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S7ZC62
OPDI_PENO1
opdI (Oxopyrrolidines biosynthesis cluster protein I)
MRGYRSSQRTFFRGFDPRHAYRFRGDGRHGGMGGALKIVFLGMMTYFIAKKAFRSSQHPPTDFNAPVQSVPQRAQRPSDTRLQGPVLLASNHPSGDSASPE
Part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. Does not seem to play a role in oxopyrrolidines A and B biosynthesis.
S7ZEI0
POXG_PENO1
Thioesterase poxG (EC 2.3.1.-) (Oxaleimides biosynthesis cluster protein G)
MVSLSCLISYGECLLETVQTHPWSTIGVVVFLSSVKNAPLMWHARLIIAVFYHSVTRKNDVVTIERYGRQGLFGYIVTSSRSPLYECDINGHKSDSTYFSDLDINRIHLITRLFKGAGDLSLRPDRPNVAPEDRPKKMRVLLGGTCCSFRREIKPYAAYEIHSRVLAWDEKWLYVVSYFVKPGSARKMASLQTEVGDKCEMTDLARSMVFTSAITKFVFKDGRKTVRPADALEEMGLLSASEEVVETSEAGEDLWTRSRVEERRKTGIKIAQHFIALDELHDQFEHVSEHPFLGKFGVLGTMF
Thioesterase part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety. The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate. The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl. 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4-enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid. The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2-aminodec-4-enoic acid which is activated and incorporated by the adenylation domain. The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (Probable). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring. The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur. This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate. Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A. Subsequent oxidation yields the maleimide scaffold oxaleimide I. Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H.
S7ZFL4
POXK_PENO1
Hydroxylase/desaturase poxK (EC 1.-.-.-) (Oxaleimides biosynthesis cluster protein K)
MTATATPVPTVASHAQDITLPPPPKGDITTPILFAQDFQKPSTGYMFIKNPPPAGVPYTNIRGEPAMVTVEDLRGKENSVNLDRDSLQVLQGLTDVPRSPEVNWNSVESVEKTFYPAVEAAIKSAIPGAHTVHIFRHGIRHTQNWPVPYNPPAMIAHLDQTGPAAINRVLRHMGPVEGPRLLQGRYRIVHFWTPLNGPVYTCPVAVASSATVKDNDIQIFVSHLGGIGGLDMPLGRPVAKPDASEQYREDFGAPRYADGQRWFYLSGITQDEALLIQIFDSNALQKDSTVQGGRAVHSAFRDPRTPQGAPDRWSIEVSCLVFSDE
Hydroxylase/desaturase part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety. The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate. The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl. 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4-enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid. The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2-aminodec-4-enoic acid which is activated and incorporated by the adenylation domain. The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (Probable). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring. The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur. This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate. Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A. Subsequent oxidation yields the maleimide scaffold oxaleimide I. Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H.
S7ZK48
POXA_PENO1
MFS-type transporter poxA (Oxaleimides biosynthesis cluster protein A)
MPASDRTSETGDVEKVTAAETPKEVPASNAAESTALTGLPLYTVLVGLGLALFLGAMDMAMLGTAVPSITSTFHTTADIGWYGAAYPLTMSSIQLLAGKIYAQFPQKLVFLVFFGLFMLGSLLCGVAVNSPMFIVGRATAGAGAAGVLSGTLAIVSAVVPLDKQSLILGLMMSLVGTAVVLGPVISGLLTDHSTWRWCFYLNLPCGGVTLLALILFFRPPKRPTRTTPLSIPELIKKLDLAGCLGFIPAVVMLLLALQWGGDGSKEHAWNSATIIGLFCGAGVSLILFLIWEHYQGDDAMLPLKFFRDLTIIASCLYGFALLGGYVVVGYFLPEWFQIIKGANPQSSAVMLLPNVITNFISKAVIGVIVNKTGYFNPWLFFGAAVLAIGSGLETNFHPSTPRPNWIGYQILQGAALGIIQAPTLGVQVALAKQKHLIPVALSLVIFFQYFGSSIMLSISLTIFQNLLRPGLVSKAGMTEAQVQQYVAAGNSEVRELTAQIDPSRLGVVLEVYNDAIAGVMWLSTAAALFGFLVSFGFPWKSLKAQTEENKKEAAEEEEEVKVAAVEA
MFS-type transporter part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety.
S8ASK6
POXJ_PENO1
WD40 repeat protein poxJ (Oxaleimides biosynthesis cluster protein J)
MVDNQGPLAKDVSLANPPSDSISELSWSPVANHLAMSSWDQTVRIYDVSQSGNGEGQALFNFPAPVLSCTFSPDGAKVLGGATDGSARLMDLVAGKEAQQVAAHDAPVRCVRFFGNPGVRDPIAVTGSWDQTVKYWDLRQDRPLATLQCQERVYAMDLCQNLLVVATAGRLVHVVQLSNADQIYKTVTSPLKHQTRTVTCIPDASGFAIGSTEGRTGFHYVDESKSSLNFTFRCHREMAASKNTQNVYAVNDVSFHPKYYTFSTAGADGTFAFWDKDAHHRLKSFPSVGAPITSTGFNHDGTIFAYAVSYDWSKGFRYNTPEHPTRVVCHPVDDVDCRPKNPVKR
WD40 repeat protein part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety. The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate. The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl. 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4-enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid. The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2-aminodec-4-enoic acid which is activated and incorporated by the adenylation domain. The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (Probable). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring. The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur. This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate. Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A. Subsequent oxidation yields the maleimide scaffold oxaleimide I. Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H.
S8AWN1
OPDG_PENO1
Oxopyrrolidines biosynthesis cluster protein G
MDHLRDSLLSSLPRDSPSIGAMDYARRDRESTRQSVARGDFEELRQAAFYNRTWVVTSRFCDIGAGVDSVEVHVHSLWYIYYELSRHISSQSPEHEGLVLDILRIQGMGPLNRPARGNSGVDIARTVDGTLWTDLPFLVGDMTSFWIEHGATMSGTHRLNLATFLAKLASARVAKDRMCQIALLLFRNVFETSLELRTGDESDGEDLNRGMRQLEVFHLLPAAVAWLKIAAHNLALLSEVCWSDCPSHISQGGEDFLESELGRRSPAGFSPWRYMFWMKRLHEIQGQAKEAGEKTLEELAADGIEYMSNTIQSRNSEIIRAFKSADSALHQDPHLSCLRNLAGFDDDEPEESQEIARES
Part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. Does not seem to play a role in oxopyrrolidines A and B biosynthesis.
S8AWQ1
OPDO_PENO1
Oxopyrrolidines biosynthesis cluster protein O
MSRRLDLDALDLSTKTIPAQAAIGTYMSSTIIKAPASSVWQAVNDTDSWPIWNTFCPGATIREQPDTTKSRSGRLQLGTKMTLHLNWNPRGTKPKQMDVGLVVTEFDPPIKGRETPGRIAWATDSSAKGFPSWLLYAERVTELHESEEWDGEECQSVTQVLSWESQRGPLAYVVRWFMGKNFKMCLRVQADDMTSFVEGQKL
Part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. Does not seem to play a role in oxopyrrolidines A and B biosynthesis.
S8B3H6
POXB_PENO1
C6 finger transcription factor poxB (Oxaleimides biosynthesis cluster protein B)
MSEAEPSVVVAEQCRRSACDRCRGQKLRCERPVSNSSTTPCRRCLKAHVRCVTTAQPHRTKPLSSLQYLHHTESNYDPHSATVAGQLPVAAVAGLGDLDPSLLHMTGVQNPRRLSHSSSMANPVDSRPPGRTRRLSNPDHFLPHPPLHPNGVLDTDGTPLLDSIDHLPDMTASRGFGFSAALTPHSPSGSSDFFDYFRPMAEDNNRSPWMDAFTNLPPDHREGTPAGSNYRGSLTGENQFRSSLQSSRGLNGFETPQRESRHREMDIVSIKNECIARMGKLNRGLLQDVGLVNSGKVAGTLLFSQASRSTYLEVEKGRKGGQNYVIGKMLHSSKELLDILKQLERCKSTLFPPGHTERTTSTADEVTTAMTETTTLNQTGSHAPSSPLGGNPLPPLSGPLSASASHSSSCASSSSASASTSGASLLSSSTSAPSTSPAISLQLDTTLTLLFLTGYTSVIQLYEGVFSFIRDSVAANPSGSNFLPTLPKLQVDGFEVGSSTRDLQICILLQVSTHILNQIEERLHAIRDRAEGHVPAALLDTILDRSDPSQRGAKGRELCRIVRDIKEHLKHYAE
Transcription factor that positively regulates the expression of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety.
S8B3I4
POXI_PENO1
Oxidoreductase poxI (EC 1.3.1.-) (Oxaleimides biosynthesis cluster protein I)
MSTVYYPSVILKKSPLPLKLTPARASGNFGTPITAALQRASFNITIITRTESSSTFPAGLPIIRTSYTLENLTTALAGQDAAICVVGPGGIGAQVLMIEAAEAAGVKRFIVDDFGWGPGFRNLPEFRAIHAHRRAGWELAKAKAQANPNFTFTGITSGNPIDWAMKRFPLMGFDIARCSAIIYDSGTEKFTATTLAGIGQSVVGVLQHPDETANRFVKVLSIITNQNELLEAFQRVTGRQWPVQRASAQTLIESGQQKFQAGMGGWVLELVVAQMYDEGEARCVMAPSWEASDSPLLGVKKESADEVVAKVLQL
Oxidoreductase part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety. The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate. The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl. 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4-enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid. The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2-aminodec-4-enoic acid which is activated and incorporated by the adenylation domain. The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (Probable). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring. The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur. This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate. Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A. Subsequent oxidation yields the maleimide scaffold oxaleimide I. Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H.
