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HexA

Gene
hexA
Protein
Fatty acid synthase alpha subunit hexA
Organism
Dothistroma septosporum (strain NZE10 / CBS 128990)
Length
1692 amino acids
Function
Fatty acid synthase alpha subunit; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690).
Similarity
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family.
Mass
183.262 kDa
Sequence
MGQKTIKRKIQSAERPAEADVAFLASTQHSKDLCYEYDAPEEVAVEEPVDETPAPETAPERPPLSRAKTAAVKPQETAAPTTATIADVPLSAEEIVRALVARKLKKPILSIPTSKSVKELCNGKSTLQNEIVGDFHSEFTNLPDRPEDIPLKELVPASQSLMLGRVSSALLSKLVSSKMPARFNADAIGKYLASKWGLGPLRSVAVMLFAIAAEPEARLGSVAAAEKYLDDTAAKYAEWAGITLQERSTQSSAGGGGSSGTVDPTVLAELTKTNTRLAKRQFQALAEYLQVDLMKPSSEQESEALAVELQQKLDAWTAEFSEEFLAGVAPTFSEKKSRRYNAWWNAARQDVLALFSGNLQEDLSRDAAALEAFLDRLSNRAGESLLAMTRSLSRRNQANAIPGLTDIARRAEKAISSCIDRPATAKVHLPATRPRTTVSDEGDIKFNEVPRPDVSGHAAYADVLQAKDLNGHPAAARFVSLKSAHSHTDLTNGMLDRIRTALDSGMSFAGKNILITGAGQGSIGAEVVRILLTGGARVIVTTSREPSSTAKYFQQMYEESGAKGSELILTRFNQASAKDCENLVDHIYDSSGLDRDLDAVLPFAAAPEGGTEIQDVGAKNELVHRLMLASVFRMLGRVIKNKRDRSIDCHPTQVLLPLSPNHGTFGGDGMYAESKLGLESLVNRVQSESWSDELAICGVKIGWTRGTGLMNANDIVAEAIEDHGVLTFSVQEMAFNIAMLMTPELVDLCENAPLMADFGGGLSALEDCAKILSAARTEINTAADVARAVKAEDDLERAASRTLPAPSSTSPVAKKSMLRIGFPRLPDFELELSPLEHLRDIKDPSETVVVVGFSELGPWGSARLRWEIESKGDFSQVGYMEMAWMMDLIKHVDGPTKNGYYVGWVDSKTGESVHDAEIEARYGEVIRKHSGIRFVDPEGSAGYDPSKKEYLHEVAVEEDLPEFEASSATAEAFRLRHGTNVSISPIEGTENCRVQVKRGASIKIPKSVPFTWGSVAGQLPKGWSPKKYGIPEDLIPQLDPVSLYTICCVAEAFYSAGITDPLEIFKYIHLSEIGNFLGSSMGGALKTRQMYRDIYLDKDIQSDVLQETYLNTTGAWVNMLLLGSTGPIKTPMGACATGVESIDSAFESIMSDKTRMCIVGGFDDFHEDESYGFSTMKATVNVEEELAKGRLPSEMSRPTAESRSGFVEAHGCGVQILCRGDVALEMGLPVYGIIAGSTMAADKVGRSVPAPGQGILTFARETGQAQLDKSSPSTNTTSRTSSVSLARRGATVSPLRASLDAWGLTIDDLDVASLHGTSTKANDLNEPEVICKQMDHLGRTPGRPLWAICQKSVTGHPKAPAAAWMLNGCLQVMDSRTIPANRNADNVDPALQTATHLCFPTRPVRVQDVRAFILTSFGFGQKGGQVVGVAPKYFFATLDEEVYKDYSVRVTKRSKTADRAYAKALMSNAIVKVQDHSPYEQEDQSRIFMDPLSRITEDAETGSYHFDTKDIRNVADVKARLTRLVRGERLNARPDAASGLAQAARSAQAWIEKQTGGRSSVDTSTVGIDLVDLSAFSAHENETFIERNFTEQEKAFAKQSLDQKMAFASRWAAKEAVFKCLHTQTKGAGAAMKDIEIVKSDNAPKVKLHNDCIKAGRKAGLEDIQLSISHGEDCLIAVAIGIAGNGPAKYTL

