G3XUF0 · MLFA_ASPNA
- ProteinMalformin synthetase mlfA
- GenemlfA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids4870 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of malformins, cyclic pentapeptides with a disulfide bond between 2 consecutive cysteins, that show potential anti-tumor as well as antimalarial and antitrypanosomal properties (PubMed:30560908).
The nonribosomal peptide synthetase mlfA is responsible of the formation of the cyclic pentapeptide (Probable). The malformin biosynthesis clusters in malformin-producing fungi also contain enzymes involved in the formation of the disulfide bond between the two consecutive cysteins within malformins, in addition to additional tailoring enzymes such as methyltransferases or oxidoreductases. They are also composed of up to 4 major facilitator superfamily transporters, and transcription factors probably involved in the regulation of the expression of those clusters (Probable)
The nonribosomal peptide synthetase mlfA is responsible of the formation of the cyclic pentapeptide (Probable). The malformin biosynthesis clusters in malformin-producing fungi also contain enzymes involved in the formation of the disulfide bond between the two consecutive cysteins within malformins, in addition to additional tailoring enzymes such as methyltransferases or oxidoreductases. They are also composed of up to 4 major facilitator superfamily transporters, and transcription factors probably involved in the regulation of the expression of those clusters (Probable)
Biotechnology
Malformins show anti-tumor properties against human colorectal and prostate cancer cells by the inhibition of proliferation and induction of apoptosis through the activation of the p38 signaling pathway (PubMed:26540166, PubMed:26645406, PubMed:28713983).
Malformin C has also been shown to exhibit potent antimalarial and antitrypanosomal properties (PubMed:19876076).
Malformin C has also been shown to exhibit potent antimalarial and antitrypanosomal properties (PubMed:19876076).
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ligase activity | |
Molecular Function | phosphopantetheine binding |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMalformin synthetase mlfA