S8B3I8
POXN_PENO1
Oxaleimides biosynthesis cluster protein N
MALDLLVVSAGSLALKVLRVTPLITTTILLVNRLAQYFALSTFLPPHTSPKKIDHVGAAFQHWLQTVVPRVWTGVISIVLFTRVALILNLFVRPDDLAGSNARFLYGVGLFLSFAHLSVAPKMLKFEKRMMSPETVPHVAMELLAGWMKVNNIRFWIVDVPFWVVGVWATLEGLKA
Part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety. The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate. The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl. 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4-enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid. The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2-aminodec-4-enoic acid which is activated and incorporated by the adenylation domain. The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (Probable). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring. The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur. This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate. Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A. Subsequent oxidation yields the maleimide scaffold oxaleimide I. Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H.
T1DKS4
TCTP_CROHD
Translationally-controlled tumor protein homolog (TCTP)
MIIYRDCISQDEMFSDIYKITEVANGLCLEVEGKMVSRKEGEIDDALIGGNASAEGPEGDGTEATVITGVDIVMNHHLQETSFTKESYKKYIKDYMKSIKARLEETKPERVKPFMTGAAEQVKHILGNFKNYQFFVGENMNPDGMVGLLDFREDGVTPYMIFFKDGLEMEKC
Venom protein that causes edema, enhances vascular permeability and is likely related to the inflammatory activity of the venom.
T1SFR8
PPR3C_CLABA
Protein phosphatase 1 regulatory subunit 3C
MPVDMAVQLYITSSPPLHHRFLSSYKDYRVRNLISVNCKPLRPCINTKNTHNTSLNPPCSVWKAPEPKAKKKVVFADSKGMSLTAVRVFSPCENKKSDSQVQFQLPKLEVALKPVQSRILAFRQPATEYMEFRKRLMKNSVCLESCTLQGHTLTGTIKVRNVSFEKSVQVRITFDSWENHRDIECTFLNDVCGCRDTDTFSFIIEIPACVLPQDSVEFCVSYTCGGKTHWDNNNGKNYALVTTHDEKKDKTKETDLLDPFRNQQKRNRFTADWNSLMIGIRGPTW
Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown.
T2KLZ3
PLH1_FORAG
Unsaturated glucuronyl hydrolase (UGL) (EC 3.2.1.-) (Glycosyl hydrolase 88 family protein P1) (P1_GH88) (Polysaccharide utilization locus H protein P1) (PUL H protein P1)
MRKLVYLVLVLGLTFLNVRCKSETKQNKKEEQNIGKQYSSLENRFQKLVNYPVGANNFPRSMSLAPEVVHKVPSKDWTSGFFPGNLWLIHELTGDSIYKVKAQEWTVLMEDQKENDRTHDMGFKVYCSFGEGLKQDPDNQYYKDVIIESAKTLITRYNDTVKSIRSWDFNKDVWDFPVIIDNMMNLELLFEATKISGDNIYHNIAVQHANTTLKHQFRPDYSVFHVINYDTISGVVKTKDTHQGFDRNSTWARGQAWAIYGYTMSYRYTNNPKYLAQAEATTQFYMEHENLPKDGVPYWDFNDPEISDAPRDASAAAIVTSALFELYTYTNNKTYLDFATQVLNTLNSEAYLLKDTVNGPFILNHSTGNWPKNDEIDEPIVYGDYYFLEALKRKQNLILK
Unsaturated glucuronyl hydrolase involved in ulvan degradation. Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). Unsaturated glucuronyl hydrolase catalyzes the cleavage of the unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) at the non-reducing end of ulvan oligomers, thus forming 5-dehydro-4-deoxy-D-glucuronate.
T2KM18
PLH26_FORAG
TonB-dependent receptor P26 (P26_TBDR) (Polysaccharide utilization locus H protein P26) (PUL H protein P26)
MFCYSSLHAQIISGTVSAEGQVLPGAAVIIKGSTKGTSTDFDGYYTIEAQASDVLVFSYVGYANKEVTVGTNTQIDVALEADNTLDEVVVIGYGTQRKSDLTGSVSSVSAEDVNVNPVSRVDQALQGRAAGVQVTQTSGAPGAASVIRVRGGNSITGSNEPLWVIDGIVVGTNFNLNNINSNDIKSIEILKDASSIAIYGSRGANGVVLVTTKTGTGAGSSKPEVSANIYTSMQMVPELPKMLSQAEQIAYTNESAAFRGAAIPFPNDPSTYPNNDWFDLLLGPAPIYNADVSITGASENVSYYTSLNYFNQEGIVKTSGIEKYIFRSNLDIRLSDKLKTGFRVNYSYIDQQNGLVGYGNAIATLPTQPIYNEDGSYNGFDEVVGSPWSNPIANMALNTNETFRNNFLGSFYIDYSPSEKWIIRSTFSPDFDNSKQNRFTSSQSPNLLYLGEGGNASVRTVNTKGWNNENTIQYQSEIGENHRITALGGASFQKVSTEIVESEAFGITNDATGFNNLSNSDPTRNILTSDYSGFQIASFFGRLNYAYKDKYLLTLVGRTDGSSVFSDDNKYEFYPSIAAAWKISEEGFMQNQETFGELKLRASYGKSGNQAIDPYRTKGLLVEANTTLNGIQQTGLTLGRPSNPNLTWETTNSLDIALEASMFNGRVFAELNYYYKKTNDLLLDVTIPKQTGFNSQLQNVGSLENKGWEFSLNTTNVRTDNFNWKSTLMLSSNKNKILDLGGVDFIDLVVDELLGSGNTRLIVGESVPVFTGVKFLGTWKSQEEIDASGLRDPQVVGGAKYHDENGDGIISTDDAVVLGSPLPDLIFGFENTLSYKNLDFSFYFQGTQGNEVYNLRMRNHYFNRGEFTKFAEVADRWTPENPTSDIPRAGGDSVTGTPPNSAYVEDGSHIRLKTVRLAYNMPVDKMGMDGVKNATVYLTGTNLLLWSDFRLIDPEGSNFGRNGIGNIAQGYNDGSYPNPRTITLGLNVTF
TonB-dependent receptor probably involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). The TonB-dependent receptor may mediate transport of ulvan oligosaccharides from the surface of the outer membrane to the periplasm for subsequent degradation (By similarity).
T2KMH0
PLH24_FORAG
Beta-xylosidase (EC 3.2.1.-) (Glycosyl hydrolase 3 family protein P24) (P24_GH3) (Polysaccharide utilization locus H protein P24) (PUL H protein P24)
MKKLWLMGLLLASFFTTVAQNNAQTKSNSDEEIDKKVATLISQMTLDEKIAEMTQDAPANERLGIPSMKYGEALHGLWLVLDYYGNTTVYPQAVAAASTWEPELIKKMASQTAREARALGVTHCYSPNLDVYAGDARYGRVEESYGEDPYLVSRMGVAFIEGLQGTGEEQFDENHVIATAKHFVGYPENRRGINGGFSDMSERRLREVYLPPFEAAVKEAGVGSVMPGHQDFNGVPCHMNTWLLKDILRDELGFDGFIVSDNNDVGRLETMHFIAENRTEAAILGLKAGVDMDLVIGKNVELATYHTNILKDTILKNPALMKYIDQATSRILTAKYKLGLFDAKPKKIDTETVETGTDEHREFALELAEKSIIMLKNDNNLLPLDVSKIKSLAVIGPNAHEERPKKGTYKLLGGYSGLPPYYVSVLDGLKKKVGEHVKINYAKGCDIDSFSKEGFPEAISAAKNSDAVVLVVGSSHKTCGEGGDRADLDLYGVQKELVEAIHKTGKPVIVVLINGRPLSINYIAENIPSILETWYGGMRAGDAVANVIFGDVNPGGKLTMSFPRDVGQVPVTYLERPDFIGSGKGQYRFSDKTPLFPFGFGLSYTTFKYGTPKLDNTSIAANGTTTVSVEVTNTGKVTGDEVVQMYVRDDYASVGRYLKMLKGFKRITLKPGETKTVSFKLGFDELNILNQDLKKVVEPGTFTISVGASSKADDLKTVSLTVK
Xylosidase involved in ulvan degradation (Ref.2, PubMed:31285597). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). Beta-xylosidase converts Xyl-Rha3S, a product of alpha-L-rhamnosidase acting on Rha-Xyl-Rha3S oligosaccharides, further to Xyl and Rha3S. The enzyme is able to degrade 4-methylumbelliferyl-beta-D-xylopyranoside (MUX) in vitro (Ref.2).
