGQPCWYRQANPISNNGTIGSIAINDSFILESCIYILIKKYFRNEPYYADILDIFHETSYQTELGQLLDLTTQPNRGDFSLFTLNTYRRIVKYKTAYYSFYLPVALAMLMAGITSTPAFSTAKDILLPMGEFFQVQDDFLDCYGSPAVIGKIGRDIEENKCSWMICQAILNGTPEQINLLKKHYGLDNPTDVELVKKIYGEIGLKKIFKDYEDESYAFLISKIKSVRIMPQEVFIKLLSKIYKRDL | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a sterol precursor. Involved in the inhibition of cell growth.
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 43590
Sequence Length: 382
Pathway: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.10
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Q4JHN6 | MSDLKTRFLEVYSVLKSELLNDPAFEFTDDSRQWVERMLDYNVPGGKLNRGLSVIDSYKLLKEGKELSDDEIFLSSALGWCIEWLQAYFLVLDDIMDSSHTRRGQPCWFRLPKVGMIAVNDGILLRNHIPRILKKHFRQKPYYVDLLDLFNEVEFQTASGQMIDLITTLVGEKDLSKYSLPIHRRIVQYKTAYYSFYLPVACALLMSGEDLEKHTNVKDILIEMGTYFQVQDDYLDCFGAPEVIGKIGTDIEDFKCSWLVVKALELSNEEQKKFLHENYGKDDPASVAKVKELYNTLKLQDVFAEYESKSYDKLIKFIEAHPSQAVQAVLKSFLGKIYKRQK | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways . Promotes the accumulation of ginsenosides .
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 39627
Sequence Length: 342
Pathway: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.10
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P42512 | MKTETKVIKGRQGIARNRHTPLCLGLLLALSPLAAAVADARKDGETELPDMVISGESTSATQPPGVTTLGKVPLKPRELPQSASVIDHERLEQQNLFSLDEAMQQATGVTVQPFQLLTTAYYVRGFKVDSFELDGVPALLGNTASSPQDMAIYERVEILRGSNGLLHGTGNPAATVNLVRKRPQREFAASTTLSAGRWDRYRAEVDVGGPLSASGNVRGRAVAAYEDRDYFYDVADQGTRLLYGVTEFDLSPDTLLTVGAQYQHIDSITNMAGVPMAKDGSNLGLSRDTYLDVDWDRFKWDTYRAFGSLEQQLGGGWKGKVSAEYQEADSRLRYAGSFGAIDPQTGDGGQLMGAAYKFKSIQRSLDANLNGPVRLFGLTHELLGGVTYAQGETRQDTARFLNLPNTPVNVYRWDPHGVPRPQIGQYTSPGTTTTTQKGLYALGRIKLAEPLTLVVGGRESWWDQDTPATRFKPGRQFTPYGGLIWDFARDWSWYVSYAEVYQPQADRQTWNSEPLSPVEGKTYETGIKGELADGRLNLSLAAFRIDLENNPQEDPDHPGPPNNPFYISGGKVRSQGFELEGTGYLTPYWSLSAGYTYTSTEYLKDSQNDSGTRYSTFTPRHLLRLWSNYDLPWQDRRWSVGGGLQAQSDYSVDYRGVSMRQGGYALVNMRLGYKIDEHWTAAVNVNNLFDRTYYQSLSNPNWNNRYGEPRSFNVSLRGAF | Function: High-affinity outer membrane receptor required for the transport of Fe(3+)-pyochelin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79992
Sequence Length: 720
Subcellular Location: Cell outer membrane
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P42513 | MPRQSGFGWAWRVPLALAGSLAAATASGYLLTRGLPLDDPLERLYAGLFGALGVGLLLLVGGLLARGPGNFAWRLGGSLLVLGLALWLLAGRG | Function: May play some role in transport of Fe(3+)-pyochelin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9569
Sequence Length: 93
Subcellular Location: Cell membrane
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Q81L65 | MKKILSIFIVVFLFAVGCGQQKEEKKETKADNKNQAITIKHAEGETKLDKPAKKVVVLEWVYSEDLLALGVQPVGMADIKNYNKWVNTKTKPSKDVVDVGTRQQPNLEEISRLKPDLIITASFRGKAIKNELEQIAPTVMFDPSTSNNDHFAEMTETFKQIAKAVGKEEEGKKVLADMDKAFADAKAKIEKADLKDKNIAMAQAFTAKNVPTFRILTDNSLALQVTKKLGLTNTFEAGKSEPDGFKQTTVESLQSVQDSNFIYIVADEDNIFDTQLKGNPAWEELKFKKENKMYKLKGDTWIFGGPESATSLATQVADVMTAKK | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36074
Sequence Length: 324
Subcellular Location: Cell membrane
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Q81L64 | MNNLQHTLRASLVFGGGGALLLLLFFIHIGQGQANISYSMIIDALISPNQSLEHQTLIMLRLPRAVIAILAGGALAASGVILQTLTKNPLAESSTMGIHSGAYFFLVAATIFLPKGLQINSLLFTFIGGAITALFVYRISGEKKGTPLRMALAGMVVTLMLSAFTGTMQLFYENETAGLFLWGAGSLIQNNWDGVQFSFPFIIISFLVLLGISRKLNILLLGDDVAVSLGEKTAVTRLIAFIAAIFLTAVIVTVVGPIGFVGLVAPHLMRLIGYRQHFTLLLSSFLWGAVLLLGADVAGRLIDPTGAELPVGAVTAMIGSPWLIYLVYRMMKSKQYMNDNGANTAGASSRYYSYKKVIIISITLCIVTIALGVTIGSNAYIESITNVISGQLTQFDKNMMMNLRLPRMLVAAIAGACLAISGLVFQGILRNPLADPSIIGISSGAGVGALTIMYVFPTLPGFFLPIGAFIGGLLAVGIVLFFSWKSGFSPTALALIGIGISALGSAIIQIFIVKANLNVAAALTWLSGSTYARGWNHLENIILYPSLILVLIIFFLIKQLDVLVLGDDLATGLGQPVNKTRLALIVLATLLASVNIAAVGTIAFLGLVAPHLARIVVGMNHQRLFVCSALFGAILLSIADLLGRTIAYPKEIPSGLVVAVLGAPYFLWLMRKSGKKVN | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72025
Sequence Length: 678
Subcellular Location: Cell membrane
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Q81LM1 | MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLMARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFGRGPHKSWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGVPEEVLCHEMFQHIFGIEVDIFQGSEKPFFTPKRISKKGGAKCEQKNVLPLS | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for energy coupling to the transport system.
Catalytic Activity: a Fe(III)-siderophore(out) + ATP + H2O = a Fe(III)-siderophore(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30996
Sequence Length: 272
Subcellular Location: Cell membrane
EC: 7.2.2.-
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Q81V82 | MQKALETKRLTLSYGETIIIDELNLEIPKGEITIFIGSNGCGKSTLLRSLARLLKPTTGDILLDNQAIQSMQTKQIARQMAILPQGPQAPEGLTVLQLVKQGRYPYQTWLKQWSEKDEEMVQNALAATGMTEFAERDVHALSGGQRQRAWIAMTLAQDTDIILLDEPTTYLDMTHQIEVLDLLFELNETEQRTIVMVLHDLNLACRYADNIVAIQDKQIYAQGKPEEVVDEKLVRDVFRMECQISTDPLFGTPLCIPHGKGRRVRKEVAHAMR | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for energy coupling to the transport system.
Catalytic Activity: a Fe(III)-siderophore(out) + ATP + H2O = a Fe(III)-siderophore(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30887
Sequence Length: 273
Subcellular Location: Cell membrane
EC: 7.2.2.-
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P48632 | MPAPHGLSPLSKAFLMRRAFQRRILPHSLAMALSLPLAGYVQAQEVEFDIPPQALGSALQEFGRQADIQVLYRPEEVRNKRSSAIKGKLEPNQAITELLRGTGASVDFQGNAITISVAEAADSSVDLGATMITSNQLGTITEDSGSYTPGTIATATRLVLTPRETPQSITVVTRQNMDDFGLNNIDDVMRHTPGITVSAYDTDRNNYYARGFSINNFQYDGIPSTARNVGYSAGNTLSDMAIYDRVEVLKGATGLLTGAGSLGATINLIRKKPTHEFKGHVELGAGSWDNYRSELDVSGPLTESGNVRGRAVAAYQDKHSFMDHYERKTSVYYGILEFDLNPDTMLTVGADYQDNDPKGSGWSGSFPLFDSQGNRNDVSRSFNNGAKWSSWEQYTRTVFANLEHNFANGWVGKVQLDHKINGYHAPLGAIMGDWPAPDNSAKIVAQKYTGETKSNSLDIYLTGPFQFLGREHELVVGTSASFSHWEGKSYWNLRNYDNTTDDFINWDGDIGKPDWGTPSQYIDDKTRQLGSYMTARFNVTDDLNLFLGGRVVDYRVTGLNPTIRESGRFIPYVGAVYDLNDTYSVYASYTDIFMPQDSWYRDSSNKLLEPDEGQNYEIGIKGEYLDGRLNTSLAYFEIHEENRAEEDALYNSKPTNPAITYAYKGIKAKTKGYEAEISGELAPGWQVQAGYTHKIIRDDSGKKVSTWEPQDQLSLYTSYKFKGALDKLTVGGGARWQGKSWQMVYNNPRSRWEKFSQEDYWLVDLMARYQITDKLSASVNVNNVFDKTYYTNIGFYTSASYGDPRNLMFSTRWDF | Function: Receptor for the siderophore ferripyoverdine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91167
Sequence Length: 815
Subcellular Location: Cell outer membrane
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A0A1L7U2E9 | MSLPKAQILVVVTVGGSTNSAPILEICSILAARGHTIDFATLSGRQKLVDNYPFVKKVHIVGPAISAEEDEKHYILFSRWNWNTARGKRDIVKGKMAFDAFWPFTYRGLKEVITTTKPDFIFSDFHVEAALDVCNEFRLPHAVMWPQMPWLMMPQKYIPGQPGMQQRCLTSEHASIYDRLFEMTFLLRSAPFFLHWIFWTKAMRRKEGVAPRPRHSKPDYLVFMNNFYGMETPRDTPPLVHPVGPILADSYPALDGDIKSFVETHQKIALVAFGTHVILDDGKIFKIIDGLADAISSGVIDGVVWALSARSRGQLDTSIRVPSLHLSHLTIDQLFKNQDQAWHFATWVPQRSVLEHDSTIIFVTHAGPSSVNESIFHGVPMVAMGIFGDQMVTTLRLERSGVAVRLDKETFDAASLTTAIRTILLFDKESFQRNVKRMKRIAMVGSRKKHFAANVIEEHLYDWDGRFENSILDLKACSNRKRGFLQASNSKDMYPRGKELRPMHLQTPDVRMSWIKLNNIDVALLFFILLGIISWITRAAANMVRL | Function: UDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem-dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C-methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C-alpha-methylation reactions of the nonaketide, while other alpha-carbons are non- or mono-methylated only. While the origin of the 4'-deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62050
Sequence Length: 546
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 2.4.1.-
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A0A1L7TZY0 | MRILCLHGMGTNSKVLEMQTSALRHQLSHSQSHKYEYVDGGEPMPPAPGIEAFIGQDESLAYYHPHSAKSILTAIDDLWEYIAEEGPFDGVLGFSQGASLAAMIIARAHHSDPPPFQFAIFFCAGLPYCEKSLSAGEVKFLRAEATQGPVIHVPTAHIFGKKDPDVSYSKAMTELCHPWGRVLLDHGAGHEIPRVPVETVDDMARAVEKVVTKAVIGQ | Function: Esterase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem-dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C-methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C-alpha-methylation reactions of the nonaketide, while other alpha-carbons are non- or mono-methylated only. While the origin of the 4'-deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).
Sequence Mass (Da): 23787
Sequence Length: 218
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.2.-
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A0A1L7TV57 | MPNLEKEFHNGVNGLNGNTKIENDGCVNPHSLGIIGGGWYGCHIAATLLALGFRVKLFEQHERLLHEASGNNQFRLHMGFHYARHSGTRLQSRDGFLRFVEHYPELSRIVPYNIYAVPTQDSLLDYNTYKAIMASSGVAFTEGAPDGVHITNVDGIMCVPERVLLLTKARAYFEAALKGALELGRKVSSIQEADDGVLIDGEGFDFVVDATWGHYMDLDLQVIYEATLLLYYEGPPEFPAVTLVDGPLASVYPTEVPGVFTLSSVPHTPLGQFKTAAEARAARDGVSPATISAKRALMEEQIMHYLPTFLETFRYIGPQLAVKTKPLGAYDDRSCRVSRRGRMFSVMSGKIDTIFFAHERILSLIDDES | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem-dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C-methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C-alpha-methylation reactions of the nonaketide, while other alpha-carbons are non- or mono-methylated only. While the origin of the 4'-deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).