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionG3XUF0
Proteomes
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000446435 | 1-4870 | Malformin synthetase mlfA | |||
Sequence: MSRRSLINAAEQLLHPGPVGAGQVSGESANTIITFEKDIESLFVTQAEAANVGTAMAQALAEVGADDHNRLIKNLNLMSPTHLESIWQFNANVPGMWEECFHDVIERRAANRPHSLAVDAWDMKLTYADLVREARLLAAYLQHRGVRPGSVVPISFERSGAALVAMLAVSKAGGAFVSVPPTLPAGRLDAILEVIEAPFVVTWSKYEPFWAERLPTLPIDSYPKPSADATVKTLGKPEDLFYVIFTSGSTGRPKGCMLSHSNWLNGALRNAPSWKYGPESRVLQMLSHTFDMSLLEICTSLGSGACVCVPRTEEIETSVSDAINRWQVNHVIMTPSLARSLRRDDVPGLKTMCLGGEAFPREIVTMWSERINLWQFYGPSECSINSSSRPITRPDADPLNIGPPNSAACWVVDTQDYNKLVPVGAIGELLVSGPIVGMGYLKNPIKTAEAFLDEVGFVAKDDPQFGGFRFYRTGDLVRWNSDGTITFCGRADTQVKLNGQRLELAEVEYQLGLEAGVQYAIAMAPQSGRCKNNLIAVLTVKCGGASNQGNADDEIPLLDRHDPIVQQTVKKLRSQLQHALPRYMVPTIWAFVGRMPMSPSGKIDRVQLRNWVQEMSQETFDAITGRSFEAEDHVLGLSQLEQEIQLAWAEALGLSAAEVGLQQPFVALGGDSIKALDAVARCRARQIKISMVHILSCEGVREASSLAEVQETPAHQVAEIAVDYSDLWTRLSTEYDISKLGVTQVEEVEDVFPCTTMQEGMFLGQIRRPGAYHMRFFHRVQLKGGSLPTVERIQQAWASLVERHPSLRTVFVDDLSSEAIYHSVVLRSVPMELTMREVPRDLNPESALAMFTEELVPFRPNAPLHRMLLLTCRGRVPYLMLEISHVIMDGYALSVFRREFIRACSSTASLPRGPDYRMFANYHRTRQTDESAKYWTNYLADCVPCHIPTDPLSVPTDASPEWPRTLQRRDFGFDNSVAFLQRCKERQVTLACAIRAAWALVLRAYTQSRDVCFGYVSSGRNVPVPEVETIFGLCLSMQGLFNTAISMEWVPPTAEDEDALLDLEEIREQDDPTEYDIAISVDIHEGHIKLGFLYWPNLSDFQITHLAEALQGAMNCFAFQPDVALNTLTLLQASDLCSTLTNGPTLLPLEAVRGNVISMIDRWVTRQPESPAIDGWDGSLTYKQLHEQSSWVARNLLHQGVKLGDRILVCADRSSRTVVTILGVVRAGCVLVLSNPTDPEKRLQWLAHKCNATLVVVDPAYEERFATSGARVFSTTSVCAPAAWDYEFSALDDQDLVSILFTSGSTGTPKGILMDHGALATSVLLGHGRTLRFSRHTRMLHFASLTFDAALAEIFTTLAHGGCICVPCEEDRLSDVSGCISRFAVNTAMLTPSVGRLLDPEALPTLKALAMIGEPMSRLDVERFAPVLDLYNGAGPTETSIMVTIAGPMKPTDEPVNLGYAVAGVRLWVTEAENPNRLAPLGAVGELIVEGRLVTRGYLDDPARTRESFLPNLPWLPSQHALYRTGDLVRYAEDGSLRYMGRKDTQVKLRGQRIELQEVEYHLRKSLQQAQVVVEMVIPEGKIRAQASLVAFVSGLTAADVESSSARNFDQSMPMSQIALPGSTIQALEEALPRYMIPSVYFALDTIPLSVNGKADRRRLREIGAALLVSSTAHKNTVDGKSEPVKWTASSKLELTLLELWTTTLGLEAETIYGDDSFFELGGDSVSAMKLVATARDRFKLSLSVPQMFRHPTIHQLAAILGEATGQPESSASSTTEEGFTFSTPDDSSTNDGVDDDFLRLATAQLAQLAQEKGKKVDIAALLKQLQGGSSSCKTPSVSSSSSSSSSRKKKSAKVVSPVEAPAPVPVPFSLLDGGADVVEKIRAQAVEQCKILPGDIEDIYPATALQEGMMALMARTPGVYTTTLTCELPERVNLARLHSAWDKAAEAHPILRTRIILTENNTAVQVVQRAKELPWDAYSLQDGDPLPDLTSNMTLGSTLLRLAEIHRQNQPRMLLVAIHHALYDGWSMPLLKQAVEDVYHGQELWPQPFTPFINYLNEGKPAAQGYWTAHLDGFAGSVFPNLPSINHHIQPTERRTRSLAVPTAPPGSQYTMATKIQAAWAVTVSRYAEAEDIVFGTVSTGRSAPVPSIDRMVGPTITTVPVRISLGNQAERLTSLLQRVQEDGWNRMDHEHLGLQHIRRLGESAAAACNLQTLLVIQPREEPRAKSISTLLSGLQDVAELKGVDTYPLMLVCEPDGVSLHLTAVFDPAVLDAVMLDRMLAHWELVLNQIWSEPDMAVMGLDGVSYRDKQTLVRWNAGEKIADGCAHDAVYEWSVRTPHAPAVFAWDGKWTYEELEKCSSLIASQVLVHGVSSGDFVALYHEKSRWAAAAILAVFKAGGILVTLDPAHPKDRIKDILDQARPRLVLTSQSLLDEARELETPVMVVQFAASQPMPGECFPLPTVSPTQAAYAPFTSGSTGRPKGIPLEHRGLAASTASVARACLLRPASRVLHFASFAFDASMMEHLIAWHAGSCLCIPVETVRQTDLARCIRDFEVTWAFLTPSCLRLISPDDVQSLEALGLGGESMTPEDIFIWGPRLRQIVQLYGPAECSIVAALTEVTKPSENRLIGRPNACRCWVVDPHSPDRLAPLGAVGELVIEGITVGRGYIDDPERTTQAFIPPPTWIQTLYPNEQQPSRLYRTGDLVRYAGTDGKLTFIGRRDGQLKLHGQRIELADVEAHLRPLIPGTQKVVVEMVHSVGNHHPLLAAFVEEILTSQDQVEQVVNLLHPSQTQCALNVKAIDSALSQTVPQYMIPSMYLHISRLPLSASGKLNRRHLRRLVAEFPRQRLSEYAAGSGLAVPNRPATAQEREMQAIWARVLSVDPDTIGVNEDFFRIGGDSISGMQVATRCNAAGMHITSADLFQHRTIEQLMRHLSANGKTGSASISLPPEPVDEWVPLAPIQQLFFEIAPQGPDHFNQSLLLRTSRRVSAEKLAGGLDILVGRHSMLRARFCRDDSGQWSQQVRSRGPYPASAFYRLTTHNHIAPELLSSLLAASQMALSIQEGPLLAVDLVNLTDDTQLVYLVAHHLIIDLVSWRILHAELEEYLQTGSFASTTGSVPFLTWSRAQAEYSANHLTPTLPLPGFQEANDGFDASRYWGISCESNTFGQTSTSTFTLDQTVTDQLFGPANNVLDTRPAEILQAALWYSFTQSLTDRPGPSIYVEGHGREPWTGSIDLSGTVGWFTTMSPLVSAPWDSLSQTSMRDFLDALSYIKDQRRRIPANGWAYFTSRYLNDEGKVAYGRMKPVVEILFNYMGQYQEMNREDAILQLAGDGIQSGTGAADVADNVPRFSLIDVSAFISNGCLTFQFILPKSLQQDSRLQGCFQEYERTLVAAANSLSTEGPRKTLADFPLMPALTYDQLSQCLDHTLPSMGLCARDVVDIYPCSPVQQGMLLAQLRDRQAYQQRFRFQVKSRGSTDRLTLEKLKDAWTEVINRHDILRTLLLPVSDYSHLDQVVMAPGSLQHLVRINAMDTNPTQGLPHSINITSDSTGTVICEWNVSHALVDAMSIAVIQQEVNEALEGSLGQHQKTPRYADYIQWLSLQDNTETQAYWKKYLEGVEPCLFPKLASSTDKVNPEGTISAIRATWTRDSRLDKLCHTHGITLTNLFHIVWSLLLSAYLGTDKVCFGYTTLGRDVPVDGVEKMVGPLVNVIATTIQLQEDDSILDALLTHQTHLSNSLQHQHYALADVYASLGLVGSQLFNTIVSLQDISHFDANDERPTRVEMLPANDVSEYDVALNIGVDQSSIQVVCSYRTLSLSVEQADALLRTTSHVLDEILRDPKQPLRDLEVISPQCKEQLVKWNAAMPAPTDEYIHEKIQDQCRLHSSREAACAWDGIFTFAEVDDLSSRLAARLIRMGVTSGHIIPIYSPKSRWTVIAILGVLKTGAAFTLLETSHPTARLRVICNEIKADIIIAPASHAVPAATLAPILVVLDSITSMSPQESDLLPAVGMPPAAEALAYLIFTSGSTGNPKGVMVTHQNLCSNASIMTTSVNMTSDSRVLHFASHAFDACLWEIFGALFAGACLIIPSESETKEDLAGCIERMVVTWAFLTPSVARILKPEALPSLRNLVLGGEPIAASDLDMWRGHVQVVCAYGPTETAILASTTSPSTFPSDGKDIGVPTGSSLWIVDKQNYNKLAPHGATGELLIEGPNVSQGYLGDPEKTNEAFPVAPRWLSQLRKSPTRVYRTGDLVRFNTSTGTIHFVGRKDNQIKFHGQRIELGDIEHHAQQAFSNASMVIVDLITPEQPQQPYIVAFVHQADTRTGTADPIDTILLPPSESFRADAIGAQNHMHKRLPHYMVPTAFLPLHRLPLSGTGKADRKRLRQCALSLSSLELNAYRATASAKRMPFTAAECKMQELVATVLGRDMSEIGMDDSFFYLGGDSIQAMRLVSEGRQQGLTLSLQAIFDAPRLGDLAYRTANLVRVSEPAPPTLPATSSDDCDHKETIVAALPIKKTDVAEVLPTTSFQRTWLDSQLKSYIVVDIPGPIDLARLRTAIQRVVKAHPILRASFVPYETTTMQVILRTAVVITEADLSTTTVEGICRKDANAPMAPGTPYLRVILATQGEVDRKLIMRLSHAQYDGISLSLLMNDLSHAYASESRPLPSSHLPAFNDYITYQQTQGADPTATTFWHRLLKDVPITYLDLQPAETPTSNGSLITRTRDINIAAFPSLPNGITTATAVKAAWSLVLAQKTGSLAVIFGQVVHGRGIALTGVEGIVGPCANITPVVARLGPQTTRMELMQTLQDQHRSAMPYETAGRKELQTIVQHQNNVMADDMELSLGEARWGKTGYVGGEDHVVDVGVE | ||||||
Modified residue | 672 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 1725 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 2901 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 4448 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 106-497 | Adenylation 1 | ||||
Sequence: ERRAANRPHSLAVDAWDMKLTYADLVREARLLAAYLQHRGVRPGSVVPISFERSGAALVAMLAVSKAGGAFVSVPPTLPAGRLDAILEVIEAPFVVTWSKYEPFWAERLPTLPIDSYPKPSADATVKTLGKPEDLFYVIFTSGSTGRPKGCMLSHSNWLNGALRNAPSWKYGPESRVLQMLSHTFDMSLLEICTSLGSGACVCVPRTEEIETSVSDAINRWQVNHVIMTPSLARSLRRDDVPGLKTMCLGGEAFPREIVTMWSERINLWQFYGPSECSINSSSRPITRPDADPLNIGPPNSAACWVVDTQDYNKLVPVGAIGELLVSGPIVGMGYLKNPIKTAEAFLDEVGFVAKDDPQFGGFRFYRTGDLVRWNSDGTITFCGRADTQVKL | ||||||
Domain | 635-711 | Carrier 1 | ||||
Sequence: LGLSQLEQEIQLAWAEALGLSAAEVGLQQPFVALGGDSIKALDAVARCRARQIKISMVHILSCEGVREASSLAEVQE | ||||||
Region | 749-1133 | Condensation 1 | ||||
Sequence: EDVFPCTTMQEGMFLGQIRRPGAYHMRFFHRVQLKGGSLPTVERIQQAWASLVERHPSLRTVFVDDLSSEAIYHSVVLRSVPMELTMREVPRDLNPESALAMFTEELVPFRPNAPLHRMLLLTCRGRVPYLMLEISHVIMDGYALSVFRREFIRACSSTASLPRGPDYRMFANYHRTRQTDESAKYWTNYLADCVPCHIPTDPLSVPTDASPEWPRTLQRRDFGFDNSVAFLQRCKERQVTLACAIRAAWALVLRAYTQSRDVCFGYVSSGRNVPVPEVETIFGLCLSMQGLFNTAISMEWVPPTAEDEDALLDLEEIREQDDPTEYDIAISVDIHEGHIKLGFLYWPNLSDFQITHLAEALQGAMNCFAFQPDVALNTLTLLQA | ||||||
Region | 1161-1550 | Adenylation 2 | ||||
Sequence: DRWVTRQPESPAIDGWDGSLTYKQLHEQSSWVARNLLHQGVKLGDRILVCADRSSRTVVTILGVVRAGCVLVLSNPTDPEKRLQWLAHKCNATLVVVDPAYEERFATSGARVFSTTSVCAPAAWDYEFSALDDQDLVSILFTSGSTGTPKGILMDHGALATSVLLGHGRTLRFSRHTRMLHFASLTFDAALAEIFTTLAHGGCICVPCEEDRLSDVSGCISRFAVNTAMLTPSVGRLLDPEALPTLKALAMIGEPMSRLDVERFAPVLDLYNGAGPTETSIMVTIAGPMKPTDEPVNLGYAVAGVRLWVTEAENPNRLAPLGAVGELIVEGRLVTRGYLDDPARTRESFLPNLPWLPSQHALYRTGDLVRYAEDGSLRYMGRKDTQVKLR | ||||||