T2KMH9
PLH34_FORAG
Putative beta-xylosidase (EC 3.2.1.-) (Glycosyl hydrolase 3 family protein P34) (P34_GH3) (Polysaccharide utilization locus H protein P34) (PUL H protein P34)
MKKLLFTFLVSTGTIFFSCQRTYTQSKDYKNASLTIEERVDALLPKMSLEEKVAQMRIFHANIGVEAEGNGNLKLSDKVIEKLKLGIAGIKNPGEHMDPVAAAKFNNDLQKYIIENNRWGIPALFVTESYNGVDAAGSTRFGRPLTSAASFNPQLVNRIWDVVGREARLRGMHMCHSPEADLVRDPRFGRMSEAFGEDTYLTTQMVVNAINGVQGNYDGLGNGTHIGAVAKHFAGYGQVLGGSNFAAIEISPRTLIDEIYPPFEAAVKEAKTLGIMASHGDINGVASHGNPELLTGVLRDQWGFKGYVVSDSNDIARLFYFMNVAESPEEAAQMGLEAGIDIDLYAEDSYAYLPEMVKKNPNLEKLIDRSVRRVLRTKFILGLFDNPYIDIEEVKKGVRANSSLTLAKESDLESIILLKNENKILPLNKNKTTKIALLGPLVKDDTKSMFETVASKHISFVAEKGFHLTDEKGGAPKLLERDENAISKMVNMAKNSDLSILFLGGDEFTSKEAFFNNALGDRATIEPVGAQDELIEKIKALGKPVIVVLKHRRTLAINTISEQADAILDTWDLSEFGDESTARIIFGEVSPSGKLPVTVPRSIGQIPFHYSMKEINYKKGYLFMEDGPLYPFGYGLSYSNFEYSDIKKSNSEMTKDSEIEVSVTIKNTGNVKAKEVVQMYIKDVKGSVIRPDKELKGFEKISLNPGESKKVSFKITPEMLKFTGLKMEKVLESGEYTVMIGTSSVDYKKTSFQLKK
Glycoside hydrolase probably involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
T2KMI3
PLH39_FORAG
TonB-dependent receptor P39 (P39_TBDR) (Polysaccharide utilization locus H protein P39) (PUL H protein P39)
MFKQKLKMKPKIKRNCTFSGLAFILMLLFSSFTVNNLNAQSEVTGTIMGEDGIPIPGVNVIQKGTKNGTVTDFDGRYSVTLVPGQLVLVYSYIGYETQEVPIKSRKVIDLTLKAELQSLDEVVVIGYGEQKRADVIGAVGSVDSEELSSVSPVDALQGIQGRVAGVQVTTNGGPGGDSEIIIRGISTFGAGSSPLYVVDGQQVNDITNINPADIESMDILKDGASAAIYGSKSANGVVLITTKQGKPGFPKMTVDYISSVSFLNNLVPVSNTRQWNKFESLRTGSTDASGQVEDSLGIRSQLVVDVQDAIKQLGVKNQVNLAFSGGGEKSKFYWNTGYLDETGIVKGSGYNRITSNLKIDFDLNKFITAGTRMTGTYQMQDGINEGSVFRNLSYRQPNVLLVDFDGSYIRERYARNNPLARAELQVNDNRQFSSTIFNYISVKLAPGLTFKTTLGFNYRNQKLNQFNPQETVNIDNGKINGRERVNTFYDFQNENFFNYNKTFNDKHTVTGLAGFSIQRWWYEYSDLNAIEFNNDYIQTFNNVKEYNLNTTGTDATTHALSSLYARIGYDYKSKYLITASIRRDGSSRFGENRIWGNFPAIQLGWKISEENFMKSLGFINLLKLRASYAITGNERIGDFESIALYNPGFFYNSVNGFAPVQLGNGDLGWEETAQQNYGIDLSLFKRRLNVSVDRYVKTTDDLLYNVPIPQETGFSNIRANIGSVENRGWEVSIAAKPIRNERFTWTTSFNFSYNENEVLELADEDGFETGGYLIEEGESLGNMYGYKNLGVFQYDESNAFTPDGIRLTPNFDANQNFVNYTLNGQAYNGDIERLKFANKVLRGGDIIFQDQNGDFNIDAANDRTIIGNGLSDFAGGFSNRFDYNGFFFSFLFNYNFGNDIYRDYDHIRDKASNAVYAPSPDRIDGAWVNPGDITKYPSLEVSRANNRSGYESNYVSSADFISLRNIQLGYSFNPDTLNKLGFINRLSLNASINNVFMFTNYEGYNPELGNRGNALEPGWDSLRYPNQTEIVIGLNVEF
TonB-dependent receptor probably involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). The TonB-dependent receptor may mediate transport of ulvan oligosaccharides from the surface of the outer membrane to the periplasm for subsequent degradation (By similarity).
T2KN63
PLH2_FORAG
SusD-like protein P2 (P2_SusD) (Polysaccharide utilization locus H protein P2) (PUL H protein P2)
MKKYKITFIVLLLTLVGCSDLEENPVGILAPESFFKTTADLQAAINGSYASMSTESFWGRKLTLTLLLRGDLADIGDQGTSGRRKEVNNFTMGDDNGMVSAFWPQAYAIIGTANQAISNAGLINDDENKVNAVAAQAYFCRAFTYYHLVRLFGDIPYIDFAVSDASEIDAISKTPENEVYEGIIADLQYAKEWLPDTQFSRALPSKATAAAYLASVYLTRGDFQKAAEEAQFVINNEARFDLRLEPDFQNLFDANQTAGLKEPLFTIDYMGQISSSGYGQDYVASVTGIRGDATHEYGEGWSVAVPSLKVYQDWDAKDYRRAVSLDTTATSKSGEVYPYTQFEEYSDLAVNRPHIAKYYRYAGLAGNNGRESSTNYIPMRYAEVLLIAAEALNEISAGSSEAVSYVNRLRERARLGSGSMHPLNISEGLLQDELRNIIIEERKIELAFEFKRWYDIKRLKLGNEVFGPNGLEPQPNFDANRDYLLPLPGPELVRNSNLMPNNPGY
Polysaccharide-binding protein probably involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). The SusD-like protein may mediate ulvan oligomer-binding before transport in the periplasm for further degradation (By similarity).
T2KN67
PLH7_FORAG
Uncharacterized protein P7 (Polysaccharide utilization locus H protein P7) (PUL H protein P7)
MKHVIMLYFIAAATLFSSCAKQDSEHRLITVKNSLDLPRAFETIEISKSDIQLHTGERFEDFSIQDVATKAILTSQFVDEDQDGTADVLLFQPELNPNSEKQFELVKVDGGVEVDSTVYCYSRFVPERTDDYTWENNKVAFRTYGPVAQKMVEDSLPGGTLSSGIDAWLKKVEYSIIDNWYAKNDKDPGYYHIDHGEGLDNFHVGSSRGVGGSAVKVDTSYYISKNFTDYKTITTGPIRTSFILKYADWDANEKTISEEKHISLDYGNNFSRFEIHVDGTDELSVGLTLHDNKGEITQNVDQGWIAYWESEYFDSELGTAIVAPKGVMTASEYYVTSMKDRSNLYAQLNVDNNKVVYYAGFAWKESKQYPTKASWEKYIQEFSEKLNTPLEVSIQ
May be involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
T2KN95
PLH37_FORAG
Uncharacterized protein P37 (Polysaccharide utilization locus H protein P37) (PUL H protein P37)
MKTYNINKRINTLLLLVITMLSFSGCDLEPQEKFRFDPEVDPQFTFGSMTTWEWLQTNPNDEFGFMIEAIKQTGLQDMYNSKTETYTFFLMKDPNWTNNGPGFFSREFNLKNTADRDPKEVFEDPAVDLDIVRNYLLYLTLPIYVDQGPDHLKTLDLPYTFETLSEDVNNQIMTIARDWNYVMQINDSPDLPTGNLGKINVPVGYHNYIFSNGNSVAHIFGLNNNGKMARRYKFGEPKMDF
May be involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
T2KNB8
PLH25_FORAG
SusD-like protein P25 (P25_SusD) (Polysaccharide utilization locus H protein P25) (PUL H protein P25)
MKIQNIIVYVFLIFSCFSCEEFLEEDPRALIAPETFYQSESDVRQAVVGLYSILKNNSIYGQLGLDLFYDNGADIIEPNRSTNVVEPLGNYSLNEAIADVSVQKMSVSDTWKDLYRVIYNANIILDNVDGNDAISEEAQIDIMAEVKFIRALCYWHIVNLWGDAPFYTEPLVLEEIRVLGRTDEDTILSTVVSDLQYAQVHLASVYPEEDRGRASKWAAAIVEAKIHMQEQNWQAGLNKCMEIISQSPHSLLGNYADVFNPNNEYNSEIIWSLDFAKDIRGQFEEGTLGADGSFPSVFGNGNWRPSMFAPRLRDEPKNSSERNALAAALQANGEAFNGTGLQVASKDFAGKFPRNDYRRALNIVDNYLGFDLNFPYMAKIWNLDVDNSPRFNHSDNRIVFRLADVYLMAAECENELNGPANAFQYINKVRERAFATQTEWELKGLDQQGFREAIYDERKWELAGECHRRYDLIRWGILLDVVQDLEYRFWTPNTNIRPYHVKLPIPLQELQVNPVLLESDATNNGYR
Polysaccharide-binding protein probably involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). The SusD-like protein may mediate ulvan oligomer-binding before transport in the periplasm for further degradation (By similarity).