Sequence Mass (Da): 40862
Sequence Length: 369
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.13.-
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A0A1L7TV54 | MSETTGLPLKHLQGSPPGTPVNTNNESNEASPDDGCRLPDTVTEAEASSDNHGSVLGDNNRNVEVAVGASDNATKQKVYHTGWRLHALTSALCLSLLLSTLETTIVSTALVSIVDALHGFNMAGWIVTSYLVTYTGFLIIYSKLSDIFGCKLMLLLAITIFTVFSMACGASDSMVPLIVFRAFQGMGGSGIYSLSTIMVPLMVPPEKYATYISIMSSTFILSSVLGPILGGAITDHTTWRWVFYFNGPGGALAAVLLAFSVPFNFPYGESDRFFHSLASKQMWKRVDFVGMTVSLAASILIIFALEQGGVAYPWGSGAIVSTFVLSGVLWIAFIAWERLLSKRDGVREPMFPWSLVHNRFVMGLLLNGFFTGFPFMAALINIPQRFQTVNMTSAINAGIRTLPLLLLSPLATAINGILVSKLRVPPLYTLFLGGSLQTIGVGLYSSLKSSTSIASAQYGYEAIMGLGFGFNLSTILMMVPLVVTEKDLAVTMGSVTQIRVLGGTIGLAVCSALLINHIKREAVKFLTAEQVAQILLSSENIGMLSIETQSRTRVLYADAYSEQMRVMLYFSIASILSLVLLVERQPRKAPAKPERAG | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64433
Sequence Length: 597
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
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A0A1L7U5T4 | MVGIALLGAGIFAREQHLPAIESVGHLNLKAVYSRSEEAAISLAKQARDRVDIYFDSPPTSGRSLDDLLARSDIAAVAACATILVQPLLIRKALRAGKHVLSEKPIAQDTATAMGLVQWYSSQSSPPIWAVAENFRFNESLRYAEMRTQEIGGELASFRLTYYGLIRKENKYFKTEWRKTPEFQGGFLLDSGIHFIASLRLLLRAVGQEPKEVMALSSLLKEHLHPVDTIHAVVSTIDSRHGTVCISFGVEHISTLEIEIISTRGVIVWTPVSVTSIIKSDSGESMNEKKEFIYNNGVKAEFEAFCQAILQNSPDPRQSPLEALRDLALLQSLLGSAACDGSMKLVKFE | Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem-dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C-methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C-alpha-methylation reactions of the nonaketide, while other alpha-carbons are non- or mono-methylated only. While the origin of the 4'-deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).
Sequence Mass (Da): 38471
Sequence Length: 349
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.1.-
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A0A1L7TV75 | MAIIPWKAIDESLSLRWKIIVTLLAIYTLRIIGTRITTTRARRKFREQHGCAPVTCQLPLKDPFFGIDFILKLMRVFKEKRLLETFANDFYKTVGITFLVERGSQQTIFTIDPENIKTVLALKFKDYGLAFRAPLFNPVTGGGMFVSDGEEWAHSRALMRPTFARDQVADLALTNRHVTDLVSKIPINTTFNLQELLFDFTMDTGTEFLFGESTDTLCNPTKASQEFTKAFDFTLKDVAYQARLGPLRRFQGSRSKALEVYQVCRSYVERYVDQAMALRTSTLTGEVTRENEPQNRHDSLLRQLARSGVSKEKIRAELLSVLIAARDTTSNLLGNLFFVLARRPDIWTKIRDEVKHLDTNEPTYEQLRHLTYAKYCINESLRLHPPVPSNGRMAYRDTILPHGGGPNGDHPIHVPKGSMVNYTVYAMHRRKDLYGQDAEEFRPERWESLRPSWFFLPFNGGPRICLGQQYAITESLLVIMRFAQEFTSIQSMDAKPWTEEIALGCGNANGVYVSFQKLK | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem-dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C-methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C-alpha-methylation reactions of the nonaketide, while other alpha-carbons are non- or mono-methylated only. While the origin of the 4'-deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59449
Sequence Length: 519
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P80489 | MTKVVEISPTTRLEGHSKLTLKVDDQGIVERGDWLSITPVRGIEKLAIGKTMEQVPKIASRVCGICPIAHTLASTEAMEASIGCEIPTDAKLLRTILHAANRIHSIALHNILILPDFYIPGTEKKFNLFANEQPARSVMARIVRIREIAQTIGAIAGGEAIHPSNPRIGGMYYNVSPRAKQKMADLAKEGLVLVHEQMEFMFDVIRNMQNREFVEVAGKQIPLPKKLGYHNQGVMATASMYGSSSLDDNPTWDFTRWKETRPWDWYMGEVTIDLEDPSYPIGGTTKIGTKANPQMEACTGVPTYDGQPVEVGPRARLATFKNFDEKGTFAQHIARQMEYPDCCYTILRCLDNLNTSGKVLADHIPQGDGSMGWAANEAPRGSNIHLARVKDGKVLWYDMLVPTTWNFPTCSRALTGAPWQIAEMVVRAYDPCVSCATHMIVVNEEEKIVTQKLMQW | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50769
Sequence Length: 456
Subcellular Location: Cell membrane
EC: 1.12.98.1
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Q60338 | MEVNFVTNRIEIAPTTRHEGHAKLILEVDEEGIVNKAYYLNTTPVRGFETMLKGKPAEFAPIAVMRICGICQTTHGIASCEAIENAIDCEVPDDGLLLRELVGIGNRLHSHPLHHLLTIDDFLKPDETDLKIELIKLIQRMRKVGQLVVDIVGGEGIHPPNIVIGGMRTNITERAKSRLYYALRQYEKDAYELYEKYTELIERYLEEIGIPDLGAHEYPYIATHTTYGDRYAINWDDVTEIPAQRYYDDEEAKQTTTIQIPLYAGVPAEGGPRARMVKFGNFREGGSAMDINIARAQENLGAVYRALEILDELDLNGKTRAEVEYKDGFGIGVHEAPRATNTHMAEVGKDGKIKSYRIIAASTWNFPIVEKAIEGYPQQYAEVIMRAYDICASCATHVIVKDEETKEIIEVRKML | Cofactor: There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 46784
Sequence Length: 415
EC: 1.12.98.1
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P19496 | MSERIVISPTSRQEGHAELVMEVDDEGIVTKGRYFSITPVRGLEKIVTGKAPETAPVIVQRICGVCPIPHTLASVEAIDDSLDIEVPKAGRLLRELTLAAHHVNSHAIHHFLIAPDFVPENLMADAINSVSEIRKNAQYVVDMVAGEGIHPSDVRIGGMADNITELARKRLYARLKQLKPKVDEHVELMIGLIEDKGLPKGLGVHNQPTLASHQIYGDRTKFDLDRFTEVMPESWYDDPEIAKRACSTIPLYDGRNVEVGPRARMVEFQGFKERGVVAQHVARALEMKTALARAIEILDELDTSAPVRADFDERGTGKLGVGAIEGPRGLDVHMAQVENGKIQFYSALVPTTWNIPTMGPATEGFHHEYGPHVIRAYDPCLSCATHVMVVDDEDRSVIRDEMVRL | Cofactor: There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 44802
Sequence Length: 405
EC: 1.12.98.1
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Q00390 | MGKTVEINPTTRHEGHTKLVLKVDDDGIVEKGNYLSVTPVRGFEKFLVGKPAEFAPIAVSRFCGICPIAHATSAVEAIEDACGIVPPKDGLLLRELTGLGNKMHSHPLHEFLIAPDFIPEKDRVEYITRIQQMRKTGQYIVDTIGGEAIHAPNIKVGGMLKSITPSAVSKIYYKCKEFEKLAKEQVEYLIPIFENRTLVDGTEIPEKLGYHDFGYLATDSTYGNRENIEQKKVHEYTPYDVYEKEVAVQACQLFQEYNGRLMEVGPRARFAKFHDFKEKGAMAIHIARAYENVIHVKRAMEIIEELNVDGLTRAKDPILGDGEKLGLGVHEAARGHNTHQASIDEKGRITYYNAIVATTWNIPLIGKAVEAHYKFAEHVVRAYDPCVSCATQHDILRL | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 44612
Sequence Length: 398
EC: 1.12.98.1
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P19499 | MVLGTYKEIVSARSTDREIQKLAQDGGIVTGLLAYALDEGIIEGAVVAGPGKEFWKPEPMVAMTSDELKAAAGTKYTFSPNVLMLKKAVRQYGIEKLGTVAIPCQTMGIRKAQTYPFGVRFVADKIKLLVGIYCMENFPYTSLQTFICEKLGLNMELVEKMDIGKGKFWVYTQDDVYTLPLKETHGYEQAGCKICKDYVAELADVSTGSVGSPDGWSTVITRTDSGDSILKQAVEAGIFETKPIEEVKPGLGLLEKLSAQKKEKAEKNIAARKEMGLPTPY | Cofactor: There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 30771
Sequence Length: 281
EC: 1.12.98.1
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P80491 | MTNKIKIGHVHMSGCTGCLVSLADNNLGLIKILDDYADLVYCLTLADVRHIPEMDVALVEGSVCLQDHESVEDIKETRKKSKIVVALGSCACYGNITRFSRGGQHNQPQHESYLPIGDLIDVDVYIPGCPPSPELIRNVAVMAYLLLEGNEEQKELAGKYLKPLMDLAKRGTSGCFCDLMYDVINQGLCMGCGTCAASCPVHAITLEFGKPQGERDLCIKCGSCYGACPRSFFNLDVIPEFENINEIIANALKEGESDD | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 28241
Sequence Length: 259
EC: 1.12.98.1
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P19498 | MAEENAKPRIGYIHLSGCTGDAMSLTENYDILAELLTNMVDIVYGQTLVDLWEMPEMDLALVEGSVCLQDEHSLHELKELREKAKLVCAFGSCAATGCFTRYSRGGQQAQPSHESFVPIADLIDVDLAIPGCPPSPEIIAKAVVALLNNDMEYLQPMLDLAGYTEACGCDLQTKVVNQGLCTGCGTCAMACQTRALDMTNGRPELNSDRCIKCGICYVQCPRSWWPEEQIKKELGL | Cofactor: There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 25817
Sequence Length: 236
EC: 1.12.98.1
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Q00393 | MVKIAHIHMSGCTGCLISLTDTYEKLLDILGSVELVYALTLTGEKTEITETDDKILIERDIPGGIDIALVEGSVCLDDHHSMDDILTTRKNSKKSLVALGACAASGGVTRFRRVGQMSQPSHASFVPIGDVIKVDLALPGCPPSTESIVKLLTAALEGDMEYLEPFAEIAKYGKDACGCDVIKEVINKSLCMGCGTCAAACQVNAIDMVEAKPNINSEFCIKCGICSAQCPRVRFPEIIRKLE | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 26040
Sequence Length: 243
EC: 1.12.98.1
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Q39101 | MASNALSSFTAANPALSPKPLLPHGSASPSVSLGFSRKVGGGRAVVVAAATVDTNNMPMTGVVFQPFEEVKKADLAIPITSHASLARQRFADASEAVINEQINVEYNVSYVYHSMYAYFDRDNVAMKGLAKFFKESSEEERGHAEKFMEYQNQRGGRVKLHPIVSPISEFEHAEKGDALYAMELALSLEKLTNEKLLNVHKVASENNDPQLADFVESEFLGEQIEAIKKISDYITQLRMIGKGHGVWHFDQMLLN | Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 28178
Sequence Length: 255
Subcellular Location: Plastid
EC: 1.16.3.1
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Q96540 | MASKALSSFTAKPAVSLLPHGVSSSASPSVMSLSFSRHTGGRGVVAASSTVDTNNMPMTGVVFQPFEEVKKADLAIPITSNASLARQRYADSSEAAINEQINVEYNVSYVYHSMYAYFDRDNVALKGLAKFFKESSDEEREHAEKFMEYQNQRGGRVTLHPIVSPISDFEHAEKGDALYAMELALSLEKLTNEKLLNLHRVASENNDPQLADFVESEFLGEQIEAIKKISDFITQLRMVGKGHGVWHFDQMLLN | Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 28169
Sequence Length: 254
Subcellular Location: Plastid
EC: 1.16.3.1
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P36088 | MGSSTGFHHADHVNYSSNLNKEEILEQLLLSYEGLSDGQVNWVCNLSNASSLIWHAYKSLAVDINWAGFYVTQASEENTLILGPFQGKVACQMIQFGKGVCGTAASTKETQIVPDVNKYPGHIACDGETKSEIVVPIISNDGKTLGVIDIDCLDYEGFDHVDKEFLEKLAKLINKSCVFK | Function: Catalyzes the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine. Does not act on S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated methionine sulfoxide. Involved in protection against oxidative stress.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (R)-S-oxide
Sequence Mass (Da): 19734
Sequence Length: 180
Subcellular Location: Cytoplasm
EC: 1.8.4.14
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Q9LMM2 | MGVGEMNKEVIDKVIKFLMMVILMGTIVIWIMMPTSTYKEIWLTSMRAKLGKSIYYGRPGVNLLVYMFPMILLAFLGCIYLHLKKSTTVNQFNSGVEKKRAKFGALRRPMLVNGPLGIVTVTEVMFLTMFMALLLWSLANYMYRTFVNVTSESAATDGNNLWQARLDLIAVRIGIVGNICLAFLFYPVARGSSLLAAVGLTSESSIKYHIWLGHLVMIIFTSHGLCYFIYWISKNQLVSKMLEWDRTAVSNLAGEIALVAGLMMWVTTYPKIRRRLFEVFFYSHYLYIVFMLFFVFHVGISHALIPLPGFYIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPMLMYSPTSTMFVNIPSISKLQWHPFTIISSSKLEPETLSVMIKSQGKWSTKLYDMLSSSSSDQINRLAVSVEGPYGPSSTDFLRHESLVMVSGGSGITPFISIVRDLFYMSSTHKCKIPKMTLICAFKNSSDLSMLDLILPTSGLTTDMASFVDIQIKAFVTREEKTSVKESTHNRNIIKTRHFKPNVSDQPISPILGPNSWLCLAAILSSSFMIFIVIIAIITRYHIHPIDQNSEKYTWAYKSLIYLVSISITVVTTSTAAMLWNKKKYYAKNDQYVDNLSPVIIESSPQQLISQSTDIHYGERPNLNKLLVGLKGSSVGILVCGPKKMRQKVAKICSFGSAENLHFESISFSW | Function: Ferric chelate reductase involved in iron reduction in roots (By similarity). May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79600
Sequence Length: 704
Subcellular Location: Membrane
EC: 1.16.1.7
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P92949 | MEIEKSNNGGSNPSAGEEFKDMIKGVTKFLMMVIFLGTIMLWIMMPTLTYRTKWLPHLRIKFGTSTYFGATGTTLFMYMFPMMVVACLGCVYLHFKNRKSPHHIDRETKGGVWSKLRKPMLVKGPLGIVSVTEITFLAMFVALLLWCFITYLRNSFATITPKSAAAHDESLWQAKLESAALRLGLIGNICLAFLFLPVARGSSLLPAMGLTSESSIKYHIWLGHMVMALFTVHGLCYIIYWASMHEISQMIMWDTKGVSNLAGEIALAAGLVMWATTYPKIRRRFFEVFFYTHYLYIVFMLFFVLHVGISFSFIALPGFYIFLVDRFLRFLQSRENVRLLAARILPSDTMELTFSKNSKLVYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSIVIKKEGKWSTKLHQRLSSSDQIDRLAVSVEGPYGPASADFLRHEALVMVCGGSGITPFISVIRDLIATSQKETCKIPKITLICAFKKSSEISMLDLVLPLSGLETELSSDINIKIEAFITRDNDAGDEAKAGKIKTLWFKPSLSDQSISSILGPNSWLWLGAILASSFLIFMIIIGIITRYYIYPIDHNTNKIYSLTSKTIIYILVISVSIMATCSAAMLWNKKKYGKVESKQVQNVDRPSPTSSPTSSWGYNSLREIESTPQESLVQRTNLHFGERPNLKKLLLDVEGSSVGVLVCGPKKMRQKVAEICSSGLAENLHFESISFSW | Function: Flavocytochrome that transfers electrons across the plasma membrane to reduce ferric iron chelates to form soluble ferrous iron in the rhizosphere. May be involved in the delivery of iron to developing pollen grains. Acts also as a copper-chelate reductase. Involved in glycine betaine-mediated chilling tolerance and reactive oxygen species accumulation.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81501
Sequence Length: 725
Domain: The C-terminus is probably located inside the membrane.