Gene
hexA
Protein
DNA mismatch repair protein HexA
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Length
844 amino acids
Function
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step.
Similarity
Belongs to the DNA mismatch repair MutS family.
Mass
94.848 kDa
Sequence
MAIEKLSPGMQQYVDIKKQYPDAFLLFRMGDFYELFYEDAVNAAQILEISLTSRNKNADNPIPMAGVPYHSAQQYIDVLIEQGYKVAIAEQMEDPKQAVGVVKREVVQVITPGTVVDSSKPDSQNNFLVSIDREGNQFGLAYMDLVTGDFYVTGLLDFTLVCGEIRNLKAREVVLGYDLSEEEEQILSRQMNLVLSYEKESFEDLHLLDLRLATVEQTASSKLLQYVHRTQMRELNHLKPVIRYEIKDFLQMDYATKASLDLVENARSGKKQGSLFWLLDETKTAMGMRLLRSWIHRPLIDKERIVQRQEVVQVFLDHFFERSDLTDSLKGVYDIERLASRVSFGKTNPKDLLQLATTLSSVPRIRAILEGMEQPTLAYLIAQLDAIPELESLISAAIAPEAPHVITDGGIIRTGFDETLDKYRCVLREGTSWIAEIEAKERENSGISTLKIDYNKKDGYYFHVTNSQLGNVPAHFFRKATLKNSERFGTEELARIEGDMLEAREKSANLEYEIFMRIREEVGKYIQRLQALAQGIATVDVLQSLAVVAETQHLIRPEFGDDSQIDIRKGRHAVVEKVMGAQTYIPNTIQMAEDTSIQLVTGPNMSGKSTYMRQLAMTAVMAQLGSYVPAESAHLPIFDAIFTRIGAADDLVSGQSTFMVEMMEANNAISHATKNSLILFDELGRGTATYDGMALAQSIIEYIHEHIGAKTLFATHYHELTSLESSLQHLVNVHVATLEQDGQVTFLHKIEPGPADKSYGIHVAKIAGLPADLLARADKILTQLENQGTESPPPMRQTSAVTEQISLFDRAEEHPILAELAKLDVYNMTPMQVMNVLVELKQKL

Gene
hexA
Protein
DNA mismatch repair protein HexA
Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Length
844 amino acids
Function
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step.
Similarity
Belongs to the DNA mismatch repair MutS family.
Mass
94.848 kDa
Sequence
MAIEKLSPGMQQYVDIKKQYPDAFLLFRMGDFYELFYEDAVNAAQILEISLTSRNKNADNPIPMAGVPYHSAQQYIDVLIEQGYKVAIAEQMEDPKQAVGVVKREVVQVITPGTVVDSSKPDSQNNFLVSIDREGNQFGLAYMDLVTGDFYVTGLLDFTLVCGEIRNLKAREVVLGYDLSEEEEQILSRQMNLVLSYEKESFEDLHLLDLRLATVEQTASSKLLQYVHRTQMRELNHLKPVIRYEIKDFLQMDYATKASLDLVENARSGKKQGSLFWLLDETKTAMGMRLLRSWIHRPLIDKERIVQRQEVVQVFLDHFFERSDLTDSLKGVYDIERLASRVSFGKTNPKDLLQLATTLSSVPRIRAILEGMEQPTLAYLIAQLDAIPELESLISAAIAPEAPHVITDGGIIRTGFDETLDKYRCVLREGTSWIAEIEAKERENSGISTLKIDYNKKDGYYFHVTNSQLGNVPAHFFRKATLKNSERFGTEELARIEGDMLEAREKSANLEYEIFMRIREEVGKYIQRLQALAQGIATVDVLQSLAVVAETQHLIRPEFGDDSQIDIRKGRHAVVEKVMGAQTYIPNTIQMAEDTSIQLVTGPNMSGKSTYMRQLAMTAVMAQLGSYVPAESAHLPIFDAIFTRIGAADDLVSGQSTFMVEMMEANNAISHATKNSLILFDELGRGTATYDGMALAQSIIEYIHEHIGAKTLFATHYHELTSLESSLQHLVNVHVATLEQDGQVTFLHKIEPGPADKSYGIHVAKIAGLPADLLARADKILTQLENQGTESPPPMRQTSAVTEQISLFDRAEEHPILAELAKLDVYNMTPMQVMNVLVELKQKL