T2KNC8
PLH35_FORAG
Oxidoreductase P35 (EC 1.-.-.-) (P35_oxidoreductase) (Polysaccharide utilization locus H protein P35) (PUL H protein P35)
MESRINWGIIGCGNVAEVKSGPAFYKTENSTLVAVMRRNEDKVIDFANRHGVANWTTNAEALIQNDLINAVYIATPPSSHLQYALRAINVGKNVYLEKPMVLNNHEANILVEAVKRSNVKVTVAHYRRELPVYLKIKELLDSNVIGNVISAEIQIKQTRNTNLIAKTEVNWRTIPEISGGGYFHDIAPHQIDLMCHYFGEVENIKKGSCKENQVSHQDVSGEVLFKNGVQFSGTWNFNALEDKDECTIKGERGSISFSFYTSTITVSKNGLIESYHYENPEHVQQPMIEKTVGYFLAHNSNPCSVEEAAMVTHIMDVFCGT
Oxidoreductase that may be involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
T2KPJ3
PLH3_FORAG
TonB-dependent receptor P3 (P3_TBDR) (Polysaccharide utilization locus H protein P3) (PUL H protein P3)
MTTKNNKQLKSVLFMFLLLIGAYVKAQEKNVSGTVTSSEDGMMLPGVNIIVKGTASGTTSDFDGNYNIEVPDSNAILQFNYLGFVTQEIKVGAQTNISVVLQVDQNELEEIVVIGYGTVKKSDVSGSVSSVKSAELTAYPTVSAEQALQGRAAGVQVQSNNGGEPGAPIKVRIRGGTSINASSDALIVVDGFVGASMPAPQDIASMEVLKDASATAIYGSRGANGVIMVTTKKGTSSKPTLELNTSYSLQHVNNTIDLLDADEFATYRQAYSENYVQGPANTDWQDEIYTTGSISNTQLAFSGGSDNSKYYISGNYFAQDGVVINSNLERFTILSNVDVDITKRFKVGLNVFGGRSTKDGVSTQAQTGGTGGGDVISSAYRFAPDLGIYNADGTYTINSLGDDIDNPYALATESVDERKADTYRANFYAAYEFIDGLEFKTTFGFSSENTQIGKFKPTTILAGAGVGGEATFEYRNTTNTLSENYLTYNKSFGAHNLSLLGGYSYQKVQNEGAFAGARSFVTNEVSYRNLEGGAVTMQPSSYLNETELVSVFGRVNYEYASKYIFTFTARRDGSSNFSKNNKYAFFPSGAIAWNMAKENFLKDSNTITTWKWRASYGATGNPSISPYETLAKFSSVYAVVGDQQVNGVVLTDFANDNLKWETSKQLDLGLDVALFDNRLELSFDYYTIKTEDLLFPRPLPEYSGVSSQIQNIGELENKGYEFSINSRNITNQDFTWSTAFNFSRNKNKMVKLPDGDDLFIDSAPGHFLQRQTQILREGEAIGSFYGYEYKGVYQGGNFPEGTATLSGDSDPGGELFADLDGNGEISTADRKIIGDPTPDFTMGFNNDLRYKNFDMNLFFQASVGGEILNYTLLELGSGAANSTADMVNAWSPTNTNTDVPRPAVREKRITSRYVYDGSYVRLKNLSFGYNLPESFLGKTGLQTVRLYVSGQNLLTFTDYPGADPEANYRNDNNQRSNTNIGLDYGSYPNVRTFTMGLNMKF
TonB-dependent receptor probably involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). The TonB-dependent receptor may mediate transport of ulvan oligosaccharides from the surface of the outer membrane to the periplasm for subsequent degradation (By similarity).
T2KPJ7
PLH8_FORAG
Putative beta-glucuronidase (EC 3.2.1.31) (Glycosyl hydrolase 2 family protein P8) (P8_GH2) (Polysaccharide utilization locus H protein P8) (PUL H protein P8)
MGFCMKDSKQYYKSSIGKSLKRSNGYLKLVLVLYLIMVSWSGYSKEVFNSRTKENINANWLYLEKNIKDINLALNDANWESINLPHTWNALDATDLNPGYRRSGSWYKKELAISNIENNKLYQLYFEGVNINSEVYVNGQKAGGHIGGYIGFTIDITEFIKSGKNDIVIRVDNSYDPEVIPSQKSDFFIFGGITRDVWLETIPKQHLSELKITTPKVSENEAELLATVAINNLNNSNLKVQANLLDAQGVTVVSSVFKIKNNTAKIHFRNIKNPKLWDTEHPNLYTLKVALLEKGDVIDSVQNRVGFRWFEFKDHGAFYLNGKRVLLRGTHRHEEHAGVGAAMSNMQHRKDMELIKDMGANFVRLAHYPQDPEVYKACDELGLLIWDELPWCRGGLGNETWKTNTKNMLTEIINQNYNHPSIIIWSLGNEMYWLPDFENGDDTDKMNSFLTELNDLAHQLDPSRKTAIRKYYEGSHIVDVFSPSIWSGWYSGSYKSYQKAIDTYKKEYPHFLHAEYGGSSHVGRHTENPVTGEGKIQSDGWEEEIVQTDVANIAQIGDWSENYIVDLFDWHLRISENDENFVGNVQWAFKDFGTPLRPENAIPYMNQKGLVDRAGNPKDAFYVFKSYWSKEPFTYIESHTWTERQGPKDLARDISVYSNCPEVELFLNGKSLGVKKRDLKVFPAAGLNWNLNFKEGKNTLVAVGKTKENKTVKDELAINYRFTKNGKAVGLKLESELLENGNYLVTAIAYDKNGLRCLDYEDQVYFQCLSGGETLKSQGTPTGSESIAMANGKAAIEVKRDGKNIPVVMMVLNQNFKGTYLTIE
Glycoside hydrolase that may be involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
T2KPK8
PLH23_FORAG
Uncharacterized protein P23 (Polysaccharide utilization locus H protein P23) (PUL H protein P23)
MKKSKASALLWLFSLVGFMLHAQTFNLNQPMVAQNVIFEEKDGLVAVEAEYFYKQTHTDLREWYRTTKDSVAVVGRDEDANHYLNASNSSYIEVLPDTRVTHSDQLVRGVNFSNKPGQLAVVSYKIKFNSPGRYYVWVRALSTGSEDNGLHVGLNGTWPEHGQRMQWCDGKKYWMWESKQRTKDEHCGVPHAIYLDVPKAGIHEVQFSMREDGFEFDKFVLTTNSNYVPIDKGPNMTLADGNLPSSYKSKSEPSYFNTIARKLPENKFIASQEFPIDGTNFYKNGKNWLAINPEQYKQAKISTLFDFESGTYDVIYVGVGENDGRSTFRIVINNKELGTYQPPLTQMLWEEGKAFNGFWKNVKLNKGDTITVEVQVASDGNEWTRGRWAGIVFAPVGQGYVVQESPSTYIFEK
May be involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
T2KPM5
PLH38_FORAG
SusD-like protein P38 (P38_SusD) (Polysaccharide utilization locus H protein P38) (PUL H protein P38)
MKKFKNISITFLILISLGVLNSCESVLEVEPESSISDEQFWKTNEDAKLGLAAAYDALQKAYRTKRFYWGEFRADNYVNSEKPQPDTQDLINNNLTPESSTEYLQWDEFYSLIFRANLAIEKIPEIPYYDTQYLGEAYALRAFAYFDAYRVWGGVPLFTKAELTFSDDAIKPRSSAQEVLDLVLSDIEEAEKNLTVVSSDYTFSKLSLLAFKAQVHMYLNEYEAANTALTSLIASNQFSLTTNRKQWRDLFLNDEINYPGEGQEGPELIMSIRYDFEEDGNRASGIYQVFFPGVPSYYVAPNLVEEWETKFPTDSTAWATKYPNVPPHVFEENEDTGELNAKYGDYRYYESIAAPGTQEEDLRISKYHKVNISPSIDDTNIILFRYADMLLLKAEALNQLGQPTEAIELVNQIREARELPLVNSGTIPDVVNINDKDELEDFILSERRLELLAEGYRWWDLVRTNKAVEVMGPINGLTQDRIIWPLWFRHLIDNPKLEQNVPY
Polysaccharide-binding protein probably involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). The SusD-like protein may mediate ulvan oligomer-binding before transport in the periplasm for further degradation (By similarity).
U3EQ60
TCTP_MICFL
Translationally-controlled tumor protein homolog (TCTP)
MIIYRDCISQDEMFSDIYKITEVANGLCLEVEGKMVSRKEGEIDEALIGGNASADGPEDCTEATVITGVDIVMNHHLQETSFTKESYKKYIKDYMKSIKARLEESKPERVKPFMTGAAEQVKHILGNFKNYQFFVGENMNPDGMVGLLDFREDGVTPYMIFFKDGLEMEKC
Venom protein that causes edema, enhances vascular permeability and is likely related to the inflammatory activity of the venom.
U3H0P2
WTF25_SCHPO
Meiotic drive suppressor wtf25
MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPLNTHRENHSYGTTDNSSPLLIILLISFTSIILFNAPAFCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWSKACGKGIKHFLKNWRNMIFAFCKSSLFCLVLLKAENKLSSHLGDQRWGWKCSASAFTFMAVSSILIFIAETVEPGSCSTDLVKRTLAFYGYEIRQHVNEDATILLREMNPESEA
Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons (By similarity). Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity).
U3PVA8
IROK_ECOLI
Protein IroK (3-hydroxypropionic acid resistance peptide)
MKPALRDFIAIVQERLASVTA
Possible increased expression of this protein (due to mutations upstream of the start codon) is proposed to be responsible for resistance to 3-hydroxypropionic acid (3-HP).