Subcellular Location: Cell membrane
EC: 1.16.1.7
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F4I4K7 | MAARGRLVVARGNRSFSSIIRKYSLKRETNKKVIKNVIKLLTMVILMGTVVIWIMMPTSTYKKIWLKSMRAKLGKSIYFGKPGVNLLVYMFPMILLASLGSIYLHLKKQTRVNQFNSRMDRKKIDKFGALKRPMLVKAGLGIVTVTEVMFLMMFMALLLWSLANYFYHTFVTITPQSLPTDGDNLWQARLDSIAVRLGLTGNICLGFLFYPVARGSSLLAAVGLTSESSTKYHIWLGNLVMTLFTSHGLCYCIYWISTNQVSQMLEWDRTGISHLAGEIALVAGLLMWATTFPAIRRRFFEVFFYTHYLYMVFMLFFVFHVGISYALISFPGFYIFMVDRFLRFLQSRNNVKLVSARVLPCETVELNFSKNPMLMYSPTSILFVNIPSISKLQWHPFTITSSSKLEPKKLSVMIKSQGKWSSKLHHMLASSNQIDHLAVSVEGPYGPASTDYLRHDSLVMVSGGSGITPFISIIRDLLYVSSTNAYKTPKITLICAFKNSSDLSMLNLILPNSTEISSFIDIQIKAFVTREKVSTCNMNIIKTLSFKPYVSDQPISPILGPNSWLWLATILSSSFMIFIIIIAIISRYHIYPIDQSSKEYTSAYTSLIYLLAISISVVATSTVAMLCNKKSYFKGLYQNVDALSPLMIESSPDQLLPEFTNIHYGERPNLNKLLVGLKGSSVGVLVCGPRKMREEVAKICSFGSAANLQFESISFNW | Function: Ferric chelate reductase involved in iron reduction in roots. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80934
Sequence Length: 717
Subcellular Location: Mitochondrion membrane
EC: 1.16.1.7
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Q9FLW2 | MGNMRSLVKMLMVVLFLGWIFVWIMISTNRFQNIWTPKLAKYLKTTYFGPQGMNLVLLTVPMMFIAVLSCVYLHTQKQPSQTQSLYKCREWKVKGRMGRVMMVMNPLGIVTATELTFSLLFLALLVWALSNYLYLSYHVHLHNHDNANDMCRWQAKFRAFGLRIGYVGHYCWAFLFFPVTRASTILPLVGLTSESSIKYHIWLGHVSNFCFLVHTVVFLIYWAMVNKLMETFAWNATYVPNLAGTIAMVIGIAIWVTSLPSFRRKKFEIFFYTHHLYGLYIVFYAIHVGDSWFCMILPNIFLFFIDRYLRFLQSTKRSRLVSAKILPSDNLELTFAKTSGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVIRKQGSWTQKLYTHLSSSIDSLEVSTEGPYGPNSFDVSRHDSLILVGGGSGVTPFISVIRELIFQSQNRSTKLPNVLLVCAFKNYHDLAFLDLIFPSDISVSDISKLNLRIEAYITREDKKPETTDDHKLLQTKWFKPQPLDSPISPVLGPNNFLWLGVVILSSFVMFLLLIGIVTRYYIYPVDHNTGSIYNFTYRVLWVMFLGCVCIFISSSIIFLWRKKENKEGDKDSKKQVQSVEFQTPTSSPGSWFHGHERELESVPYQSIVQATSVHFGSKPNLKKILFEAEGSEDVGVMVCGPKKMRHEVAKICSSGLAKNLHFEAISFNW | Function: Ferric chelate reductase probably involved in iron reduction in shoots. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates. May act in iron metabolism in reproductive organs . May function as root surface cupric chelate reductase and participate in the reduction of Cu(2+), for Cu(+) acquisition via Cu(+) transporters in response to copper deficiency .
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81166
Sequence Length: 707
Subcellular Location: Cell membrane
EC: 1.16.1.7
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Q3KTM0 | MDDHETPLLSKDLSSSSSSSSSSSSVVVSSLKWILKVVMSVIFVTWVVFLMMYPGSLGDQILTNWRAISSNTLFGLTGSMFLIFSGPILVIAILASLYLIISGEETVFTKKKITKFPRFRLWTFPVLVDGPFGVVSAAEFLGIMVFSVFFLWAIYAYTLRNLNVLDYFHVLPNNRSIFLLELTGLRFGMIGLLCMVFLFLPISRGSILLRLIDIPFEHATRYHVWLGHITMTFFSLHGLCYVVGWTIQGQLLELLFEWKATGIAVLPGVISLVAGLLMWVTSLHTVRKNYFELFFYTHQLYIVFVVFLALHVGDYLFSIVAGGIFLFILDRFLRFYQSRRTVDVISAKSLPCGTLELVLSKPPNMRYNALSFIFLQVKELSWLQWHPFSVSSSPLDGNHHVAVLIKVLGGWTAKLRDQLSTLYEAENQDQLISPESYPKITTCVEGPYGHESPYHLAYENLVLVAGGIGITPFFAILSDILHRKRDGKDCLPGKVLVVWAIKNSDELSLLSAIDIPSICHFFSKKLNLEIHIYVTRQSEPCLEDGMVHKVVHPSVKTPWTNGCSMSVLVGTGDNIWSGLYLIISTIGFIAMITLVDIFYINKYNITTWWYKGLLFVVCMVASVLIFGGLVVVFWHRWEHKTGEVEANGNDKVDLNGEETHNPSAAELKGLAIEEDVQNYTTIRYGTRPAFREIFESLNGKWGSVDVGVIVCGPATLQTTVAKEIRSHSIWRSANHPLFHFNSHSFDL | Function: Ferric chelate reductase involved in iron mobilization from the cytosol into the chloroplast. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates. Might be involved iron homeostasis in trichomes.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84126
Sequence Length: 747
Subcellular Location: Plastid
EC: 1.16.1.7
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Q8VY13 | MAKVLTLLVLRLLMNLLLIGWISLWIIKPTTIWIQSWRQAEDTARHTFFGYYGLNFAVFSFPPIALSIVGLIYLSLLPQHHHPTRGGRGAAITVSRPAIINSFIGIVSCFEILALLLFLLFLAWNFYARVSNDFKKLMPVKTMNLNLWQLKYYRVATRFGLLAEACLSLLLFPVLRGLSMFRLLNIEFAASVKYHVWFGTGLIFFSLVHGGSTLFIWTITHHIEEEIWKWQRTGRVYVAGLISLVTGLLMWITSLPQIRRKNFEVFYYTHHLYIVFLVAFLFHAGDRHFYWVLPGMFLFGLDKILRIVQSRSESCILSANLFSCKAIELVLPKDPMLNYAPSSFIFLNIPLVSRFQWHPFSIISSSSVDKHSLSIMMKCEGDWTNSVYNKIEEAANCENKINNIIVRVEGPYGPASVDFLRYDNLFLVAGGIGITPFLSILKELASKNRLKSPKRVQLVFAVRTFQDLNMLLPIASIIFNPIYNLNLKLKVFVTQEKKPSNGTTTLQEFLAQSQVQSIHLGTDEDYSRFPIRGPESFRWLATLVLITVLTFLGFLIGLSHFFIPSEHKNHSGVMKLAASGAMKTAKEKVPSWVPDLIIIVSYVIAISVGGFAATILQRRRKHKEAPRMSKEVVIKPEERNFTELKPIPITEEHEIHIGERPKLEEIMSEFEKNLRGWSSVGVLVCGPESVKEAVASMCRQWPQCFGVEDLRRSRMKMNLNFHSLNFNL | Function: Ferric chelate reductase probably involved in iron reduction in leaf veins for transport. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83230
Sequence Length: 728
Subcellular Location: Mitochondrion membrane
EC: 1.16.1.7
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Q04800 | MAINSSDKWTVIAICLILGILLAFILMFWLERFRVIIKSNAHKHDPSDKRQIWLEKYYLFVRQIYTYLVTHKVILTLIAVPVVFAISIPFIGMQTPASSHGKQTTQVSTGNWSKNAVAARLGFLACGLYVTSYFFSIKNNPFALLLISSHEKMNYVHRRLSQYAIMIGAIHGFAYIGLAAQGKRALLTARVTIIGYVILGLMVIMIVSSLPFFRRRFYEWFFVLHHMCSIGFLITIWLHHRRCVVYMKVCVAVYVFDRGCRMLRSFLNRSKFDVVLVEDDLIYMKGPRPKKSFFGLPWGAGNHMYINIPSLSYWQIHPFTIASVPSDDFIELFVAVRAGFTKRLAKKVSSKSLSDVSDINISDEKIEKNGDVGIEVMERHSLSQEDLVFESSAAKVSVLMDGPYGPVSNPYKDYSYLFLFAGGVGVSYILPIILDTIKKQSRTVHITFVWSARSSALLNIVHKSLCEAVRYTEMNINIFCHLTNSYPVEEVSSLNSQSARNYSLQYLNGRPDVNDYFKDFLHATGTQTAALASCGSDKLLRHLKSCVNTHSPSTVDLYQHYEEI | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity). Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores (By similarity). Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity). Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity).
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64092
Sequence Length: 564
Subcellular Location: Cell membrane
EC: 1.16.1.9
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O94727 | MILARDDKWTLGSIALIFVLLIGFALLFLLERFRVKEKSRTFKDCVNVYQCPSKGERVYLALRHWFIFLATHKAQMTLILSPLVMLVTIPFTGKETKNSIASYDWNLTGVAARLGYLSCGLFFVSYFFSLKNNPFCLMLFSSHEKMNYLHRWLSVYAVLISVLHGILFMIFSAQSYKPLLYDKISIYGYFITVVLFLMTVASLPSVRRKFFEWFFVLHHTCSVLIIFLIWLHHPRTIVYMKACIIIYAFDRGCRLFRSIWNRSNFRIYLLNEDMIYMVGRKPKRSFFALPWAAGSHVYINIPSLSYWQVHPFTLASAPFDDFIELFVAVHSGFTERLANRLYSMPHEYPNFSLAPGTPESLSNTYRELNSFKSYAVEIENTAQGHTYEPEDLYLETTVFMDGPYGTTSNVFKEYSYVLLIAGGVGFSYTLPILRDLILKECNVTSITFIWSCRSLSLLKVASKSLNSLLHQSNVRLKIINHFTGSISCKESSEFSNQTTENSEMEFFDDRPDLDMYIQKFFDYVGYQTAALAACGSQSFLKRIKNSVNKSISSTTDIYQHYEEL | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity). Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores (By similarity). Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity). Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity).