Domain | 1688-1765 | Carrier 2 | ||||
Sequence: TASSKLELTLLELWTTTLGLEAETIYGDDSFFELGGDSVSAMKLVATARDRFKLSLSVPQMFRHPTIHQLAAILGEAT | ||||||
Region | 1764-1794 | Disordered | ||||
Sequence: ATGQPESSASSTTEEGFTFSTPDDSSTNDGV | ||||||
Compositional bias | 1766-1789 | Polar residues | ||||
Sequence: GQPESSASSTTEEGFTFSTPDDSS | ||||||
Compositional bias | 1829-1852 | Polar residues | ||||
Sequence: GSSSCKTPSVSSSSSSSSSRKKKS | ||||||
Region | 1829-1859 | Disordered | ||||
Sequence: GSSSCKTPSVSSSSSSSSSRKKKSAKVVSPV | ||||||
Region | 1898-2313 | Condensation 2 | ||||
Sequence: EDIYPATALQEGMMALMARTPGVYTTTLTCELPERVNLARLHSAWDKAAEAHPILRTRIILTENNTAVQVVQRAKELPWDAYSLQDGDPLPDLTSNMTLGSTLLRLAEIHRQNQPRMLLVAIHHALYDGWSMPLLKQAVEDVYHGQELWPQPFTPFINYLNEGKPAAQGYWTAHLDGFAGSVFPNLPSINHHIQPTERRTRSLAVPTAPPGSQYTMATKIQAAWAVTVSRYAEAEDIVFGTVSTGRSAPVPSIDRMVGPTITTVPVRISLGNQAERLTSLLQRVQEDGWNRMDHEHLGLQHIRRLGESAAAACNLQTLLVIQPREEPRAKSISTLLSGLQDVAELKGVDTYPLMLVCEPDGVSLHLTAVFDPAVLDAVMLDRMLAHWELVLNQIWSEPDMAVMGLDGVSYRDKQTL | ||||||
Region | 2336-2728 | Adenylation 3 | ||||
Sequence: VRTPHAPAVFAWDGKWTYEELEKCSSLIASQVLVHGVSSGDFVALYHEKSRWAAAAILAVFKAGGILVTLDPAHPKDRIKDILDQARPRLVLTSQSLLDEARELETPVMVVQFAASQPMPGECFPLPTVSPTQAAYAPFTSGSTGRPKGIPLEHRGLAASTASVARACLLRPASRVLHFASFAFDASMMEHLIAWHAGSCLCIPVETVRQTDLARCIRDFEVTWAFLTPSCLRLISPDDVQSLEALGLGGESMTPEDIFIWGPRLRQIVQLYGPAECSIVAALTEVTKPSENRLIGRPNACRCWVVDPHSPDRLAPLGAVGELVIEGITVGRGYIDDPERTTQAFIPPPTWIQTLYPNEQQPSRLYRTGDLVRYAGTDGKLTFIGRRDGQLKL | ||||||
Domain | 2864-2940 | Carrier 3 | ||||
Sequence: RPATAQEREMQAIWARVLSVDPDTIGVNEDFFRIGGDSISGMQVATRCNAAGMHITSADLFQHRTIEQLMRHLSANG | ||||||
Region | 2957-3422 | Condensation 3 | ||||
Sequence: WVPLAPIQQLFFEIAPQGPDHFNQSLLLRTSRRVSAEKLAGGLDILVGRHSMLRARFCRDDSGQWSQQVRSRGPYPASAFYRLTTHNHIAPELLSSLLAASQMALSIQEGPLLAVDLVNLTDDTQLVYLVAHHLIIDLVSWRILHAELEEYLQTGSFASTTGSVPFLTWSRAQAEYSANHLTPTLPLPGFQEANDGFDASRYWGISCESNTFGQTSTSTFTLDQTVTDQLFGPANNVLDTRPAEILQAALWYSFTQSLTDRPGPSIYVEGHGREPWTGSIDLSGTVGWFTTMSPLVSAPWDSLSQTSMRDFLDALSYIKDQRRRIPANGWAYFTSRYLNDEGKVAYGRMKPVVEILFNYMGQYQEMNREDAILQLAGDGIQSGTGAADVADNVPRFSLIDVSAFISNGCLTFQFILPKSLQQDSRLQGCFQEYERTLVAAANSLSTEGPRKTLADFPLMPALTYDQ | ||||||