U3THC0
FG2KI_SOYBN
Inactive UDP-glycosyltransferase 79A6 (Inactive flavonol 3-O-glucoside (1->6) rhamnosyltransferase) (GmF3G6''Rt-b)
MPSELAMNNDELHVVMFPFLAFGHISPFVQLSNKLFSHGVHVTFLSAASNIPRIRSTLNLNPAINVISLKFPNGITNTAELPPHLAGNLIHALDLTQDQVKSLLLELKPHYVFFDFAQHWLPKLASEVGIKSVHFSVYSAISDAYITVPSRFADVEGRNITFEDLKKPPPGYPQNSNISLKAFEAMDFMFLFTRFGEKNLTGYERVLQSLGECSFIVFKTCKEIEGPYLDYIETQFRKPVLLSGPLVPEPSTDVLEEKWSKWLDGFPAKSVILCSFGSETFLSDYQIKELASGLELTGLPFILVLNFPSNLCQS
Has no flavonol 3-O-glucoside (1->6) rhamnosyltransferase activity in vitro.
U3U715
HISAT_SCOAU
Histidine N-acetyltransferase (EC 2.3.1.33)
MKIDTSLTMPQLPEALSQAGLQFAVATEEDFDEIMAMSQDIYGGLDYLPTRYTSWLQETNRTVILARKQGKVIALESVCVIDNGETMLVEGLRVAPQERGKGVAGVLLRFCCELVKSKYPEVKVTRLTRDDQLGPKDFQKYRLITKQGILLVRFRAEDLKLRLSELNLGGDIQSSLSTSSSNTPPVRLDHTAIHRLYLTTDLMQGVLPNATIIQDWQPFKPLPSNMAILLKKDIDWMVDDVANPTMASLCTFPYRVPVGDDWYYLNIDMFGKDLDLAQQQFLCHLQRHTTTLKGHVMCQMFLDPPLWKPMAEFCNKTLSVELVKEYTEQCVVESDVV
Enzyme responsible for the N-acetyl-histidine (NAH) synthesis, which is a major constituent of brain and lens of ectothermic vertebrates.
U3UBT3
PLS6_PHYSA
Phylloseptin-S6 (PLS-S6)
MAFLKKSLFLVLFLGLVSLSICEEEKRETEEEEHDQEEDDKSEEKRFLSLIPHIVSGVASIAKHLG
Antimicrobial peptide with high activity against Gram-positive bacteria, low activity against Gram-negative bacteria, and moderate activity against fungi (By similarity). Acts by causing bacterial membrane disruption inducing leakage of the intracellular content followed by cell death (By similarity). It adopts an alpha-helical amphipathic structure in membrane environments (By similarity). Also shows highly potent antiparasitic activity against Leishmania species (By similarity). Shows moderate hemolytic activity on human erythrocytes (By similarity). Is also active on human monocytes (By similarity).
U5GKY6
NRP62_POPTR
Metal transporter Nramp6.2 (PotriNRAMP6.2) (PtNRAMP6.2) (Natural resistance-associated macrophage protein 6.2)
MASSQQEQQACEIAPASRGNSNRIAALNLDGQSPPCIDDYDQQKPGWRKFLPYVGPGFLVSLAYLDPGNLETDLQAGANHGYELLWVILIGLIFALIIQSLAANLGVSTGRHLAELCKAEYPKYVRWSLWLLAEVAVIAADIPEVIGTAFALNILFHIPVWAGVLMTGLSTLLLLGLQKYGIRKLELLISALVFTMAACFFGELSYVKPPASGVLKGLFIPKLSGQGATGDAIALLGALVMPHNLFLHSALVLSRKVPNSVRGINDACRYFLIESGFALFVAFLINVSIISVSGTVCLAKNLSPENADQCGDLTLKGASFLLKNVLGKSSSTIYAIALLASGQSSTITGTYAGQYIMQGFLDLKMRKWLRNLTTRCIAILPSLFVSIIGGSSGASRLIIIASMILSFELPFALIPLLKFSSSNPKMGPHKNSIYIIVISWTLGFMIIGINVYYLSTGFVGWLTHNNLPKVGNVIIGIIVFPLMAIYILAIIYLTFRKDTAVTYIDPVKNDPNLEANMENGQGKSNQEMAFGRVPYREDLADVPLPE
Probable divalent metal transporter.
U5L396
MSD6_AMAEX
MSDIN-like toxin proprotein 6 [Cleaved into: Toxin MSD6]
MSDINTTRLPFVFVASPPCVGDDIAMVLTRGENLC
Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L397
PHAT2_AMAEX
Phallacidin proprotein 2 [Cleaved into: Phallacidin]
MSDINATRLPAWLVDCPCVGDDVNRLLTRGESLC
Toxin that belongs to the bicyclic heptapeptides called phallotoxins. Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin. Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption.
U5L3J5
AMAN1_AMAEX
Amanexitide proprotein 1 [Cleaved into: Amanexitide 1]
MSDINTARLPVFSLPVFFPFVSDDIQAVLTRGESLC
Cyclic nonapeptide that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L3J7
MSD7_AMAEX
MSDIN-like toxin proprotein 7 [Cleaved into: Toxin MSD7]
MSDINATRLPAWLTDCPCVGDDVNRLLTRGESLC
Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L3J9
MSD8_AMAEX
MSDIN-like toxin proprotein 8 [Cleaved into: Toxin MSD8]
MSDINATRLPFVFVASPPCVGDDIAMVLTRGENLC
Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L3K1
AMAN2_AMAEX
Amanexitide proprotein 2 [Cleaved into: Amanexitide 2]
MSDINATRLPVFSLPVFFPFVSDDIQAVLTRGESLC
Cyclic nonapeptide that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L3M6
MSD5_AMAEX
MSDIN-like toxin proprotein 5 [Cleaved into: Toxin MSD5]
MSDINATRLPLFFPPDFRPPCVGDADNFTLTRGENLC
Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L3M7
BAMAT_AMAEX
Beta-amanitin proprotein [Cleaved into: Beta-amanitin]
MSDINATRLPIWGIGCDPCVGDDVTALLTRGEALC
Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
U5L3M8
MSD3_AMAEX
MSDIN-like toxin proprotein 3 [Cleaved into: Toxin MSD3]
MSDINVIRAPLLILSILPCVGDDIEVLRRGEGLS
Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L3X0
MSD1_AMAEX
MSDIN-like toxin proprotein 1 [Cleaved into: Toxin MSD1]
MSDINATRLPIFWFIYFPCVSDVDSTLTRGER
Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5L3X2
AAMA2_AMAEX
Alpha-amanitin proprotein 2 [Cleaved into: Alpha-amanitin (Amatoxin) (Gamma-amanitin)]
MSDINATRLPIWGIGCNPCVGDDVTSVLTRGEA
Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
U5L406
AAMA1_AMAEX
Alpha-amanitin proprotein 1 [Cleaved into: Alpha-amanitin (Amatoxin) (Gamma-amanitin)]
MSDINATRLPIWGIGCNPCVGDDVTSVLTRGEALC
Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
U5L408
AAMA5_AMAEX
Alpha-amanitin proprotein 5 [Cleaved into: Alpha-amanitin (Amatoxin) (Gamma-amanitin)]
MSDINATRLPIWGIGCNPCVGDEVAALLTRGEALC
Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
U5L409
MSD2_AMAEX
MSDIN-like toxin proprotein 2 [Cleaved into: Toxin MSD2]
MSDINATRLPIIWAPVVPCISDDNDSTLTRGQR
Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
U5T8F7
PHEA3_HEMAN
Phycoerythrin alpha-3 subunit
MMSKIVLVGLVGSAAAFNAPMMTVRRDAIATGAAAAVVAPILRPAGAAMKKNSKAPCVTIFDERDGCGGPTRAKTGAGEEGLMVKIQMQEIKLGRGAGAEYVSIFTNYDKKLFGVK
Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
U5TBU0
PHEA3_CHRS2
Phycocyanin PC645 alpha-3 subunit
MIAKTAVALALVASAVALRPTMSLSANRREVVAGAGAAAVVAPMLRPAEANAVYTRGTSLSAPVITIFDARGCTDHANKEYKGDWSGRAEDDECCVKIQMQKISVAEDVARLVRLECLNELKSK
Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
U9W8F2
RM31_NEUCR
Large ribosomal subunit protein mL60
MFGAFRFTNPLSGGLLWKIPWRMSKFQKLRQRRRLRAVDNVVATIENALAKKGETVKAVERWRAEMPTEAEMLPKDKYTIFDRKEKRYRKGIHKLPKWTRVSQRVNPPGY
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
V5GZ08
E1132_IXORI
Evasin P1132
MEVKTFAFLQIAVFIALGAQIFLAGTDALSDEDELFSVEYCGTNCTKQDTGSWTTCSGNCTCYHEDGKKVGLCLSTEYTDFTKFPKPTSEEIANARPLPKREKTLN
Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL5 and CXCL8.
V5HBW0
E1156_IXORI
Evasin P1156
MEVKTYAFLQIAVFIFLGMQIFASLTDAADDDNELFTVQYCGMNCTKDEGGTWTGCTGKKEGCKCYHESGKNYGLCLSTEYTDFSQYGNPSDSEIEAAKPKRSDTLSH
Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6 and CXCL8.
V5I2G9
E1172_IXORI
Evasin P1172
FLLKSQLCYCLFGIELIGAGIHALHEDEIFTVDYCGTNCTKQSNGSWTTCPGNCSCYHEDGKTDGFCLSTEYTDFTQFPNLTSEEMDAATPRPE
Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL5 and CXCL8.