Gene
HexA
Protein
Hexamerin-1.1
Organism
Anopheles gambiae
Length
692 amino acids
Function
Larval storage protein (LSP) which may serve as a store of amino acids for synthesis of adult proteins.
Similarity
Belongs to the hemocyanin family.
Mass
83.495 kDa
Sequence
MKLLILAVAISLAVLASGSYVPSTKFEAKYADKEFLFKQKFFFEVLRNIHLPLKYDEYIPYTKTWVSDETKYNDFAQVAEFFDYYKTGAFLEKGELFSIYNEQYLRQTYAVFTFLYNSADWDTYYKNMIWARDNINEGMFIYVLHLTVMHRPDLQGIVLPAIYEIYPYYFFNTDVIRTINYKKLYDPKFGFYGNGKYNVVYANYTATYPMDYYNNFYTEEYLNYYTEDIGLNACYYYFMMDYSFLLGGDKFGLIKDRRGELYWYMHQMLLARYNLERMSNYMGTVKPLVWRFPLKTGYFSLLSYWNGVPFKSRDYNYMISDESYFKLDWINAWEAKIRKIIEDGFFVKEDGTRINLRLPESVEFFGNLLNSNVDSVDANYVGYIEVFSRLLLSGNDFNAYKVWPSALMQFETSLRDPVFYQLYERFMDLYYYFKRFLPSYTYEELNFNGVVIKDVTFDKLMTYFDYFDSDVSNVLPMQSTDKYFDYAVFARQRRLNHKPFSYTMNVMSDYTGKAIIRAFVGPKFDRFFDLQFYKKYFFEIDQYLVDFTAGKNTFVRNSRDFYWSVKDRTMYTDLYKKIMLGYNGQEKFALDMSEAHCGFPDRLILPKGWTSGMPMQFYFIITPYTAKTYEQGYQYDKTFTCGVESGMRFYDSLPFGYPFDRVINFNYFYTKNMYFKDVFIFHTEEMKMNQRY

Gene
HEXA
Protein
Beta-hexosaminidase subunit alpha
Organism
Entamoeba histolytica
Length
564 amino acids
Function
Hexoaminidase complex may contribute to amoebic pathogenicity and may be involved in the destruction of extracellular matrix components.
Similarity
Belongs to the glycosyl hydrolase 20 family.
Mass
63.935 kDa
Sequence
MLFIFIVFISSVFAGNGLNVQNQLLLMPYPSSVSFQWKSPLAIALTSSIQLNVKSTCNTDCMNFLKSNFNHTISFPLQQQTGLQDFKVSLFKEIDLPRITPSVSSVITDVVVELSSSNPMPKLQIGFDESYILEVTTNSISIKAVTVYGARHAFETLLQLIRISSNKFVISQLPIKISDAPRFKWRGLMVDPSRNPLSPLMFKRIIDTLASVKANVLHIHLSDAQTFVFESKKYPLLHQKGMYDESFVLTQSFLRELAQYGANRGVIVYGEIDTPAHTASWNLGYPGVVANCWDYIVSTSMRYGENVLSLNPANPNTFPIIDALMKELSDTFGTDYVHVGGDEVWTSGWSKSKEYSDIQKFMKSKGLNSLTELEGYFNKYAQEQVIHNGKHPVVWEEVFKKGNADKNTIIQVWDDIRLLQQVVNSGYKAIFSAGFYLDKQMPLCNSYDSSTCVNTHSMWVWTNRDMYDNDPVKSLSSSEKENVLGGEGCSWGESTDEQNFFDRVFQRYSAIAERLWSKESVVDKESHEVRANYLRCLDVRRDIMKGTGPLYHSFCQLPKKEKSN

Gene
HEXA
Protein
Beta-hexosaminidase subunit alpha
Organism
Bos taurus
Length
529 amino acids
Function
Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.
Similarity
Belongs to the glycosyl hydrolase 20 family.
Mass
60.353 kDa
Sequence
MAGSTLRFSLLLAAAFAGRATALWPWPQYIQTSELRYTIFPQSFQFQYHLSSAAQVGCSVLDEAFQRYRDLLFGSVAFRFPHPIEKRHTSEKNSLVVLVVTPGCDQFPSLGSVENYTLTINDEQSLLLSETVWGALRGLETFSQLIWRSPEGTFYVNKTDIEDFPRFPHRGLLLDTSRHYLPLASILDTLDVMAYNKFNVFHWHLVDDSSFPYESFTFPELTKKGSYNPATHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGVPGLLTPCYSGSHPSGTFGPVNPALNNTYEFMSTFFLEISTVFPDFYLHLGGDEVDFTCWKSNPDIQAFMKKKGFGDDFKKLESFYIQTLLDIVSAYGKGYVVWQEVFDNKVKVRPDTIIQVWREEIPVKYVKELALVTRAGFRALLSAPWYLNHITYGPDWKEIYLVEPLAFEGSPEQKALVIGGEACMWGEYVDSTNLVPRLWPRAGAVAERLWSNKMVSNLDFAFKRLAHFRCELLRRGVQAQPLSVGYCDMEFEQT