Region | 3443-3862 | Condensation 4 | ||||
Sequence: DIYPCSPVQQGMLLAQLRDRQAYQQRFRFQVKSRGSTDRLTLEKLKDAWTEVINRHDILRTLLLPVSDYSHLDQVVMAPGSLQHLVRINAMDTNPTQGLPHSINITSDSTGTVICEWNVSHALVDAMSIAVIQQEVNEALEGSLGQHQKTPRYADYIQWLSLQDNTETQAYWKKYLEGVEPCLFPKLASSTDKVNPEGTISAIRATWTRDSRLDKLCHTHGITLTNLFHIVWSLLLSAYLGTDKVCFGYTTLGRDVPVDGVEKMVGPLVNVIATTIQLQEDDSILDALLTHQTHLSNSLQHQHYALADVYASLGLVGSQLFNTIVSLQDISHFDANDERPTRVEMLPANDVSEYDVALNIGVDQSSIQVVCSYRTLSLSVEQADALLRTTSHVLDEILRDPKQPLRDLEVISPQCKEQLV | ||||||
Region | 3887-4277 | Adenylation 4 | ||||
Sequence: HSSREAACAWDGIFTFAEVDDLSSRLAARLIRMGVTSGHIIPIYSPKSRWTVIAILGVLKTGAAFTLLETSHPTARLRVICNEIKADIIIAPASHAVPAATLAPILVVLDSITSMSPQESDLLPAVGMPPAAEALAYLIFTSGSTGNPKGVMVTHQNLCSNASIMTTSVNMTSDSRVLHFASHAFDACLWEIFGALFAGACLIIPSESETKEDLAGCIERMVVTWAFLTPSVARILKPEALPSLRNLVLGGEPIAASDLDMWRGHVQVVCAYGPTETAILASTTSPSTFPSDGKDIGVPTGSSLWIVDKQNYNKLAPHGATGELLIEGPNVSQGYLGDPEKTNEAFPVAPRWLSQLRKSPTRVYRTGDLVRFNTSTGTIHFVGRKDNQIKF | ||||||
Domain | 4411-4487 | Carrier 4 | ||||
Sequence: MPFTAAECKMQELVATVLGRDMSEIGMDDSFFYLGGDSIQAMRLVSEGRQQGLTLSLQAIFDAPRLGDLAYRTANLV | ||||||
Region | 4524-4837 | Condensation 5 | ||||
Sequence: EVLPTTSFQRTWLDSQLKSYIVVDIPGPIDLARLRTAIQRVVKAHPILRASFVPYETTTMQVILRTAVVITEADLSTTTVEGICRKDANAPMAPGTPYLRVILATQGEVDRKLIMRLSHAQYDGISLSLLMNDLSHAYASESRPLPSSHLPAFNDYITYQQTQGADPTATTFWHRLLKDVPITYLDLQPAETPTSNGSLITRTRDINIAAFPSLPNGITTATAVKAAWSLVLAQKTGSLAVIFGQVVHGRGIALTGVEGIVGPCANITPVVARLGPQTTRMELMQTLQDQHRSAMPYETAGRKELQTIVQHQNN |
Domain
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for L- to D- amino acid conversion) are present within the NRP synthetase. MlfA has the following architecture: A-T-C-A-T-C-A-T-C-C-A-T-C, with the functions of the five condensation domains during malformin biosynthesis being DL-joining (epimerizing subtype), LL-joining, epimerization, DL-joining and cyclizing domain, respectively.
Sequence similarities
Belongs to the NRP synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length4,870
- Mass (Da)535,293
- Last updated2011-12-14 v1
- Checksum9BDDCA217490CA0C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1766-1789 | Polar residues | ||||
Sequence: GQPESSASSTTEEGFTFSTPDDSS | ||||||
Compositional bias | 1829-1852 | Polar residues | ||||
Sequence: GSSSCKTPSVSSSSSSSSSRKKKS |