V5I3C5
E1174_IXORI
Evasin P1174
LKTFCLFLQIAVFIALGIQIFLCGTDALNNENELFSVEYCGANCTQQDNGSWTKCKGNCTCYHEDGKRYGLCLSTEYTDFTQFPKPTSEEIADASPRPKETNSH
Salivary chemokine-binding protein which binds to host chemokines CXCL1 and CXCL8.
V5ILE0
RT04_NEUCR
Small ribosomal subunit protein uS2m
MIVRNIGARLGRRALATPLSRASFPAQSRFLSQDNFTAPPPPPTNSKKQAAKTAFAEPTLEEQAEFYAESIEKHTPEFAASPAAEAWSAPSATATETVTTWDPSLVDEEALKLKQQIEAIPGNFKLFKQTKAQTQKLGAGVEVRYIPEQYLRNPPSDASLEDLMAAQAHMGHNTSLWNPANARYIYGVRQGIHIISLETTATHLRRAARVVEEVAYRGGLILFVGTRPGQRPIVVRAAELAKACHLFTKWRPGTITNREQLLGGVPLTVVDELDRPLSGFEDHLHDRRPLAPDLVVCLNPKENMTLLYECSLAKIPTIGIIDTNTNPSWVTYQIPANDDSLRATALISGVLGRAGERGQKRRLEAAQRGVVTWKTPADVQGYFELASARAADARRRQAQDNSVEEQKEKDTFLSEDALKAMFGGDARI
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
V5IM60
RM39_NEUCR
Large ribosomal subunit protein bL33m
MAKKAKSRIINVRLISMAMTGYFYTFTRPRTSLPMSMLKYDPIVRRKVLFLEQKRKGRS
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
V5IQE0
RM28_NEUCR
Large ribosomal subunit protein mL40
MSSTFTSLRGLATRLFAGGARPSPSSLLLPNKPATAALPTAIQHQQTASYASKGKSGPPAGMFSGQKAGSKKSKGPKQVDPRIINILRHFAVLSPKRIPPPLRFGRNRYLRHWTIHRAWLLFRRQQREQRERILMQQHQSMSNACEELRNTEGPGTRETGYLYRVAMLKNGVYGLKSIPIEYASRALVETPGRQAWNHEWKR
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
V5QRX7
3098A_MYCTU
Putative toxin Rv3098A/RVBD_3098A
MVIRGAVYRVDFGDAKRGHEQRGRRYAVVISPGSMPWSVVTVVPTSTSAQPAVFRPELEVMGTKTRFLVDQIRTIGIVYVHGDPVDYLDRDQMAKVEHAVARYLGL
Putative toxic component of a possible type II toxin-antitoxin (TA) system. Its toxic effect may be neutralized by cognate antitoxin Rv3098B/RVBD_3098B.
V5T8H7
TCSR1_PAESO
RNA polymerase sigma factor TcsR
MSNLYESIRKYKCGYIEEILNILDMFDPLLNKFQRNSCYEDMKSELSLFMFNLIDNFPLEKDCFKEDKFIINYIYKSLKNKFIQVNKLHQKVKSYETNIDIIWVNNCDYANLLSTVIFEDIIKDLTQNEKNILRKIYLHGLRESEISRELNISRQAVNKTHLRALEKLKKLIN
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (Probable). Transcriptional regulator specifically required to activate expression of the toxin gene locus, composed of tcsL and tcdE/utxA (By similarity).
V5TD18
AMBI3_FISAU
3-((Z)-2-isocyanoethenyl)-1H-indole synthase (EC 1.14.20.11)
MIVSTSVEQSAQFSVKSLTPFGALLEATEDHSDIQQLSIEQLCQLTWEHRLIVLRGFSLLEREELSTYCQRWGELLVWNFGTVLDLIVHQNPENYLFTNGNVPFHWDGAFAEAVPRFLFFQCLKAPEAGSGGESLFCDTVRILQNVSPQQREIWQKTEISYKTQKVAHYGGEITKSLVIKHPITGLSTLRFAEPLNDASVHLNPLYVEVCNLPAEEQNPFINELIENLYLPQNCFAHEWQEGDFLIADNHALLHGRNPFLSNSQRHLQRVHIL
Involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Responsible for the synthesis of Z-3-(2-isocyanoethen)-indole, a biosynthetic precursor to all ambiguines.
V5TES5
AMBI2_FISAU
L-tryptophan isonitrile synthase AmbI2 (EC 4.1.99.25)
MTQIINITQSKVISEQILRHVFRHRRLISDTEPCVHQPCSLCLAPHLEKVQYFVEHNEPIHFILPAFPAKSPNTQKVLGTMPDMGEQVSLKFLQSLCDQISEIYAPGAKLTICSDGRVFSDLVGVTDENVTLYGQIIQALLKEMKADAIDVFNLEDMYTDLSFDEMRQKLVKLYGQTIEAIKDAVKNNDHQCQMFNGIHRFLVEDYQVLEAHKSRNKIRLECKTRAYEVIQRSNAWSVLISELYPHSVRLSIHPQHYHSEKIGIHMIKTLDQWGTPWHNATVFDGKEFMLMKRSHLESMGATLVCQNGHPSYFAWTEQPLETRITVQEVI
Involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Responsible for the synthesis of the isonitrile group on tryptophan using ribulose 5-phosphate as the source of the carbon atom.
V5TF65
AMBI1_FISAU
L-tryptophan isonitrile synthase AmbI1 (EC 4.1.99.25)
MISEKILRHIFQYRRLLSDTEPCAKEPCSICLAPHLPKIQSFIENNEPIHFILPAFPAKSPNPQKVLGPMPDMGERVALQFLQNLCNQISEIYASGAKITICSDGRVFTDLVAITDENVSLYRQGIQRLLNEINADAIDTFCLENVFTGMSFDQMRKTLVKQYAQPIESIQERVNSEDKHRQFFKGIYHLLFDDYLVLYPDKSREQIEVECNLRAYEVIQRSNAWTTLVGQHFPQSLRLSIHPQDYHSNKIGIHMIKTSDQWGTPWHNAPMFNGKEFLLMKRKHIEDIGASLVWHNDHPSHYILSEQVSQALVTLDNKS
Involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Responsible for the synthesis of the isonitrile group on tryptophan using ribulose 5-phosphate as the source of the carbon atom.
V5XKK6
AFT8_ALTAL
Putative epoxide hydrolase AFT8 (EC 3.-.-.-) (AF-toxin biosynthesis protein 8)
MASYKNIPSTAKGSPISFDFSFPQPKLDHLRQVLELHPLGREAPSKTLRGSSKPQWFGNAKEIMRRFDWAAEEELLKAFPHYVVGVEDTIGGQMLQVHFVALFSTSPDAIPVLLIHSWFSSYVEYLCLLSVFTERFPQACDLPFHVIVPSLPGYDFSSPLSRETNNAQINEDNARVLNQLMVNLGFGAGSGGIGGYVVHGGVSSLRMCYTLAKEYKDCRALHANLDGAYRHTLTSSGGDEFEAVKSVLAELHPPEDWDSHERDMIRLAISTSPVSLLALIGSQFFGEQEQGAALRMVALIVAHHWMTDTYPDASQESYCIKDMSAEDLSHVLKHTGLEPNKPVGISFFSHGQGSASDIRPIVDGSSWSSRHEGNPFVAVLDQPNQTVGDLLGFVRQVQKQHS
Putative epoxide hydrolase part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype (Probable). AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2-hydroxy-valeric acid (PubMed:15066029, Ref.4, PubMed:22846083). These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) moiety (PubMed:15066029, Ref.4, PubMed:22846083). On cellular level, AF-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment. The aldo-keto reductase AFTS1 catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an alcohol. The acyl-CoA ligase AFT1, the hydrolase AFT2 and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide synthase AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450 monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural moiety (PubMed:12019223, Ref.4, PubMed:18986255). The exact function of each enzyme, and of additional enzymes identified within the AF-toxin clusters have still to be determined (PubMed:12019223, Ref.4, PubMed:18986255).
V5XYQ7
AF151_ALTAL
Acyltransferase AFT15-1 (EC 2.3.1.-) (AF-toxin biosynthesis protein 15-1)
MKVTITSIDQVLPSVEITAPKSLALSHIDEWHSRGRSSLVWLYPKPKKPTQSLQLLDHLRSSLSQALNKFPQYAGKLSHSLQTGTSQKSKTRLCLTWGTGNDPGVHYITARASSPIDALLPPLGTSTGFTNGSGSYAWDRSGRSCIGLWPAVPLNKVYETCIQITTFECGGFSLSITMNHAVADATSVILFARHWSKTHELMVKVQTPSLSIAEPCFAPHLIDQYSTLELQDEGDNGKLLNKAHALPTLRNDLYESGARSLPDRLELSETYSVGDDIAVGDWERSGPMRSYMLHFSKEDINKIWESAKKEAGQDVSRQAAIVSYIWLAIIRAREWDKHGVCEPIKLFITFDVRRRLGLPDTLLGSPVLVTHVKFNGNDAISKSHGLLANRIWKTLSTYDVESVCAALYDITSSRPLISPAIWLGGRSTLFSSLCHADMYDVTFHETGPLLAAPAFAGMGGMIGLIKSKSAVPSRLPETYEDGIDMFFELDTESSIKLFSDPALSIFDGRALLQEFRQ
Acyltransferase part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype (Probable). AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2-hydroxy-valeric acid (PubMed:15066029, Ref.4, PubMed:22846083). These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) moiety (PubMed:15066029, Ref.4, PubMed:22846083). On cellular level, AF-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment. The aldo-keto reductase AFTS1 catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an alcohol. The acyl-CoA ligase AFT1, the hydrolase AFT2 and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide synthase AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450 monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural moiety (PubMed:12019223, Ref.4, PubMed:18986255). The exact function of each enzyme, and of additional enzymes identified within the AF-toxin clusters have still to be determined (PubMed:12019223, Ref.4, PubMed:18986255).