Gene
HEXA
Protein
Beta-hexosaminidase subunit alpha
Organism
Homo sapiens
Length
529 amino acids
Function
Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. The form B is active against certain oligosaccharides. The form S has no measurable activity.
Similarity
Belongs to the glycosyl hydrolase 20 family.
Mass
60.703 kDa
Sequence
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT

Gene
HEXA
Protein
Beta-hexosaminidase subunit alpha
Organism
Pongo abelii
Length
529 amino acids
Function
Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.
Similarity
Belongs to the glycosyl hydrolase 20 family.
Mass
60.605 kDa
Sequence
MASSRLWFSLLLAAALAGRATALWPWPQNIQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPDIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIRPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYVVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT

Gene
Hexa
Protein
Beta-hexosaminidase subunit alpha
Organism
Mus musculus
Length
528 amino acids
Function
Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.
Similarity
Belongs to the glycosyl hydrolase 20 family.
Mass
60.613 kDa
Sequence
MAGCRLWVSLLLAAALACLATALWPWPQYIQTYHRRYTLYPNNFQFRYHVSSAAQAGCVVLDEAFRRYRNLLFGSGSWPRPSFSNKQQTLGKNILVVSVVTAECNEFPNLESVENYTLTINDDQCLLASETVWGALRGLETFSQLVWKSAEGTFFINKTKIKDFPRFPHRGVLLDTSRHYLPLSSILDTLDVMAYNKFNVFHWHLVDDSSFPYESFTFPELTRKGSFNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGAPGLLTPCYSGSHLSGTFGPVNPSLNSTYDFMSTLFLEISSVFPDFYLHLGGDEVDFTCWKSNPNIQAFMKKKGFTDFKQLESFYIQTLLDIVSDYDKGYVVWQEVFDNKVKVRPDTIIQVWREEMPVEYMLEMQDITRAGFRALLSAPWYLNRVKYGPDWKDMYKVEPLAFHGTPEQKALVIGGEACMWGEYVDSTNLVPRLWPRAGAVAERLWSSNLTTNIDFAFKRLSHFRCELVRRGIQAQPISVGYCEQEFEQT

Gene
Hexa
Protein
Beta-hexosaminidase subunit alpha
Organism
Rattus norvegicus
Length
528 amino acids
Function
Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.
Similarity
Belongs to the glycosyl hydrolase 20 family.
Mass
60.538 kDa
Sequence
MAGCRLWVSLLLAAALACLATALWPWPQYIQTSHRRYTLYPNNFQFRYHAGSAAQAGCVVLDEAFRRYRSLLFGSGSWPRPSFSKKQQPLGKNILMVSVVTAECNEFPNLESVENYTLTINDDQCLLSSETVWGALRGLETFSQLVWKSAEGTFFINKTKITDFPRFPHRGILLDTSRHYLPLSSILNTLDVMAYNKFNVFHWHLVDDSSFPYESFTFPELTRKGSFNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGAGVPGLLTPCYSGSRLSGTYGPVNPSLNSTYDFMSTFFLEISSVFPDFYLHLGGDEVDFTCWKSNPNIQAFMKKKGFTDYKQLESFYIQTLLDIVSDYDKGYVVWQEVFDNKVKVRPDTIIQVWREEMPVQYMKEIEAITQAGFRALLSAPWYLNRVKYGPDWKEMYKVEPLAFRGTPAQKALVIGGEACMWGEYVDSTNLVPRLWPRAGAIAERLWSSNLTTNMDFAFKRLSHFRCELLRRGIQAQPISVGYCEQEFEHT

Gene
hexA
Protein
Fatty acid synthase alpha subunit hexA
Organism
Dothistroma septosporum
Length
325 amino acids
Function
Fatty acid synthase alpha subunit; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690).
Similarity
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family.
Mass
35.522 kDa
Fragment
single
Sequence
AAAWMLNGCLQVMDSRTIPANRNADNVDPALQTATHLCFPTRPVRVQDVRAFILTSFGFGQKGGQVVGVAPKYFFATLDEEVYKDYSVRVTKRSKTADRAYAKALMSNAIVKVQDHSPYEQEDQSRIFMDPLSRITEDAETGSYHFDTKDIRNVADVKARLTRLVRGERLNARPDAASGLAQAARSAQAWIEKQTGGRSSVDTSTVGIDLVDLSAFSAHENETFIERNFTEQEKAFAKQSLDQKMAFASRWAAKEAVFKCLHTQTKGAGAAMKDIEIVKSDNAPQGQAGRKAGLEDIQLSISHGEDCLIAVAIGIAGNGPAKYTL