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65262
Sequence Length: 564
Subcellular Location: Cell membrane
EC: 1.16.1.9
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I1S165 | MTIQSTANHQDGYLPAILCLHGAGTNATIFNLQARTIVRCLKHKFRFIFVNAPFESLPGPGVIPTFAEIRPYLRWHCDENAIQEFDVSPELVDNERRLVRSMISDKIEQEATGPSLGIVGVMAFSQGTRVATGLCLDPEFGSSIQFAIIIAGTFPALSLENPVSDSETTNLFSGINGNKHEQLQIPSVHVQGTMDPWGPESARLLKECWSADLAMVVKFHGAHQVPTSKKDAQAVAQAVLSCWDSAQT | Function: Thioesterase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 . Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin . Prefusarielin is oxygenated at C15 and C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme . The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism .
Sequence Mass (Da): 27075
Sequence Length: 248
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.2.-
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A0A0E0RXA9 | MSVTRLSEPLQNILLQDLRNFYDRASRIATLSVSAIAAIKSAWTRGSPFAAATALYPTNEEGKYVIQAEGIRMEFTNYGGAVTNLWLNNSRGEEVDIVLGLDHARDYEDYPKNPYLNGAIGRYAGFMRGGRFDMDGESYQVATNAHNGSSTFNGGDRGWGRSILDIGSHTENSITFVLFDRSWNGFPGTAASCLTHTVTPYEWRVAFGVTPTKKPGPINMSQQAFFNLDGFKKKNLTGSVPVSDKTVRDHKLHLPLSGLRFETDALGLSTGDILGNPRGSEYDFWSASRRIGDVLEKPYMGICDRCQKRQYHNHNPSGAYDTIFQLGRSQPWNKEDVPAAILSSPESGISMKLYSDQEALHVHTWSQKEFPLKLKKGQGQGMVPQHGGISFEMQDWPDGLNHPEWRRESKTIWGMDGLYTAFSSYRFSVDKTEP | Function: Epimerase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 . Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin . Prefusarielin is oxygenated at C15 and C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme . The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism .
Sequence Mass (Da): 48477
Sequence Length: 434
Pathway: Secondary metabolite biosynthesis.
EC: 5.1.-.-
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I1S163 | MSVIGLWLVTVTATLSLFVWQLIFLLSIPKSIVVCLIAESLFFVAWFFYWTVIYPRYLTPFRHLPTPASRSILTGNQNGLFTENSWDVARRVSQTVPNSGLIRYYVALSNERILVTNTRALSDVLTNHSHDFGKSNLAKFALKRLTGNGLGFLEGNEHKVHRKNLMPAFTRKHVKELTPIFWDKAMEMVKGMEAEVRCGKDTSTQGTGIVEIHDWATRATLDIIGTAGFGYDFGTLHNPSNEIGQQYKKMFLEPSTAFNWLELLGNYIDFRFLMTLPVKKNRDLTAGSNFMREIAKKVIRERRHELFQRMTSQAGNMKNTKKDIITTALASDCFTDDQLVDHVMAFLVAGHESTATAFEWAMYELGHRPEMQKRVRDEVRTYLPSPSAGGVKNITFESVPYLQAICNEVLRLYPFLPFATRVAEKDTWVADQFVPKGTIVAYAAHISNRDSELWSGPALDAFDPERWMEPGKESSGGANSNYAMLTFSAGPKSCIGEAWTRAELPCLVGAMVGSFEIELVEGKQADGTVYPTVDFKMGKVLKSRDGVFVRLRRLEDW | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 . Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin . Prefusarielin is oxygenated at C15 and C16 by FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme . The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62897
Sequence Length: 557
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A0E0RXA7 | MTNLPSHHTAIVGSEDGSLKVAEQVPLPRLENDMILVRNTAVALNPIDGKMVGNLASVGAVAGMDYVGTVVGIGPKVKTASEIQLGDRVCGAVQGMHSLTPSVGAFAQFVGATDIVTLKVPPSMTVEDAATLGSGVGTIGLALFRSLDVPGYPEAPATERIPVLVYGGSTATGTLAIQLLKLSGLIPITTCSPHNFDLVKSFGAEAVFDYRRPETPDEIRKFTRNSLKYVLDCISEPETMQFCYKCIGRTGGKYTALEPFPQFLHTRPTIQPDWVLGPTLLGKPIGWGPPFERVGDPDVREFAIKWFATAQRLLDQGKLQTHPVKLMEGGFEGILCGLEMLKKKQVSGQKLVYMIPQVA | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 . Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin . Prefusarielin is oxygenated at C15 and C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme . The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism .
Sequence Mass (Da): 38517
Sequence Length: 359
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q556J4 | MVSNKNLLPIIYIFFIILYFGDVAKSQYFPLDKGATCQKYRGDSPGIQLCDGFLSNPNSIYINSTSSQEAIQAQGNLVRQYINFYKSFESCKNPRTFALLCAFLFPECEKYTDPVSKVTYAYPILPCYNNCLNMTTSCQISTSRLSCATKYTFENISYSVFPKNTTTYQIDSLSYTNTCENTDLIANSQNTSIQQCFEPLVYHVSTDEIHDKSIGYIFPSTNTTCVVGCPAPLYYANQWRNIYRLSDVLSILSCILTLFLVITLGIINPKVSRFDKINVMLLSSIFLQAFSGALMTFNGTENTLCPEDGRFASYIDRMCVATGFLLHGSSLLVVQWWCVLSFEVWFTIFQVGKKQKDRFIYYLVASLIIAWIPPIVSISKNEYSGGPANPFCWLTTFNYRRFAFWLPMGIFLCLGGVFLILLMREIYVIVSGNVQSTKESRFKVLKMEAKPIISLIMYFSCLLYLFIYDQWINNHMHVYTDSIPSYALCLLTSTSTNDCLLKAPDITGLGYFIYSIRVFGVYAFIIYGISKKTLQIWKYNYFVVFIGQKIEQFTNATTTAKSSNSNNSSTTNNISVKASSNMEYETRQENENGDSQSVELDSNSDAL | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68945
Sequence Length: 607
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Membrane
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A4J0S6 | MKKVPSDLEIAQAHEMIPIAEIAKNIGLGEDDIDLYGKYKAKISLDVLRKFNDRAMGKLIDITAITPTPLGEGKTVTTIGLCQGLGKIGKKVITTLRQPSMGPVFGIKGGAAGGGYSQVVPMEDINIHFTGDIHAVEAANNLLAAMIDTSILLGNPLNIDPMTVMWNRVLDTNDRALRDIVVGLGGKENGYPRQTSFDMAVASEVMAILALAENLHDLRQRLGRIIVAYTYDGKPVTAEDLKAAGAMTVIMKEALKPNLVQTLEGQACIMHAGPFANIAHGNNSVLADKIALNLADYVVTESGFGSDLGMEKFMDIKCRQSGLRPSCVVITCTIRALKMHGGLGNVVAGKPLPEELTRENLPALEKGCANLAHHIKVASYYGVPVVVSINRFTPDTDAEVDLVRKKALEAGALGAYPITVWAEGGEGAIELAEAVVAACEKTADFQLLYPDNLSIKEKIEVLATKVYNADGVVFEPLAERKIKQFEDLGLGHLPICMAKTHLSISHDPAMKGLPKNYIFPIRDIRASVGAGFLYPLAGAMRTMPGLGSKPAAHNVDIDEYGRTVGLF | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60771
Sequence Length: 567
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q8RHF4 | MTDIQIAQAAKKENIVEIAKKLGLTEDDIEQYGKYKAKVNLDVLQKNKRPNGKLILVTAITPTPAGEGKSTVTIGLTQALNKMGKLSAAAIREPSLGPVFGMKGGAAGGGYAQVVPMEDINLHFTGDMHAIGIAHNLISACIDNHINSGNALGIDVTKITWKRVVDMNDRALRNIVIGLGGKANGYPRQDSFQITVGSEIMAILCLSNSITELKEKIKNIVIGTSVTGKLIKVGDFHIEGAVAALLKDAIKPNLVQTLENTPVFIHGGPFANIAHGCNSILATKMALKLTDYVVTEAGFAADLGAEKFIDIKCRLGGLKPDCAVIVATVRALEHHGKGDLKAGLENLDKHIDNIKNKYKLPLVVAINKFITDTDEQINMIEKFCNERGAEVSLCEVWAKGGEGGIDLAEKVLKAIDNNKTEFDYFYDINLTIKEKIEKICKEIYGADGVIFAPATKKVFDVIEAEGLNKLPVCMSKTQKSISDNPALLGKPTGFKVTINDLRLAVGAGFVIAMAGDIIDMPGLPKKPSAEVIDIDENGVISGLF | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 58321
Sequence Length: 544
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q5V5Y2 | MEPIWELVEPWGLGLDDLQYFGEYTAKVKQHAIERLREQAENREQNLVLVTGMTPTPKGEGKTVTTVGLGQTLNHVGEEAMIAIREPSLGPVFGVKGGAAGGGRSQVLPMEDINLHFTGDLHALTSAHNLIAAMLDAKISQGDDLNIDINNVSWPRAIDMNDRALRETVVGLGGKTGGTPREDSFILTAASELMAVLCLASDIGDLKERVSRIIVAYDEDGDPVTVEDIEATGPATMLLRDAIKPNVVQTIEGTPALVHGGPFANIAHGTNSLVADKTAFGMGDYLVTEAGFGSDLGAEKFMDVVCRKGDMTPNAVVLVASVRALKYHGLNQWPVDYDEIGEAGVEAVEAGFSNLDKHARNLQKFGVPVVVSVNRFPDDTDEEVQAVLDHCREDLGVRAAESNVFSDGSEGGVDLAENVIEATEESNEEDFRMLYDDDDSIKEKIHTVATEIYGADDVKYTGGALDDIEQMNDLDFDDYPVVMSKTFHSLSDDASQKGAPEGWELEISEVYPSAGAGFLVALTADALTMPGLPARPAAADMDIDGDGNISGLF | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59251
Sequence Length: 553
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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A9B4H8 | MKTSLQIAAEATPRPITQIAEELAIAEQFVEPYGRYRAKINLDLLDASHDRPRGKQILVTAMTPTPLGEGKTATTIGLGMALSRLGKRAICTLRQSSLGPVFGIKGGGSGGGYSQVIPLEDSLMHLTGDIHAVTQAHNQIAAMTDNSWYQKNRLGIDPEQIQIRRVLDVNDRFLRSITIGQGGSQHGIPRQTGFDITAASELMAILALVSGENHADVMRDLRQRIGRMVVAFTRQGQPITADDIQAAGAATVIMRNAIHPTLMQTIENTPVLMHGGPFANIAHGNASVVADQVGLRIADYVVTEAGFAMDMGGEKFFDIKCRAFDAKPAVVVLVATIRALKAHSGRWNIKPGRDLPTDLLQENPDAVYAGGANLQKHIRNAQLFGLPVVVALNSFPDDHPSEIEAVREIAMSAGAFDVAVSKVFSQGGVGGEELAEKVLAAIDQAGQAQFLYELEQPLTAKIATIATKIYGAAEVSYSEAASEQLAKLEANGFGNLPICMAKTHLSISHDPALKGAPTGYSFPIREVRASIGAGFIYPIAGDMMTMPGLSANPAAQQIDIDEHGNTVGLF | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60778
Sequence Length: 570
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q1GA94 | MVKSDIEIAQAAEELPITDVAAKLGLTSQDLEPYGYDKAKVNWQAIKRSEENGHLGKLILVTSISPTPAGEGKSTMTIGIGDAINNQLGKKTVIALREPSMGPVFGMKGGAAGGGYAQVIPMEDINLHFTGDMHALTSAIDNLSALVDNYIYQGNELGLDPEKIVIKRGLDVNDRTLRKVTIGQGSKFNGVERPASFQLTVGHELMAILCLSKDIADLKERIGKVLVGYTYEDEPVFVKDLGFQGAIAALLSTALKPNLVQTLEHTPAFVHGGPFANIAHGNNSILSTNLALHLSDYVLSEAGFGSDLGGQKFLDFVSTKLEKKPDAAVVVATVRALKYQAEKSTDHLKEENLDSLKEGFANLDRHMNNVRSYNIPVLVVINKFPTDTEAELDLLKSLIEEQGFPCEIVTAHDEGSKGAKAAAEKIVELADKSDYEIKRSYDLDDDLETKIEKVAKRIYHAADVEYTDKAKDQLVKLKKMGKDKLPVIIAKTQYSFTDNVKELGAPTGFTLHVKGLSLRNGAGFVVVSTGHILDMPGLPKHPAALDIDVDETGKISGLF | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60503
Sequence Length: 559