V5XYR2
AKT41_ALTAL
Hydroxymethylglutaryl-CoA synthase-like protein AKT4-1 (EC 2.3.3.-) (AK-toxin biosynthesis protein 4-1)
MSFCDDREGQRALRILQARLIRSPDACSFALTAVSSLLRKYSIDPRRIGRLEVGTESLVDKSKSIKSFVMQLFEESGNFDIEGVDTVNACYGGTNALFNAVNWVESSAWDGRDAIVVASDISLYGKGNARPTGGAGCVAMLVGPDAPIAFEPGRRGSYMAHTYDFYKPDFTTEYPYINGKHSIECYIQAVEACYRAYTKRERRATERLEEERPDHQAGYETPLDRFDYLCFHSPTNKLVSKSYARLLYVDYLENPANPIFAEVPDSIREVEYRASLTDKSIEKTFMGLAQERFARCVQPSTEIPNMCGNMYSASVYGSLCSLLCNVNSETLLGKRITIFSYGSGLASSMFSLKVRGSTKQMAEKLDVHRRLVDRVVVSPEDVRERAYLKKCFKPKGGAGPIPADVYSLAEVDELFRRVYTVKS
Hydroxymethylglutaryl-CoA synthase-like protein part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype. AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment. The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety. Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes. The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated. The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK-toxin, probably via the catalysis of a side reaction of EDA or its precursor.
V5XZU2
AKT61_ALTAL
Enoyl-CoA hydratase AKT6-1 (EC 4.2.1.-) (AK-toxin biosynthesis protein 6-1)
MTFSTTKSVAMSPDDDAPSFDINSSRRLMSHSEVESRGNGYEVLQQAGTVRILLSRPERGNALSLSLAKDLTQLFQTFSSQHSVHRIVLTGKGKYFCSGMDLGEELYEDATERCLALQDLFGAIDACPKTTVAAINGPAFGGGVGLAFVCDIRVAVSTSFFCLSEVKLGLCPATVSRFIIREWGVSLARMAMLTARKIHPQALQEMGVLHAVALDEEALKVVTENLLDDLGFAAPQASAWCKALTRKTRNGNSDHDQFARQISETMVAPGSESEYGVAQFRRGRKNIRWEQAECLHTR
Enoyl-CoA hydratase part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype. AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment. The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety. Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes. The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated. The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK-toxin, probably via the catalysis of a side reaction of EDA or its precursor.
V6F244
MMS5_MAGGM
Magnetosome protein Mms5
MLSAKGVSLGLGLGLGAWGPVLLGVVGVAGALALYGYYKNRNAEPAAAEAV
Might be involved in magnetite crystal growth.
V9P9L8
ATRGB_MALDO
Alcohol acyl transferase 1 allele RGb (AAT1-RGb) (EC 2.3.1.-)
MMSFSVLQVKRLQPELITPAKSTPQETKFLSDIDDQESLRVQIPIIMCYKDNPSLNKNRNPVKAIREALSRALVYYYPLAGRLREGPNRKLVVDCNGEGILFVEASADVTLEQLGDKILPPCPLLEEFLYNFPGSDGIIDCPLLLIQVTCLTCGGFILALRLNHTMCDAFGLLQFLTAIAEMARGAHAPSILPVWERELLFARNPPRITCAHHEYEDVIDHSDGSYTSSNQSNMVQRSFYFGAKEMRVLRKQIPRHLISTCSTFDLITACLWKCRTLALKINPKQAVRVSCTVNARGKHHNVRLPLGYYGNAFAFPAAVSKAEPLCKNPMGYALELVKKAKATMNEEYLRSVADLLVLRGRPQYSSTGSYLIVSDNTRAGFGDVNFGWGQPVFAGPAKALDLVSFYVQHKNNTEDGILVPMCLPSSAMERFQQEFEMITQEPKEDICNNLRSTSQ
Involved in the biosynthesis of volatile esters which confer ripe apple fruit flavor (By similarity). Alcohol acyl transferase that can use a wide range of alcohols as substrate to produce esters (By similarity).
V9P9S4
ATGSB_MALDO
Alcohol acyl transferase 1 allele GSb (AAT1-GSb) (EC 2.3.1.-)
MMSFSVLQVKRLQLELITPAKPTLQETKFLSDIDDQEGLRFQVPVIMCYKDNPSLNKNCNPVKVIREALSRALVYYYPLAGRLKEGPNRKLMVDCNGEGILFVEASADVTLEQLGDKILPPCPLLEEFLFNFPGSDGIIGCPLLLVQVTCLTCGGFILALRVNHTMCDAPGLLLFLTAIAEMARGAHAPSILPVWERELLFSRDPPRITCVHHEYEDVIDHSDGSYASSNQSNMVQRSFYFGAKEMRVLRKQIPPHVISTCSTFDLITACLSKCRTLALKINPKQAVRVSCVVNARGKHHNVRLPLGYYGNAFACPAAFSKAEPLCKNPLGYALELVKKAKATMNEEYLRSVADLLVLRGRPQYSSTGSYLIVSDNTRAGFGDVNFGWGQPVFAGPAKALDLISFYVQHNNNTEDGILVPMCLPSSAMERFQQELESITPEPKEDICNNLRSTSQ
Involved in the biosynthesis of volatile esters which confer ripe apple fruit flavor (By similarity). Alcohol acyl transferase that can use a wide range of alcohols as substrate to produce esters (By similarity).
V9QEI7
TXA2_LATHE
Alpha-latrotoxin associated low molecular weight protein 2 (Alpha-latrotoxin-associated LMWP2) (Latrodectin-2)
MLKLICIAFLVTVLTLVAGEDSLDPAEYGCADDINQEDLLKKNDVCLQCEDLHKEGVVFSLCKTNCFTTQYFTNCVKDLEEAEKEPPE
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
V9QER4
TXAD_STEGR
Alpha-latrotoxin associated low molecular weight protein SGV242-280 (Alpha-latrotoxin-associated LMWP SGV242-280) (Latrodectin)
MSKLHFLILLSVIVSVFCIEPQDIGCTGISTAEFEEKDATCSKCEEDYSGNGMIDRCRSDCYSGPFFKSCVELLNKGYDEKDENVKPEW
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
V9QF69
TXA1_LATGE
Alpha-latrotoxin associated low molecular weight protein (Alpha-latrotoxin-associated LMWP) (Latrodectin-1) (Latrodectin)
MNKLFFVVFLCLIISVLAIGPADLGCTDMPQAEFDEKNANCEKCGNEEGFGEEMVSRCRDKCFTDNFYQSCVDLLNKVYEEKDVPVPPEE
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
V9QFG7
TXA2_LATGE
Alpha-latrotoxin associated low molecular weight protein 2 (Alpha-latrotoxin-associated LMWP2) (Latrodectin-2)
MLKLICIVFLVTVLTFVVGEDTLDPAEYGCPSDVDMAELTEKNEVCLRCEDFHKEGVAFTLCKTNCFTTEYYKNCVKDLEEAGKETEE
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
V9QFG9
TXAC_STEGR
Alpha-latrotoxin associated low molecular weight protein SGV150-311 (Alpha-latrotoxin-associated LMWP SGV150-311) (Latrodectin)
MNVLHFLILLMSVVSVFCINPEDIGCDDSITPEKFAENDAKCVQCKEQFEETNMLEQCREDCFKGKFFRSCVDHLSGAYDEKDDVEAPPPE
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
V9QFH5
TXA1_LATHE
Alpha-latrotoxin associated low molecular weight protein (Alpha-latrotoxin-associated LMWP) (Latrodectin-1) (Latrodectin)
MSKLFFVAFLCLIISVFATTPDEIGCTDISQAEFDEKNANCIKCGEEGFGEEMVKRCRNKCFTDNFYQSCVDQLNGVYEEKDTPPVKE
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
V9QFH8
TXA2_STEGR
Alpha-latrotoxin associated low molecular weight protein 2 (Alpha-latrotoxin-associated LMWP2) (Latrodectin-2)
MFKLICIVFIATILSITSAADNEDELTIEDFLSYECNESMDIEELKEKDKVCSRCANLHKTQSVIERCRLNCFTSEYFKNCEDNLQAKEEEPEEETL
May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana.
V9TSX0
LPPX_PAEBA
Chaperone protein LppX
MRKWLIFLLIAAVAGLSACSTSGNTTVSDDLVLVEGGAFKTSKSSYSDKNVTLSDFYIGKYEVTQKQWMDVMGDNPSGFKGEERPVERVTWYDAIEYCNARSIKENLKPYYTIDKETTDPDNKNENDNIKWTVTINEGANGYRLPTGAEWEYAASGGQKSQNFTYSGSNNPDEVAWYWMNAGEKPLTGDWNWPAIENNRNQTKPVGQQKANELGIYDMSGNVREWCWEWHSHPETPENTWRISKGGGWVSSVNTAEISYPGKFDANGLGPDQGLRVVRSK
Is required for the expression of the adjacently encoded xylanase Xyn11E in an active form. LppX seems to act as a specific chaperone necessary for the correct folding of the xylanase during secretion across the cytoplasmic membrane.
