Madu_00430 Madu_00430   Madu_00450 Madu_00450

Madu_00440 : CDS information

close this sectionLocation

Organism
StrainATCC 39144
Entry nameMaduropeptin
Contig
Start / Stop / Direction69,911 / 64,077 / - [in whole cluster]
69,911 / 64,077 / - [in contig]
Locationcomplement(64077..69911) [in whole cluster]
complement(64077..69911) [in contig]
TypeCDS
Length5,835 bp (1,944 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.1 PKS
Productpolyketide synthase
Product (GenBank)enediyne polyketide synthase
Gene
Gene (GenBank)mdpE
EC number
Keyword
  • iterative
  • enediyne core
Note
Note (GenBank)
  • enediyne PKS; MadE
Reference
ACC
PmId
[17918933] Characterization of the maduropeptin biosynthetic gene cluster from Actinomadura madurae ATCC 39144 supporting a unifying paradigm for enediyne biosynthesis. (J Am Chem Soc. , 2007)
[12536216] A genomics-guided approach for discovering and expressing cryptic metabolic pathways. (Nat Biotechnol. , 2003)
[25019332] Enediyne polyketide synthases stereoselectively reduce the beta-ketoacyl intermediates to beta-D-hydroxyacyl intermediates in enediyne core biosynthesis. (Org Lett. , 2014)
comment
[PMID:17918933]
Maduropeptin生合成遺伝子クラスターの報告

mdpE: Enediyne PKS

配列解析から4つのドメイン(KS, AT, dehydratase(DH), KR)を検知。enediyne PKS familyでは、中央にACP domain, C末端にphosphopantetheinyltransferase (PPTase) domainを持つことが知られている。

enediyne core産生のために12のORFs(MdpE through MdpE11)がある。
mdpEは最低限10の付加タンパク質(MdpE2 through MdpE11)を含むtailoring enzymesにより修飾されnascent linear polyunsaturated polyketide骨格を形成すると推測される。

C-1027生合成遺伝子sgcE, Neocarzinotatin(NCS)生合成遺伝子ncsEの各mutant株へmdpE/E5/E6/E10を導入すると、それぞれの株でC- 1027, NCSの生産が確認され、mdpEはsgcEやncsEを相補出来る事を示した。cloned mdpE enediyne PKS geneはC-1027のsgcE or NCSのncsEをcross-complement出来ると示した。

---
[PMID:12536216]
warhead cassette(UNBL-UNBV-UNBU-PKSE-TEBC)はactinomyceteにおいて全てのenediyne生合成遺伝子座で保存されているが、機能は未知のままである。enediyne warheadのformation, stabilization, or transport に関与しているのではないかと推測している。
MaduropeptinでもMadu_00430-Madu_00470で保存されている。

---
[PMID: 25019332]
Enediyne Polyketide SynthaseのKR domainについての調査。
Related Reference
ACC
Q8GME1
NITE
C1027_00520
PmId
[12183628] Biosynthesis of the enediyne antitumor antibiotic C-1027. (Science. , 2002)
[12536216] A genomics-guided approach for discovering and expressing cryptic metabolic pathways. (Nat Biotechnol. , 2003)
[14528002] Rapid PCR amplification of minimal enediyne polyketide synthase cassettes leads to a predictive familial classification model. (Proc Natl Acad Sci U S A. , 2003)
[18223152] A phosphopantetheinylating polyketide synthase producing a linear polyene to initiate enediyne antitumor antibiotic biosynthesis. (Proc Natl Acad Sci U S A. , 2008)
[25019332] Enediyne polyketide synthases stereoselectively reduce the beta-ketoacyl intermediates to beta-D-hydroxyacyl intermediates in enediyne core biosynthesis. (Org Lett. , 2014)
comment
BLAST id66%
Streptomyces globisporus
Polyketide synthase

---
[PMID:18223152]
C-1027生合成遺伝子SgcE geneの機能解析

下記残基をアラニンに置換したmutant株でのC-1027の生産をみたところ、C211, S659, S974, D1827, D1829は必須であるが、S860は必須ではないことが判明。

Ecoでrecombinant SgcEを発現。
S974のセリンに4'-PP cofactorが付着により340massがシフトすることを確認。C211A, S659A, S860Aでは同様のシフトが見られたが、他のmutantはシフトを観察できなかった。同様の実験をNcsEでも行い、同じ結果を得た。したがって、SgcE と NcsEがACPを含んだPKSであり、 C末端ドメインのPPTase(phosphopantetheinyl transferase)の存在も示唆された。

in vitroで4'-PP cofactorの取り込みをモニタリングを行ったところ、SgcE と NcsEはACP-dependentであり、ACP domainはC-terminal PPTase domainによって翻訳後に修飾されることが判明した。