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q9KLX7 | MLPDIEICRATPLAPIDTIAQKAGLHANEYESHGQHKAKVSLHCLERLANKPKGKFILVTAITPTPLGEGKTVTTIGLAQGLAKLNHSVMACIRQPSMGPIFGVKGGAAGGGYSQVAPMEELNLHLTGDIHAVTAAHNLAAAAIDARIYHEQRLGYADFERRTGMPALRIDPKQVIWKRVMDHNDRALRMVTVGRNEPGKNINGYEREDGFDISAASELMAILALASDLRDLRRRIGNVVLAYDLDGNPVTTEDLKVAGAMAVSMKEAIEPTLMQTLEGVPTLIHAGPFANIAHGNSSIIADEIATRLADYTVTEGGFGSDMGFEKACNIKAKASGKTPDCAVIVATLRGLKANSGLYDLRPGQAVPDALFAPDSAALQAGFANLKWHIDNVNQYGVPAVVAINRFPQDCAEELEQLVKLIEALPNRVSVAISEGFAKGGEGTKLLAEKVVEQCQHPTKFTPLYDSGIPLDEKLKAVAVKGYGAAEIALSDKAAQQLAKLQTQGFDHLAVCLAKTPLSISTDPAIKGAPRDFIVPIRELRLCAGAEFVYALCGSVMTMPGLPEKPSFMALDIDQHGNIVGLS | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 62074
Sequence Length: 582
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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A1JMA3 | MTPTLSSSADVLPSLSNMSSETNLLPIQQIAPQLGLSADDLIPYGHHMAKVDISALRPSGPQGKLILVSSITPTPLGEGKTVTTIGLSQGINRLGYRGVACIRQPSLGPVFGVKGGAAGGGAAQVLPMEKLNLHLTGDIHAISAAHNLAAAALDARLYHEQRLGAVFSQQTGMPLLNIDAQQILWPRVVDHNDRALRHIQVGVGGGTHGVERHDHVEITAASELMAILALSESLHDMRQRIGRIILAHSTSGQAITADDLGVAGAMTALMKETIHPTLMQTSEQTPVLIHAGPFANIAHGNSSVLADRLGLQLADYVVTEAGFGSDMGMEKFFNIKYRQSGITPSCVVLVATLRSLKANSGVFDIKPGQPLPAEILNTNIPLLSQGCANLKWHINNAKSYGLPVVVAVNCFPDDSPEELAFLADYALSAGAIACEISEAFAKGGAGTTALAQRVIDACAHASPPVLAYPDNASLEQKIEILAQRYGAREVTFTPQARQQLDSITAAGFGHLPLCIAKTPLSISADASLKNVPHDFVLPVTACAVSAGAGFVRIYAGDIMTMPGLGTQPAYYHIDIDDEGCIRGLS | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 61470
Sequence Length: 585
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q9FL59 | MAAKDGAKSQEDYKLKDMKPELGERWPHGGQRGGTGWIGSERAASTYDLVEQMFYLYVRVVKAKDLPPNPVTSNCDPYVEVKIGNYKGKTKHFEKRTNPEWNQVFAFSKDKVQSSTVEVFVRDKEMVTRDEYIGKVVFDMREVPTRVPPDSPLAPQWYRLEDRRGESKKRGEVMVAVWLGTQADEAFPDAWHSDASSVQGEGVQSVRSKVYVSPKLWYLRVNVIEAQDVEPSDRSQPPQAFVKVQVGNQILKTKLCPNKTTNPMWNEDLVFVAAEPFEEQFFLTVENKVTPAKDEVMGRLISPLSVFEKRLDHRAVHSKWYNLEKFGFGALEGDKRHELKFSSRIHLRVCLEGGYHVMDESTLYISDVKPTARQLWKSPIGILEVGILSAQGLSPMKTKDGKATTDPYCVAKYGQKWVRTRTIIDSSSPKWNEQYTWEVYDPCTVITLGVFDNCHLGGSEKSNSGAKVDSRIGKVRIRLSTLEADRIYTHSYPLLVLQTKGLKKMGEVQLAVRFTCLSLAHMIYLYGHPLLPKMHYLHPFTVNQLDSLRYQAMSIVAARLSRAEPPLRKENVEYMLDVDSHMWSMRRSKANFFRIVSVFAGLIAMSKWLGDVCYWKNPLTTILFHVLFFILICYPELILPTTFLYMFLIGLWNFRFRPRHPAHMDTKVSWAEAASPDELDEEFDTFPTSKGQDVVKMRYDRLRSVAGRIQMVVGDIATQGERFQALLSWRDPRATCLFVIFCLVAAMILYVTPFKIIALAGGMFWMRHPKFRSKMPSAPSNFFRKLPSKADCML | Function: Involved in the export of FT from the phloem companion cells to the sieve elements through the plasmodesmata . Regulates flowering time under long days . May function as a signaling molecule by regulating the trafficking of other regulators .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91003
Sequence Length: 794
Subcellular Location: Endoplasmic reticulum membrane
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Q69T22 | MTMTGGHHHDAHHEDFQLKDTNPLLGEQWPKGAAGPARPAVGGGIAGWLGLEKPSSTYDLVEQMFFLYVRVVKAKDLPPNPITGSPMDPYVEVKLGNYKGTTKHYDRRANPEWDQVFAFSKSRVQSNVLEVYLKDKEMLGRDDYVGRVVFDLAEVPTRVPPDSPLAPQWYRLEERRVGGGGDGGGLKVRGELMLAVWIGTQADEAFPEAWHSDAATVRGEGVASVRSKAYVSPKLWYLRVNVIEAQDVQPQARGRAPEVFVKAQVGNQILKTSVVAAPTLNPRWNEDLVFVVAEPFEEQLLLTVEDRVTPRKDDLLGRAALPLALFEKRLDHRPFVQSRWFDLEKFGIGGAIEGETRRELRFASRVHVRACLEGAYHVMDESTMYISDTRPTARQLWKPPVGVLEVGILGAAGLQPMKNRDGRGTTDAYCVAKYGQKWVRTRTMLGTFSPTWNEQYTWEVFDPCTVITIGVFDNNHLGNGNGNGNNAGGGGGGSPPARDARVGKIRIRLSTLETDRVYTHAYPLIVLQPSGVKKMGELRLAVRFTCLSLMNMVHLYTQPLLPRMHYLHPFTVTQLDALRYQAMGIVAARLGRAEPPLRREVVEYMLDVESHMWSMRRSKANFFRAVSLFSGAAAAARWFADVCHWKNVATTALVHVLLLILVWYPELILPTVFLYMFMIGLWNYRRRPRHPPHMDTKMSWAEAVHPDELDEEFDTFPTSRQQDVVYMRYDRLRSVAGRIQTVVGDMATQGERLQSLLGWRDPRATCLFVVFCLVAAVVLYVTPFRVVALVAGLYLLRHPRFRSRLPAVPSNFFRRLPSRADSML | Function: Involved in the export of the long day-specific flower-promoting signal (florigen) RFT1 from the phloem companion cells to sieve elements . Promotes flowering under long days through the transport of RFT1 from the leaves to the shoot apical meristem (SAM) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92948
Sequence Length: 824
Subcellular Location: Endoplasmic reticulum membrane
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Q9C8H3 | MQRPPPEDFSLKETKPHLGGGKVTGDKLTTTYDLVEQMQYLYVRVVKAKELPGKDLTGSCDPYVEVKLGNYRGTTRHFEKKSNPEWNQVFAFSKDRVQASYLEATVKDKDLVKDDLIGRVVFDLNEIPKRVPPDSPLAPQWYRLEDGKGQKVKGELMLAVWFGTQADEAFPEAWHSDAATVSGTDALANIRSKVYLSPKLWYLRVNVIEAQDLIPSDKGRYPEVFVKVIMGNQALRTRVSQSRSINPMWNEDLMFVVAEPFEEPLILSVEDRVAPNKDEVLGRCAVPLQYLDKRFDYRPVNSRWFNLEKHVIMEGGEKKEIKFASKIHMRICLEGGYHVLDESTHYSSDLRPTAKQLWKPNIGVLELGVLNATGLMPMKAKEGGRGTTDAYCVAKYGQKWIRTRTIIDSFTPRWNEQYTWEVFDPCTVVTVGVFDNCHLHGGDKNNGGGKDSRIGKVRIRLSTLEADRVYTHSYPLLVLHPSGVKKMGEIHLAVRFTCSSLLNMMYMYSMPLLPKMHYLHPLTVSQLDNLRHQATQIVSTRLTRAEPPLRKEVVEYMLDVGSHMWSMRRSKANFFRIMGVLSGIIAVGKWFEQICVWKNPITTVLIHILFIILVIYPELILPTIFLYLFLIGVWYYRWRPRHPPHMDTRLSHADSAHPDELDEEFDTFPTSRPSDIVRMRYDRLRSIAGRIQTVVGDLATQGERFQSLLSWRDPRATALFVLFCLIAAVILYITPFQVVAFAIGLYVLRHPRLRYKLPSVPLNFFRRLPARTDCML | Function: Required for proliferation and differentiation of shoot stem cells in the shoot apical meristem (SAM), thus determining the appropriate balance between the maintenance of shoot stem cells and their differentiation into other aboveground plant parts via the control of subcellular localization and intercellular trafficking of STM in the shoot apex . Prevents intracellular trafficking of STM to the plasma membrane in cells in the peripheral shoot meristem region thus facilitating STM recycling to the nucleus to maintain stem cells . May function as a signaling molecule by regulating the trafficking of other regulators .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89154
Sequence Length: 776
Subcellular Location: Endoplasmic reticulum membrane
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Q60EW9 | MMQRPFRPEEYSLKETSPHLGGGAAGDKLTTTYDLVEQMQYLYVRVVKAKDLPSKDITGSCDPYVEVKLGNYKGTTRHFEKKTNPEWNQVFAFSKERIQSSVVEIIVKDKDFVKDDFIGRVLFDLNEVPKRVPPDSPLAPQWYRLEERNGHKVKGELMLAVWMGTQADEAFPEAWHSDAASIPGDGLASIRSKVYLTPKLWYLRVNVIEAQDLIPNDRTRFPDVYVKAMLGNQALRTRVSPSRTLNPMWNEDLMFVAAEPFEEHLILSVEDRIAPGKDDVLGRTIISLQHVPRRLDHKLLNSQWYNLEKHVIVDGEQKKETKFSSRIHLRICLEGGYHVLDESTHYSSDLRPTAKQLWKHSIGILELGILTAQGLLPMKTKDGRGTTDAYCVAKYGQKWVRTRTIIDSFTPKWNEQYTWEVYDPCTVITIGVFDNCHLNGGEKANGARDTRIGKVRIRLSTLETDRVYTHAYPLIVLTPAGVKKMGEVQLAVRFTCSSLLNMMHLYSQPLLPKMHYVHPLSVMQVDNLRRQATNIVSTRLSRAEPPLRKEIVEYMLDVDSHMWSMRKSKANFFRIMGVLSPLIAVAKWFDQICHWRNPLTTILIHILFVILVLYPELILPTIFLYLFLIGVWYYRWRPRQPPHMDTRLSHAESAHPDELDEEFDTFPTSRPPDIVRMRYDRLRSVAGRIQTVVGDLATQGERLQSLLSWRDPRATALFVTFCFVAAIVLYVTPFRVVVFLAGLYTLRHPRFRHKMPSVPLNFFRRLPARTDSML | Function: Promotes nuclear translocation of the transcription factor OSH1, which directly suppresses the auxin biosynthetic gene YUCCA4 during the late development of anthers . Reduction of auxin levels at late stage of anther development, after meiosis of microspore mother cells, is necessary for normal anther dehiscence and seed setting . Required for jasmonate (JA) biosynthetic genes expression and JA production in anthers .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89345
Sequence Length: 774
Subcellular Location: Cell membrane
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Q4WAW7 | MPPAPPDQKPCHQLQPAPYRALSESILFGSVDEERWWHSTAPILSRLLISSNYDVDVQYKYLSLYRHLVLPALGPYPQRDPETGIIATQWRSGMVLTGLPIEFSNNVARALIRIGVDPVTADSGTAQDPFNTTRPKVYLETAARLLPGVDLTRFYEFETELVITKAEEAVLQANPDLFRSPWKSQILTAMDLQKSGTVLVKAYFYPQPKSAVTGRSTEDLLVNAIRKVDREGRFETQLANLQRYIERRRRGLHVPGVTADKPPATAADKAFDACSFFPHFLSTDLVEPGKSRVKFYASERHVNLQMVEDIWTFGGLRRDPDALRGLELLRHFWADIQMREGYYTMPRGFCELGKSSAGFEAPMMFHFHLDGSQSPFPDPQMYVCVFGMNSRKLVEGLTTFYRRVGWEEMASHYQGNFLANYPDEDFEKAAHLCAYVSFAYKNGGAYVTLYNHSFNPVGDVSFPN | Function: Brevianamide F prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities . The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA . Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B . FtmPT1/ftmB shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus . The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively . The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B . Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties . In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Catalytic Activity: brevianamide F + dimethylallyl diphosphate = diphosphate + tryprostatin B
Sequence Mass (Da): 52607
Sequence Length: 464
Pathway: Mycotoxin biosynthesis.