W2MBG9
RXLR2_PHYPR
Secreted RxLR effector protein 2
MRLLLWVLLVTLVTFLSSGDAAPVDSNKQLERAAINKVTSRNLANDNSLKHEKRFLRGDRSNIVNLKDGDENEERKIGQKMTTALKSIKVWYLKWEQKILLPGFKKMAKKEMTYSKLMDRFRVRMMNSGRWGTPSGFKRYGRLYKDYLISINRADLTV
Secreted effector that completely suppresses elicitor-induced cell death in host and enhances virulence of P.parasitica.
W2N2K3
RXLR5_PHYPR
Secreted RxLR effector protein 5
MRFYYTLLATAAALLVHSDALSAAAETSLNQLTAVDGTTTTSQRFLRRHTDSETTDNEERLNSGPIVLDTAKKIDDLFEVEKLDKILDPKMADKFLDGKTFFGWLDKSALDEALNGNIAQKTKVFEHWREKRLRPKALTKVLTTDPAVRKKYKFVYEMYDSYIKYVARKKLSGLKRNRGD
Secreted effector that partially suppresses elicitor-induced cell death in host and enhances virulence of P.parasitica.
W2P2K7
RXLR3_PHYPR
Secreted RxLR effector protein 3
MRPPLLLFLTVTVLVSCASAVSTGNAAELRSLRSIKTTTNDDAAEEERGGFYHKFDLNFLDDIFHGLPEQFQRMRNQPERLRTMFENWKTGWMSVDDAVAYMTREGLSEKAISQFKAAYQAYLKHKG
Secreted effector that partially suppresses elicitor-induced cell death in host and enhances virulence of P.parasitica.
W4VRU3
ICK41_TRILK
Toxin ICK-41
MKPIVYMLLFCAFTVVILGHPNNHGALIPHHDKLPNGESCTRPGYSCSESSQCCTPVDGETFTYGCGRAWMEGSKICYICNRESSMC
Probable neurotoxin with ion channel impairing activity.
W4VRU5
ICK36_TRILK
U17-barytoxin-Tl1b (U17-BATX-Tl1b) (Toxin ICK-36)
MKTIIVFLSLLVLATKFGDAKEGVNQKQKKEVTQNEFREEYLNEMAAMSLVQQLEAIERALFENEAGRNSRQKRCLGENVPCGDNIPCCGKLACEKTAGYGWWYKSPYCVKPTSG
Ion channel inhibitor.
W4VRU6
ICK31_TRILK
U16-barytoxin-Tl1c (U16-BATX-Tl1c) (Toxin ICK-31)
MKTIIVFLSFLVLVLATKFGDANEGVNREQTKEVIQNEFRGDFLNEMAAMSLLQQLEAIESALLEKEADRNSRQKRCNGKNVPCGSNHSPCCSGLSCEETFGYGWLYKSPYCVIPSNG
Ion channel inhibitor.
W4VRU8
ICK26_TRILK
U16-barytoxin-Tl1b (U16-BATX-Tl1b) (Toxin ICK-26)
MKTIIVFLSLLVLATKFGDAKEGVNQKQKKEVTQNEFREEYLNEMAAMSLVQQLEAIERALFENEAGRNSRQKRCNGENVPCGPNHSTCCSGLSCEETFGYGWWYASPYCVKPSKG
Ion channel inhibitor.
W4VRU9
ICK21_TRILK
Toxin ICK-21
MMKYFLVLCLVVLAVAAVQAAGLEEEKFLNLGESLAMPEESRCKARRYGCTDKAECCSEKCAYPALTCVFNWSCEKVCA
Ion channel inhibitor.
W4VRV1
TX21G_TRILK
Toxin ICK-16
MKPIVSILLFCALAVVIMGHPMNQGYGIPHDVVKLPNGQWCKTPGDDCSKSSECCKAKDTVTYSSGCSQEWSGQLGGFVKLCHICNVESSMC
Probable neurotoxin with ion channel impairing activity.
W4VRV2
ICK11_TRILK
Toxin ICK-11
MMKLYSLVIIATLAAAAFAATSEEISAAVGEIISQHQEDLERYAKVVERGEEPKKYIRCSKQLGESCYLNCECCGAAAVCEDYKYICKEKVSDNSVLNALGQAWNAVGNSISRYYCDAE
Ion channel inhibitor.
W4VRV3
ICK6_TRILK
U12-barytoxin-Tl1a (U12-BATX-Tl1a) (Toxin ICK-6)
MKTMIAWLVLLTFAAALCFADEGLKQEHMNERKKSRFREDIPDEISEDLLLQEMEAMEAELLEKEMRMEENRNSREKRCLGEDISCGEKPGDLVRMPCCAKYECKETAGYWWYQKRFCVKKKSG
Ion channel inhibitor.
W4VRV4
ICK1_TRILK
U8-barytoxin-Tl1a (U8-BATX-Tl1a) (Toxin ICK-1)
MKTLVLVAVLGLASLYLLSYASEVQQLSVAEEEFGALIDAFGGLLETEERGVNKEGCRKFLGGCENTGQCCLHLFCKYDTPFNHFCAWDLSFGRK
Ion channel inhibitor.
W4VRV7
ICK42_TRILK
Toxin ICK-42
MKPIVYMLLFCAFTVVILGHPNNHGALIPHHDKLPNGESCTRPGYSCSESNQCCTPVDGETFTYGCGRAWMEGSKICYICNRESSMC
Probable neurotoxin with ion channel impairing activity.
W4VRW1
ICK37_TRILK
U17-barytoxin-Tl1c (U17-BATX-Tl1c) (Toxin ICK-37)
MKTIIVFLSLLVLATKFGDAKEGVNQKQKKEVTQNEFREEYLNEMAAMSLVQQLEAIERALFENEAGRNSRQKRCLGENVPCGDNIPCCGKLSCEKTFGYPWWYKSPYCVKPSSG
Ion channel inhibitor.
W4VRW4
ICK32_TRILK
U16-barytoxin-Tl1a (U16-BATX-Tl1a) (Toxin ICK-32)
MKTIIVFLSLLVLATKFGDAKEGVNQKQKKEVTQNEFREEYLNEMAAMSLVQQLEAIERALFENEAGRNSRQKRCNGKNVPCGANHSPCCSGLSCEETFGYGWLYKSPYCVIPSNG
Ion channel inhibitor.
W4VRW6
ICK27_TRILK
U16-barytoxin-Tl1c (U16-BATX-Tl1c) (Toxin ICK-27)
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAPMSLLQQLEAIESTLLEKEADRNSRQKRCNGKNVPCGSNHSPCCSGLSCEETFGYGWLYKSPYCVIPSNG
Ion channel inhibitor.
W4VRX0
TX33A_TRILK
Toxin ICK-22
MKLSVIVLVASFGFAVALPSKKREETAAENELTGDQQDAEQHMIYAVAFPEIRTSCVIGWKQQGATCERDCECCGVAATCITGDKSTGFCGYHQTPNVLGQGILYTADTIKNGFSAIFCAG
Ion channel inhibitor.
W4VRX3
TX21H_TRILK
Toxin ICK-17
MKSIVSILLFCALAVVIMGHRLNQGYGIPHDVVKLPNGQWCKTPGDDCSQSSECCKAKDTVTYSSGCSQQWSGQQGGFVNLCRICNVESSMC
Probable neurotoxin with ion channel impairing activity.
W4VRX8
ICK12_TRILK
Toxin ICK-12
MKSIVYMLLFCTFTVVILGHPNDHGALIPYRAEKLPNGEWCIRPGYSCSERGQCCMPVDGDTYTYGCGRAWSEGSKVCFICNRESSMC
Probable neurotoxin with ion channel impairing activity.
W4VRY7
ICK7_TRILK
U13-barytoxin-Tl1a (U13-BATX-Tl1a) (Toxin ICK-7)
MKTIIVFLSLLVLATKFGDAKEGVNQEQKKEVTQNEFRVEYLNEMAAMSLLQQLEAXESALFEKEAGRNSRQXRCAMGDVPCTKGKTNCCKGYECKPKSPSWWYDTDFCQPIHGGRPIGI
Ion channel inhibitor.
W4VRY9
ICK2_TRILK
U9-barytoxin-Tl1a (U9-BATX-Tl1a) (Toxin ICK-2)
MNTMITFLVLFVLTAANGAPEANERKIPEAIHNEDQSLAEMAEELMFFLQQTEFEAPLLQEEEEAEXAEXRNSRERRCAMGDVPCTKGKTNCCKGYECKPKSPAWWYDTDFCQSIHSGRPIGI
Ion channel inhibitor.
W4VS08
ICK40_TRILK
U17-barytoxin-Tl1d (U17-BATX-Tl1d) (Toxin ICK-40)
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAPMSLLQQLEAIESTLLEKEADRNSRQKRCLGENVPCGDFPCCGKLACEKTFGYGWWYKSPFCVKPSKG
Ion channel inhibitor.
W4VS12
ICK35_TRILK
U17-barytoxin-Tl1a (U17-BATX-Tl1a) (Toxin ICK-35)
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCLGENVPCGDFPCCGKLVCQKTFGYGWLYKSPYCVKPSNG
Ion channel inhibitor.