EC: 2.5.1.106
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Q4WAW5 | MKPSHSDTPLMMPSVMKCGYLATAGLIGICTHLSYFRYGEHHLYPWRYVRFHLCLTMGVAALLYAKKPPQYTLCSMDLVKDVSLLMATYLVGLFASLLLYRTLFHPLRQIRGPWAAKISSFWLSFRLRRGPSFRILHELHEEYGPVVRVGPSEVSIIHPEAVRMIYGPNSRCSKNTFYDNGHPMMSLHSYRDRIAHDQRRRVWSAGFGDRALRGYEQRMRVYRQKLFQRLEARAVAESAINISQWFNFYSYDTMGDLAFARSFDMLDASRNHWAVDMLMHGMIGYRYLFPSWFFRLLATMPSLSSDWHKFIGFATDTMLRRVGEQVDVPDIFASLLAPLNGREPTEDERNMLMGDAMLIITAGSDTTATSLTSIVYELARHLDEVDKLRAELDPIEADSDGEYQHDTLAKLPHLNGFINETLRLHPPIPGVIPRKTPPEGIHVKDVFIPGNMTVFSPQWSMGRSEAAYIDPEIFNPERWYKHMDLVKDPSAFAPFSIGPYSCIGKPLALMNIRTTVARLIMSFDVRFPEGEDGIRWMDAADEHFAMGIHQMPVVLTRRH | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities . The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA . Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B . The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively . The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B . Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties . In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + tryprostatin B = 6-hydroxytryprostatin B + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64183
Sequence Length: 559
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.14.14.118
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Q9FIM2 | MTSIELLSPLIHDKFRFSTCCSTSSLLYLHASSFFRDRSFGFRQNPNRFVSNSSIQLPQSVPGSINQERFNLWQGFSRKKSTSSSRTIVNCQEGDQKASSSEGEGKTNKDKGRKQGKNELWWSKGKKWQWKPIIQAQEIGVMLLQLGIVMFVVRLLRPGIPLPGSEPRTQTTFMSVPYSDFLSKVNNDEVQKVEVDGFHVLFKLKDDGNLQESETSSSSIKLSESSETMLRSVAPTKRVVYSTTRPRDIKTPYEKMLENNVEFGSPDKRSGGFFNSGLIVLFYIAVLAGLLHRFPVNFSQSTTGQLRTRKSGGPGGGKVSGDGETITFADVAGVDEAKEELEEIVEFLKNPDRYVRLGARPPRGVLLVGLPGTGKTLLAKAVAGESDVPFISCSASEFVELYVGMGASRVRDLFARAKKEAPSIIFIDEIDAVAKSRDGKFRMVSNDEREQTLNQLLTEMDGFDSSSAVIVLGATNRADVLDPALRRPGRFDRVVTVESPDKVGRESILKVHVSKKELPLGDDVNLASIASMTTGFTGADLANLVNEAALLAGRKSKMTVDKIDFIHAVERSIAGIEKKTARLKGSEKAVVARHEAGHAVVGTAVASLLSGQSRVEKLSILPRSGGALGFTYIPPTHEDRYLLFIDELHGRLVTLLGGRAAEEVVYSGRISTGALDDIRRATDMAYKAVAEYGLNEKIGPVSVATLSAGGIDDSGGSPWGRDQGHLVDLVQREVTNLLQSALDVALTVVRANPDVLEGLGAQLEDEEKVEGEELQKWLNRVVPSEELAVFIKGKQTALLPAQASSS | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87838
Sequence Length: 806
Subcellular Location: Plastid
EC: 3.4.24.-
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A2ZVG7 | MSALQASLLLRPLPSPLPPRRRLPLPSSSASFPRAGHHRRLPLPLRALASEGPQPAPSPAPDPPPPELPAAPEAEEVVGTAAAEGGGKVEEEELEDLVEKGRAWVLALAAAVVAAARRFFDWVVSGDWMSWWPFWRPDRRLQRLIDDADANPADPAKQSALLHELNKFSPEDVIKRFEQRSHAVDSRGVAEYLRALILTNGIADYLPDEQSGRSASLPALLQELKQRVSGNEDKPFMNPGISEKQPLHVVMVDPKATGRSTRFAQEIFSTVLFTIAVGLMWVMGAAALQKYIGSLGGIGASGVGSSSSYSPKELNKDIMPEKNVKTFKDVKGCDDAKKELEEVVEYLKNPSKFTRLGGKLPKGILLTGSPGTGKTLLAKAIAGEAGVPFFYRAGSEFEEMFVGVGARRVRSLFQAAKKKAPCIVFIDEIDAVGSTRKQWEGHTKKTLHQLLVEMDGFEQNEGIIVMAATNLPDILDPALTRPGRFDRHIVVPNPDVRGRQEILELYLQDKPVSSDVDVNAIARSTPGFNGADLANLVNIAAIKAAVEGADKLAAAQLEFAKDRIIMGTERKSMFISDESKKACLFKLLYFILRELILTAYHESGHAIVALNTQGAHPIHKATILPRGSALGMVTQLPSQDETSISKKQLLARLDVCMGGRVAEELIFGEDNVTTGARNDLHTATELAQYMVSNCGMSDAIGPVHVKERPSVEMQSRIDAEVVKLLREAYGRVKRLLKKHEKQLHALANALLERETLTADEINKVVHPYQEEPQLSFQEEDFALT | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85793
Sequence Length: 784
Subcellular Location: Mitochondrion membrane
EC: 3.4.24.-
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Q8VZI8 | MIFSKLGSSLARSSRSKGFVYGGGVRSAVFNQGRLRAPQNLEAAVNQVDGGLGFLRRHFASFAARKGLEAGDLSRAFANPRLRRFFSSQTPKKKNYENYYPKDSKKAPKNEQKSESRDGSKKNENENAGDAFSNEYQNMLIPLMAIALILSTFSLGSREQQQISFQEFKNKLLEAGLVDHIDVSNKEVAKVYVRSSPKSQTTEEVVQGPGNGVPAKGRGGQYKYYFNIGSVESFEEKLEEAQEAIGVNSHDFVPVTYVSETIWYQELLRFAPTLLLVATLIFGARRMQGGLGGLGGPGGKAGRGIFNIGKAQITRADKNSKNKIYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYYSQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVISKLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGTAALGFAQYVPNENLLMTKEQLFDMTCMTLGGRAAEQVLIGRISTGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQREDEFSKPYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVAQIAELLLEKEVLHQDDLTKVLGERPFKSGETTNYDRFKSGFEESEKESQKESVPVKPVEDDGIPPLEPQVVPT | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V of the mitochondrial oxidative phosphorylation system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 89555
Sequence Length: 813
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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Q9FGM0 | MSSSTLQASLFLRPPLHTSSFKLYPCLFSSSSLSFCPQSLSSFYRLSSVLHNSRFRPLPCSLRQDNVASDSDFIPKDSAFEVTDSAESNRLVSDTEVSELETNDRFVGGEETKSGGEEAEVSNGVTEGKEEDQKKSKFRIVVLMMALWAAIKRAIEKVMEWEWLSWWPFSRQEKRLEKLIAEADANPKDAALQGALLAELNKHIPEAVVQRFEQREHTVDSRGVAEYIRALVITNAISEYLPDEQTGKPSSLPALLQELKHRASGNMDESFVNPGISEKQPLHVTMVNPKVSNKSRFAQELVSTILFTVAVGLVWIMGAAALQKYIGSLGGIGTSGVGSSSSYSPKELNKEITPEKNVKTFKDVKGCDDAKQELEEVVEYLKNPSKFTRLGGKLPKGILLTGAPGTGKTLLAKAIAGEAGVPFFYRAGSEFEEMFVGVGARRVRSLFQAAKKKAPCIIFIDEIDAVGSTRKQWEGHTKKTLHQLLVEMDGFEQNEGIIVMAATNLPDILDPALTRPGRFDRHIVVPSPDVRGREEILELYLQGKPMSEDVDVKAIARGTPGFNGADLANLVNIAAIKAAVEGAEKLSSEQLEFAKDRIVMGTERKTMFVSEDSKKLTAYHESGHAIVALNTKGAHPIHKATIMPRGSALGMVTQLPSNDETSVSKRQLLARLDVCMGGRVAEELIFGLDHITTGASSDLSQATELAQYMVSSCGMSEAIGPVHIKERPSSDMQSRIDAEVVKLLREAYERVKSLLKRHEKQLHTLANALLEYETLTAEDIKRILLPKQEGEKFEEQQQEEGDLVLA | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V. Involved in thermotolerance but not in high light stress resistance or in the assembly/stability of the complexes I and V of the mitochondrial oxidative phosphorylation system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 88717
Sequence Length: 806
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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Q9SAJ3 | MEIAISYKPNPLISSSTQLLKRSKSFGLVRFPAKYGLGATRKKQLFRVYASESSSGSSSNSDGGFSWVRLAQSIRLGAERIGEKIGESVKTEIGFDSEEASGRVNEYVARVKDSVHKGHHELTRFKNETVPSFIDWNKWEHWKDIRNWDGKRVAALFIYAFALLLSCQRVYVAIQAPRVERERRELTESFMEALIPEPSPGNIEKFKRNMWRKATPKGLKLKRFIEAPDGTLVHDSSYVGENAWDDDLETTEGSLKKIIGRNARIQTEAKKKLSQDLGVSGEIGDSVGNWRERLATWKEMLEREKLSEQLNSSAAKYVVEFDMKEVEKSLREDVIGRTSETEGTRALWISKRWWRYRPKLPYTYFLQKLDSSEVAAVVFTEDLKRLYVTMKEGFPLEYIVDIPLDPYLFETICNAGVEVDLLQKRQIHYFMKVFIALLPGILILWFIRESAMLLLITSKRFLYKKYNQLFDMAYAENFILPVGDVSETKSMYKEVVLGGDVWDLLDELMIYMGNPMQYYEKDVAFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGAAKINEMFSIARRNAPAFVFVDEIDAIAGRHARKDPRRRATFEALIAQLDGEKEKTGIDRFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSYIYQQDIVDVLDKQLLEGMGVLLTEEEQQKCEQSVSYEKKRLLAVHEAGHIVLAHLFPRFDWHAFSQLLPGGKETAVSVFYPREDMVDQGYTTFGYMKMQMVVAHGGRCAERVVFGDNVTDGGKDDLEKITKIAREMVISPQSARLGLTQLVKKIGMVDLPDNPDGELIKYRWDHPHVMPAEMSVEVSELFTRELTRYIEETEELAMNALRANRHILDLITRELLEKSRITGLEVEEKMKDLSPLMFEDFVKPFQINPDDEELLPHKDRVSYQPVDLRAAPLHRS | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 115105
Sequence Length: 1008
Subcellular Location: Plastid
EC: 3.4.24.-
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A8ZNZ4 | MPIETEPNRTRKNFEPKRFGGSLFILFTLLLFLNLFVLRGPRFPITAYSDFITQVEAGQVERVEVRPDRIRYILKSDQYGFNEGTETAAVFDTVPVGIDLELPKFLREHDVQYFAPPPSSLSWLPTLLGWVVPPLIFFGIWSWLINRNQGAGPAALTVGQSKARIYSEGSTGVTFDDVAGVEEAKTELLEIVDFLAHADKYTRLGAKIPKGVLLVGPPGTGKTLLAKAIAGEAKVPFFSISGSEFIELFVGIGAARVRDLFEQAKQQAPCIVFIDELDALGKARGGPGGFTGGNDEREQTLNQLLSEMDGFDPNVGVILLAATNRPEVLDPALLRPGRFDRQIVVDRPDKMGREAILKVHVRGVKLAEDINLTKLAVRTPGFSGADLANLVNEAALLAARQSRDAVVMSDFNEAIERVVAGLEKKSRVLNDLEKKTVAYHEVGHAIVGSLMPGAGTVEKISVIPRGIGALGYTLQLPEEDRFLITASELRGRIATLLGGRSAEELIFGVVSTGASDDIQKATDLAERYVTLYGMSDELGPIAYEKAQQQFLEGVPNPRRTVGPQVVEAIDQAVKDVVDGAHHMALSILSINQDMLQLTASHLLEKEVLESQELHSLLSQPQFPPDMDEWLQTGKLPQGKELIQTTLNSHQLIGIN | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71566
Sequence Length: 655
Subcellular Location: Cellular thylakoid membrane
EC: 3.4.24.-
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A9NE17 | MNKQQKPKRSPLRPDYLVIVIIILLAIGMYFFFTEMMAPKVKQFDEFEFIAAIESGQIATVRSEYVGGDNFNLWEVTGTFTTGNAPEGVGSYVIILYGDRLNNIQDIIITYNELNPSTPITVSFVPHVSVDFWNIISTLLLIAAPIVLVVIMFRSMSSQSNKAQDFTKNRAKLSQGRKVKFSDIAGADEEKAEMAELIDFLKNPKKYADMGARVPKGVLLVGQPGTGKTLLAKAVAGEAQVPFFSISGSDFVELYVGVGASRVRDLFKVAKQSAPCIIFIDEIDAVGRQRGAGMGGGNDEREQTLNQLLVEMDGFSANLGIIIMAATNRPDVLDPALLRPGRFDRQITMQVPDQKSREEILKVHARSKKLDPTIKFSEVAMRIPGFTGADIENLLNEAALLAARESRTVISMQDIDEAADRVTMGPAKKSRKYSPNEKKMVAYHEAGHAVIGLKVNLASTVQKVTIVPRGRAGGYALYTPVEEKFNYAKSELLAMITSALGGRVAEEIMFDDVTTGAYDDFKRATKLARSMVTEYGMSDLGPIQYESDSGNVFLGRDYLKDKNFSDAVALEIDREVRAIITECYEHARKVINENKNLLDNIAKYLIAVETLTKTDIDEIAATGQLQWWDNREVEEDSKKSE | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70955
Sequence Length: 641
Subcellular Location: Cell membrane
EC: 3.4.24.-
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A0LR74 | MSREVTSGLPQDKPTGSAPPPPPPWRRWLLPIGLLVSLVLLFTFPMRPSSGKTLTYSEFLTALHHHDIKTITIHSDGEASGQFADGRPYSTTIPIGLAGSQLLNELENNGVQISARPPGPSLASQVLAGVLSFLPFLLLLGLFAYSGRRAGAGFLAGLPGIGRARAKIFTTERPQTRFSDVAGYDGVKAEIAEVVDFLRSPERYRRAGAAIPRGVLMVGPPGTGKTLMARAVAGEAGVPFLSVTGSSFVEMFVGVGASRVRDLFEEARKHAPCIVFVDEIDAIGQRRAGAGTIVANDEREQTLNQLLAEMDGFEPAQGVVVLAATNRPEVLDPALLRPGRFDRQVTVPLPSQADRAAILRVHCRNKRLAPDVDLDAVARATPGFSGAELANLVNEAAIAAARAGRRDLTAEDFRYARDRIILGRREDSNVLLPSERHAVAVHEAGHAVVAACSENADPVERVTILPAGRALGVTFQLPLAERHLYSESYLRDSLAVRLGGRAAELEILGEASTGAVNDLSSATELALRMVREYGLSPRLGPVSYPVGGSMYLPGGQELTPRPYAEATQQRIDQEVADLLRDAEERARDIIRRNRQAVDELASLLLEQESVDGAVVYQLVGRPVPTPEEHREAAARHVRRPGIAAATGASMAGGSEPRTAASSDDLL | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71287
Sequence Length: 666
Subcellular Location: Cell membrane
EC: 3.4.24.-
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C1F8X6 | MNSTVKTIVFWVFILACCILLWQVFQRSSNTGKEQEISFSQFLNDAQQGQIHDVTVVGGEVHGHFRSANAAFHVEVPTNYPQLYDILNKNHVAVTVKDNSGSPWWSILIQFSPVLVLVALWFFMIRQMQSGGNKALSFGKSRARLLSMQQKKVTFKDVAGVDEAKEELKEIIEFLREAQKFQKLGGRIPKGVLLVGPPGTGKTLLARAVAGEANVPFFSISGSDFVEMFVGVGASRVRDLFEQGKKNAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEANDGVILVAATNRPDVLDPALLRPGRFDRRVVVGRPDVRGREEVLRVHAKKVPLAEDVDLRVLARGTPGFSGADLANMVNEGALSAARANRKVVTMQDFESAKDKVLMGAERKSMLLTDEEKRVTAYHESGHAIVAAMRKHADPLHKVTIIPRGMALGVTMQLPEEDKHTVTKDYLETQLAILMGGRIAEEIFLHQMTTGAGNDIERATEMARKMVCEYGMSRLGPLTYGKKEEQIFLGREIAQHRDFSEETARQIDAEVRSLVDEAYRASYQLLNDNQPIMHKMAAALLERETIDANDIRMIIEGKDLPPLKPSGGSGTATTDDVQQVLKPSSDRGAGGLPEGSPSPA | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70328
Sequence Length: 639
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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C7M0M0 | MMPSSQRPSPRGSRQSPSPDQRGRIAFAILATLVVAVLLLTLFSHAPSGQPLGYSTFIHDVQAKQVRTAVLNNTTGQITGSLTNGTAYSVTGPLPYTSSELSTLSKAHVQVSYITPGPGIASTIIEYVIFFGIFIGIWVYLTRRTQGSVNGIMSVGRSRAKTYTTERPKTTFDDVAGYQGVKGEVKEVVDFLRDPSRFSQLGARIPKGILLVGPPGTGKTLLARAVAGEAGVPFMSVSGSDFMEMFVGVGAARVRDLFQTARRQSPSIIFIDEIDSIGRKRGTGLGGGHDEREQTLNQMLSEMDGFDPAEGIVVMAATNRPDILDPALLRPGRFDRQIVVPLPDLPERLAILQVHTRGKRLAPDVDLEVMAKGTPGMSGADLANLVNEAALNAVRRGATDIAMADFDSARDRIIMGQRREATILSDEEKERVAFHEGGHAVLAYVLDYSDPVHKVTILPTGMALGVTQQLPERDRHLYPREYIEDTLVVRMGGRVAELLVYGDLSTGAANDLQGNTELARRMVREWGMSERLGPMAWGSQNVVFLGEDLLHSAEYSDRTARLVDEEVERILREQEERATELLRQHLPGLIAVAHALLERETISGEEVGRLVDEAAGHPIHPDGKRVLPIAKLPEYAELEQFTVTNGNNHAASHDDTDPVS | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71888
Sequence Length: 660
Subcellular Location: Cell membrane
EC: 3.4.24.-
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B2UMY1 | MPPSPPRPPKFPGSGRPESPNWGVWVMVLLIVGVLAFGFFTPESFGLGPRKENLESFEAQYKAGRVVLNDPKAPVEVVLSENGSEGVIHALVYRKEIQPKVEMTPFALTYSMSLPDRDKPLLNELSGYRVVESPYRTEEGKNVSLIPEGAQKLSVPEFNRLALEGRIAGGKDGIILAEDGNQNVLVGQIVTRIWPAATGDASVDKQRFERVEVPFTLEFQGDRVKQLLGPDTKFKRESGSWGGILLNLLPIVLILVILFFMFRAQSGGARGAMSFGKSRARLISPDKNKVTFKDVAGISEAKEEVWELVEFLRNPEKFRDLGATIPRGVLMVGAPGTGKTLLARAIAGESNASFYSISGSDFVEMFVGVGASRVRDMFEQAKRTAPSLIFIDEIDAVGRQRGYGMGGGNDEREQTLNALLVEMDGFENNSNVIVIAATNRADILDPALLRPGRFDRQVVVNLPDVRGREQILQVHARKVKMAPGVSFERIARGTSGFSGAQLANLVNEAALLAARKGLKEITEAELEEARDKVSWGRERRSLAINERGRRITAVHEAGHAICLLKTPHSEPLHRVTIVPRGGALGMTMWLPSDDKMHQLRSEMLDQLVVAMGGRCAEQIVFGDVTSGATGDIKSATNLARRMVCEFGMSEKLGLIEYGEHQGEVYIARDLGTRSRNYSESTAELIDSEVRFLVDSAYERAMAILTENRDKLDILTEALMEFETLEGSQVMDILEYGEMKNPPARVTPPPMPSEVEEQPGKDDSGHNEKKEAEETRADGAEERKMEEELEQAERAPFSYNPVDEFGKDGGEKK | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89455
Sequence Length: 812
Subcellular Location: Cell membrane
EC: 3.4.24.-
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P94304 | MNRIFRNTIFYLLIFLVIVGIVSVFNSDQTETENVSFNEFAERLENGQVQELSVKPERQVYLVRGQFNDQAEDEFFQTYALRSEQTAELLFNAEDPTGTPFNLEIEPADETSGWVQFFTGIIPFIIIFILFFFLLSQAQGGGSRVMNFGKSKAKMVNEDKKKAKFKDVAGADEEKQELVEVVEFLKDPRKFSAIGARIPKGVLLVGPPGTGKTLLARAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQIQVNRPDVNGREEVLKVHARNKPLNDDVNLKTIATRTPGFSGADLENLLNEAALVAARHDHTKISMIHIEEAIDRVIAGPAKKSRVISPKEKKIVAWHEAGHTVVGVKLENADMVHKVTIVPRGMAGGYAVMLPKEDRYFMTQPELLDKIIGLLGGRVAEEVTFGEVSTGAHNDFQRATGIARKMVTEYGMSEKLGPMQFISGSGGQVFLGRDIQNEQNYSDAIAHEIDLEVQRIIKECYARCKQILLENKDSLDLVAKTLLDMETLDAEQIKSLVHEGKLPDDHHLNAHLEKEKASESDVKVNINSKKEETPQVEAEQPQEPNTDEPIEKDPSVEDNRSFEDDTNKKE | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75446
Sequence Length: 679
Subcellular Location: Cell membrane
EC: 3.4.24.-
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B8J992 | MSADEKKGHGQRSERGRGPGGPGTQPRIPLASPAAWLVLIALAIFLFRAFQDVGVRRIPYSQFKEMVRQSAFERVVIGPDWVRGVPKPVEAGAAQGGGAQPQQQAQGEGERNGQALPYVATRIPGGGDDLVQAVEKAGVPYDAVAGGGMGDLFWVWIAPIAIGLLFWAWVMRRMSGQLGQGPPGVMAFGKSRARIHMEPDTGVTFQDAAGIDEAVEELQEIVEFLKTPEKYRRLGGRIPKGVLLVGPPGTGKTLLARATAGEAGVPFFSLSGSEFVEMFVGVGAARVRDLFAQATQKAPCIVFIDELDALGKSRNAGIMGGHDEREQTLNQLLAEMDGFDARAGLIIMGATNRPEILDPALLRPGRFDRQVLVDRPDKRGREQILRIHARNVKLGPDVDLRSVAARTPGFAGADLANVVNEAALLAARRNKNHVTRAEFEEAIERVVAGLEKKSRRINEREKEIVAFHEAGHALVSWMLPFADRVSKVSIIPRGLGALGYTLQLPLEDRYLLTRSELRDRMAGLMGGRVAEEEVFGEPSTGASNDLQHATAVARMMVRDYGMSPALGPVSLGDQNGPSFLGVKGFETRSYSDHTALAVDREVQALVEEAQDRARTVVREHRERLEALAARLLTIEVVEEDEITRLWGPKVVRPGTIEGRGHEESPPETPNRPVAASADASAGFGRSGPQPPQALARHAGGDPDPES | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76249
Sequence Length: 706
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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O67077 | MNALKNFFIWAIIIGAAIVAFNLFEGKREFTTKVSLNEVVKLVEEGKVSYAEVRGNTAIIQTKDGQKLEVTLPPNTNLVDKMVEKGVRVEVANPEPPGGWLVNVFLSWLPILFFIGIWIFLLRQMSGGGNVNRAFNFGKSRAKVYIEEKPKVTFKDVAGIEEVKEEVKEIIEYLKDPVKFQKLGGRPPKGVLLYGEPGVGKTLLAKAIAGEAHVPFISVSGSDFVEMFVGVGAARVRDLFETAKKHAPCIIFIDEIDAVGRARGAIPVGGGHDEREQTLNQLLVEMDGFDTSDGIIVIAATNRPDILDPALLRPGRFDRQIFIPKPDVRGRYEILKVHARNKKLAKDVDLEFVARATPGFTGADLENLLNEAALLAARKGKEEITMEEIEEALDRITMGLERKGMTISPKEKEKIAIHEAGHALMGLVSDDDDKVHKISIIPRGMALGVTQQLPIEDKHIYDKKDLYNKILVLLGGRAAEEVFFGKDGITTGAENDLQRATDLAYRMVSMWGMSDKVGPIAIRRVANPFLGGMTTAVDTSPDLLREIDEEVKRIITEQYEKAKAIVEEYKEPLKAVVKKLLEKETITCEEFVEVFKLYGIELKDKCKKEELFDKDRKSEENKELKSEEVKEEVV | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70686
Sequence Length: 634
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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Q2NIN5 | MSFFDKIFKKFHMGVLYFAVILIGATFIYCYFTKHEKKDNNTFDALAQKNEIEKIQYNPIFANSAFCDIVVTTTDGRVIDFFNIPYDKVFEKKPNGKYKYNTYSVDPRPWNGYEHVFWVFRQCLTMLFFYCFFLFFADTIKQMGQEILASTSGKKGAKSRKVIINHKRFTFSDVAGADEEKEEMSELIDFLKNPRKYAAMGARIPKGVLLYGPPGTGKTLLAKAVAGEAGVPFFAASGSDFDEVYVGVGASRVRDLFKEAQLAAPCIVFIDEIEAVARKRGSNIGGSNGSEQTLNQLLVEMDGFNQKMGVIVIAATNQPEVLDSAILRPGRFDRHFNITLPNVKDREAILKLHASNKKLSEEISLEELAKQTPGFSGAQLEGTLNEAALLAARRNATFINKKDISEALDRILIGPTKKSKKYNDKEKRMVAYHEAGHAVIGIKIPFAQIVQKITIIPRGNAGGYNLMLPQEETFFSSKKALLAQITSFLGGRVAEELMFDDVSNGAYNDFKHATQIAKLMVTKYGMSDLGPVQYSGNTFQNDFSDPKGLEIDQQIQKIIANCYQQAKQIIQENQDLLDTIAKYLLEIETLNKRDIDEIVATGKIAWWEKEKEETNAPTQTTSQMSSNNETTNTDKTPLNDELEITTNLDNQESNESNPNNNEKASPEVLSTDSEQT | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75765
Sequence Length: 676
Subcellular Location: Cell membrane
EC: 3.4.24.-
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P37476 | MNRVFRNTIFYLLILLVVIGVVSYFQTSNPKTENMSYSTFIKNLDDGKVDSVSVQPVRGVYEVKGQLKNYDKDQYFLTHVPEGKGADQIFNALKKTDVKVEPAQETSGWVTFLTTIIPFVIIFILFFFLLNQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEATDRVIAGPAKKSRVISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIFGEVSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQGGQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQILTENRDKLELIAQTLLKVETLDAEQIKHLIDHGTLPERNFSDDEKNDDVKVNILTKTEEKKDDTKE | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70937
Sequence Length: 637
Subcellular Location: Cell membrane
EC: 3.4.24.-
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O83964 | MERSPLPRIIALTFGTLLFVSAVLLTLSTFLPLFTLHRASHWFFVPGTLLYETYAFSSLLVPLLLLHTALLLFVGGRSLRAESALVAFPLLFITAVCGEHGLYALRRALAARSISPSTRGGIDIVCVLCLLALLGAELYAALIYGERCYVWFHARIPRDFIADGFQDPSFPPSTADHPDTVSPPPAPSCATADVQTPEASAPPEGQFSTEVPLQGGEFLISEAEVQPATQVAACGGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDEQGPPRPIPASAAPLRHPCRGYQVPYDLLDQYSEDTYEGIDELTKNLALLLEETFSEFNIRVEITGIKKGPVVTMFELLPPPGIKLSKITNLQDNVALKLAASSVRIVAPIPGKHAIGVEVPNKKRSLVTFKELLHTRTAGSNRMAIPVILGKDVTGEPQVIDLAQTPHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHLLTPVITEPKRALQALQYILCEMERRYALLEQLECRDIKTYNKKIQEKSIATQPLPFIVIIIDEFADLMVASGKELETSVARLCAMSRAVGIHLVLATQRPSIDVITGLIKANIPSRIAFMVSSKMDSRIILDEMGAEKLLGRGDMLYMNPSQSFPTRIQGAYVSERELARVIAHVRAWGTPEYLDEEIFFDDDDASISGNFVDESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAARLIEEMEARGVVGPPNGSKPRDVLRS | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Required for activation of the Xer recombinase, allowing activation of chromosome unlinking by recombination (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86606
Sequence Length: 799
Domain: Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains form the DNA pump, and the gamma subdomain is a regulatory subdomain (By similarity).
Subcellular Location: Cell inner membrane
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Q83MS8 | MSAKKSYLKVWRGLAGAAGSCARVFSKKSLARRDRRDQLPFALFLFGLVGAVFQWFLYGNWLSGIVSEYTVAAFFGGFSIVLPILLIGFSIWLFRNPQKTHDNIRVSIGLFMFSSFSAAFLHFSAGFPYPSSGIRILSTAGGIIGWLVGLPLTTLPSYLAKTVCIIFIVLSVSVISKTPISKIVRVIFRYAKWLFNSDSVKTSPNSSVSSSSEHQELTGRDMPDTAGDNRHDETVTVLSGTSLTGSPVSEYHGESSDYALPSLDILNSYPPAKHDDAENEKVITALSGVLRQFSVNARFSGFSRGPTVTQYELELGEGVKVERIIALTKNISYAVASDKVSILSPIPGKSAIGIEIPNKKRELVALGSVLQSIHPDAHPMTVGLGKDSSGGFVLTNLTTMPHLLVAGATGSGKSSFVNSMITSILLRAHPSQVRLVLIDPKRVELAIYSGVPHLITPIVTDPKKASEVLQWVVKEMERRYDDLASFGFRHIDDFNLAVRAKKIASDSRELTPYPYLLVIVDELADLMLVAAKDVEESIVRITQLARASGIHIVLATQRPSVNVVTGLIKANVPSRLAFAVSSLVDSRVILDRPGAEKLVGQGDGLFLPISAGKPIRIQSSWVTENEILRVVEYVKSQAHPDYYVLEVQNQGNIDSHIGDDMPLLLKATELVINSQLGSTSMLQRKLRVGFAKAGRLMDLMESMGIVGPGQGSKAREVLVTPQDLDSTLARISASVSDSKLD | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Required for activation of the Xer recombinase, allowing activation of chromosome unlinking by recombination (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80484
Sequence Length: 741
Domain: Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains form the DNA pump, and the gamma subdomain is a regulatory subdomain (By similarity).
Subcellular Location: Cell membrane
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Q84I33 | MFKENKNKVETIIKTSEEAPSSRLNGSQRLKESGLILAFLFSIFLAVALFSFNPADPSWSQTAWGTDIHNAGGLVGAWLADTLFFVFGSLAYPLPFITAFAAWVLLRKRDEGDEIDFTLWGTRLLGLTIVLLTSCGLADINFDDIWYFSSGGVIGDVLTSLALPTLNILGTTLVLLFLWGAGITLLTGISWLRIVEWIGERSIAAFVGLFNRLRGEKAERVKPALVKPELPVEELEPTFSASMDTEIDEPAPSLRRFNIHMPEERDVPDIHFEPQVEPKVELKPEPPRQREPAPHFSRVAAQNTQVEPVSSARTQQWDATIEELEQQARLVDDYAVEDDAVPSVLTSSTLSDVEDSILTTAISVDEEEESLSENFNHSFNIEVEDEEVEPSIANLHWSDDEDELEETPSVMVSPAIESDWEDEDEPDDRDVAAFQNIVSQAQANAAAQQNPFLVQKAVNLPKPTEPMPTLELLYHPEKRENFIDREALEEIARLVESKLADYKIQAQVVDIFPGPVITRFELDLAPGVKVSRISSLSMDLARSLSAMAVRVVEVIPGKPYVGLELPNMSRQTVYLSDVIASPQFKESKSPTTVVLGQDIAGDAVVADLSKMPHVLVAGTTGSGKSVGVNVMILSMLYKASPEDVRFIMIDPKMLELSVYEGIPHLLAEVVTDMKDASNALRWCVGEMERRYKLMSVLGVRNIKGFNDKLRMAAEAGHPIYDPLWKDGDSMESEPPLLEKLPYIVVVVDEFADLMMVVGKKVEELIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPTRVAFTVSTKTDSRTILDQSGAESLLGMGDMLYLPAGSSHTIRVHGAFASDDDVHAVVNNWKARGKPNYISEIIQGDHGPEALLPGEQSESDEELDPLFDQVVEHVVETRRGSVSGVQRRFKIGYNRAARIVEQLEAQGIVSAPGHNGNRDVLAPAPIRD | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105888
Sequence Length: 960
Domain: Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains multimerise to produce a hexameric ring, contain the nucleotide binding motif and form the DNA pump. The gamma subdomain is a regulatory subdomain that controls translocation of DNA by recognition of KOPS motifs and interacts with XerD recombinase (By similarity).
Subcellular Location: Cell inner membrane
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Q8D8M2 | MFKENAKKVQTIIKTSEEAQSSRLNGFQRLKECCLILGVLTSAFLSIALLTFSPADPSWSQTSWGGDISNAGGQFGAWVADTLFFTFGLLAYLLPVLLVIVTWVFFRTRDEDEHIDLMLWGTRLLGLAILILTSCGLADINFDDIWYFSSGGVLGDVLNSLALPTLNLLGTTLVLLFAWGAGFTLLTGISWLSIVEWIGSLFLDVCQWALNRLRGEKTEVIAPELQPIALSDDEPKAQPQIEAQQDEIVEEERIPDPLPVEPVVQMRREYPIHMPQTVSYQTVSDELDELEDNSFERAKKLNATIEELEQEALSVNDLPDDTMSTERARYNVADIAQVSAEHSQTTQVEHAQDFSVDVEEFDHVISLSELDKISEEIDEPVMVGFAEEAPLHHNEAQRSAMASSAEPMFSHLGVEQTTQHTTQEEIVDLPVADSVGDVNPEMEDYVEEDEDQDQDVVAFQNMVSKAQQNMAATQNPFLMKQDTSLPVPKEPLPTLELLYHPEKRENFIDKEALEQVARLVESKLADYKITAEVVGIFPGPVITRFELDLAPGVKVSRISSLSMDLARSLSAMAVRVVEVIPGKPYVGLELPNMSRQTVYLSDVIDSPQFQNATSPTTVVLGQDIAGEALVADLAKMPHVLVAGTTGSGKSVGVNVMILSMLYKASPEDVRFIMIDPKMLELSVYEGIPHLLAEVVTDMKDASNALRWCVGEMERRYKLMSVMGVRNIKGFNEKLKMAADAGHPIHDPFWQEGDSMDTEPPLLEKLPYIVVVVDEFADLMMVVGKKVEELIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPTRVAFTVSTKTDSRTILDQGGAESLLGMGDMLYLPPGSSHTIRVHGAFASDDDVHAVVNNWKARGKPNYIDEIISGEQGPESLLPGEQMESDEDLDPLFDQVVEHVVQSRRGSVSGVQRRFKIGYNRAARIVEQLEAQGIVSAPGHNGNREVLAPAPPRE | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108746
Sequence Length: 985
Domain: Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains multimerise to produce a hexameric ring, contain the nucleotide binding motif and form the DNA pump. The gamma subdomain is a regulatory subdomain that controls translocation of DNA by recognition of KOPS motifs and interacts with XerD recombinase (By similarity).
Subcellular Location: Cell inner membrane
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Q8P993 | MAKQVPERSKPAEGKSSSRKPAAADTPRRQKLWRDLALIAVAPLLLYLLASLFTYSAADPGWSQTGSVVAPVHNMGGRVGAWIADVLLQLFGYVAFLLPVVLGAVAWIALFGMDKEGQAEADLGPALRLVGMVGFLIASTGFLHLRLFNGDVAGAGGILGRLVSNSLSAGFGALGANLFVVVLLLVSITLATGLSWFVVMERIGKWVLALGPLLQRKSHQATEWQQTRVMREEREEVRKVDAVKQAKREPVKIEPPPAPVVEKSERAKRDTQIPMFQGVSTDGSDLPPLALLDDPKPQAKGYSEETLETLSRQIEFKLKDFRIEAQVVGAYPGPVITRFEIEPAPGVKVSQISSLDKDIARGLSVKSVRVVDVIPGKSVVGLEIPNVTREMIFLSELLRSKEYDKSASPLTLALGKDIAGRPTVADLARMPHLLVAGTTGSGKSVAVNAMVLSLLFKASHKELRMLMIDPKMLELSVYQGIPHLLAPVVTDMKEAANGLRWCVAEMERRYKLMSAVGVRNLAGFNKKVKDAEDAGQPMMDPLFKPNPELGEAPRPLETLPFIVIFIDEFADMMMIVGKKVEELIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPTRVAFQVSSKIDSRTILDQSGAEALLGNGDMLYLPPGTALPDRVHGAFVSDEEVHRVVEHLKASGPVAYVDGVLDEVQTMGDGTVVGATGLPESSGGGGDESDPLYDEALRIVTETRRASISGVQRRLKIGYNRAARLIEAMEAAGVVSPPEHNGDRTVLAPPPPK | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84638
Sequence Length: 785
Domain: Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains multimerise to produce a hexameric ring, contain the nucleotide binding motif and form the DNA pump. The gamma subdomain is a regulatory subdomain that controls translocation of DNA by recognition of KOPS motifs and interacts with XerD recombinase (By similarity).
Subcellular Location: Cell inner membrane
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Q81WC4 | MSNLAVKYKQQAQEEVQIQTPPQQMVQPKAKAKITRIEKLLYVAFIGFLLYACVAFIGNKAGLYQVNVEAATIEQKIVQQQKENQELQAEVEKLSRYERIAEVAKKHGLEINANNVKGLK | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 13601
Sequence Length: 120
Subcellular Location: Cell membrane
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Q07867 | MSNLAYQPEKQQRHAISPEKKVIVKKRASITLGEKVLLVLFAAAVLSVSLLIVSKAYAAYQTNIEVQKLEEQISSENKQIGDLEKSVADLSKPQRIMDIAKKNGLNLKDKKVKNIQE | Function: Essential cell division protein that may play a structural role. Probably involved in the regulation of the timing of cell division. Also required for sporulation.
PTM: Cleaved by RasP. Cleavage is important for turnover and function of FtsL.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 13073
Sequence Length: 117
Domain: The cytoplasmic region is involved in protein stability.
Subcellular Location: Cell membrane
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Q7VUP7 | MGRISLIVAALLMLSAISLVTSRYQSRQLFIELGRSQAEARDLDTNWRRLQLERAELARNARIDRAARDDLKMIPIVPDRTLYMNQPAGGAQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 10438
Sequence Length: 92
Subcellular Location: Cell inner membrane
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