また、精製したSgcE or NcsE solutionは黄色色素が検出され、これはSgcE と SgcE10、NcsE と NcsE10を共発現させることにより検出されることが判明。HPLCでこの産物は、1,3,5,7,9,11,13-pentadecaheptaeneであることがわかった。さらに、同位体炭素の取り込みによりその生合成経路が判明した。

---
[PMID: 25019332]
Enediyne Polyketide SynthaseのKR domainについての調査。
ACC
Q84HI8
NITE
Dynm_00180
PmId
[18328078] The biosynthetic genes encoding for the production of the dynemicin enediyne core in Micromonospora chersina ATCC53710. (FEMS Microbiol Lett. , 2008)
[22589546] Crystal structure of the acyltransferase domain of the iterative polyketide synthase in enediyne biosynthesis. (J Biol Chem. , 2012)
[12536216] A genomics-guided approach for discovering and expressing cryptic metabolic pathways. (Nat Biotechnol. , 2003)
[25019332] Enediyne polyketide synthases stereoselectively reduce the beta-ketoacyl intermediates to beta-D-hydroxyacyl intermediates in enediyne core biosynthesis. (Org Lett. , 2014)
comment
BLAST id43%
Micromonospora chersina
PksE_pksE
DynE8

[PMID: 22589546]
dynemicin生合成遺伝子DynE8の結晶構造解析。
iterative PKSのAT domainでは初めての構造解析報告。

malonyl 特異的 AT domainはacetyl-CoAを認識出来ないとされてきたが、構造解析および生化学解析からDynE8のAT domainは触媒残基Ser651上でmalonyl-CoAまたはacetyl-CoAかのどちらか一方からacyl基をuploadする事が出来ることを示した。DynE8のAT domainは加水分解からアセチル酵素中間体ではなくマロニル化酵素を保護し、ACPへのmalonyl基の移動を促進することを明らかにした。

close this sectionPKS/NRPS Module

A1 acetyl-CoA
malonyl-CoA
KS4..414
AT618..846
ACP934..1028
KR1217..1397
DH1467..1622
PPT1722..1937

close this sectionSequence

selected fasta
>polyketide synthase [enediyne polyketide synthase]
MSSTRLAVVGAACRYPDAASPRELWENALAGRRAFRRLPDERMRLEDYWDADPAAPDRFY
ASKAAVIEGYEFDRVAHRIAGSTYRSTDLTHWLALDVAGRALADAGFPEGRDLPRERTGV
IVGNTLTGEFTRANVLRLRWPYVRRVVAAGLREQEGWDDDRLGAFLDDLEEAYKEPFPAI
DEDSLAGGLSNTIAGRVCNHFDLKGGGYTVDGACSSSLLSVATACRSLLDRDIDVAVAGG
VDLSIDPFEIIGFAKTGALARGEMRLYDRRSNGFWPGEGCGMVVLMREEDARAQGRRIYA
TVAGWGVSSDGRGGITRPEADGYRLALSRAYERAGFGIDTVALFEGHGTGTEVGDTTELT
ALSLARRAAAPQAAPAAVGSVKGMIGHTKAAAGVAGLIKAVMAVRDQVLPPTTGCVDPHP
LLADDDAALRVLRKAEPWPADAPVRAGVTAMGFGGINTHIVLEGADERRRVPFDTRTRAL
AASVQDAELLLVDADSADALRARVAELAEFVPKLAYAQLSDLAAVLQRDLGDRPYRAAVV
ASSPEHAEARLRRVLAVLESGESGLHAPDGGAFLGRVSGRGRIGFLFPGQGSGTGTAGGA
LRRRFAEVEDVYLRAKLPERGDMIATHVAQPRIVTGAMAGLRALSLLGLEAEAAVGHSLG
ELSALHWAGAMDEDALLRVAGVRGRTMAEHSASGTMASARCSAAEAAALVGDRPVVIAGH
NGPAQTVLAGSVEDIEAVGRDAAANGVSWVRLPVSHAFHSPLVAPAADAFARELDGERFG
PVGRRVVSTVTGDGLAAGADVRALLRRQITDPVLFGRAVEVAAKDVDLFVEVGPGRVLTG
LATDITEVPAVAMDTDDESLGGFLTVLAAAYVRGAPVRHEVLFHGRLARPLEIGAEFSFF
ASPCETPPPVRITGTGRRSGRAVPVPDAPADGAAAGGAEADAAEPSIDLLRRLLAERVEL
PPEMVADDSRPLDDLHLSSITVGQVVNQAVRLRGLAVTQAPTNFATATLRELAETLDTLA
ETALPGDLEPGSAVAGAAAWARAFSLDLDTEPLPRPATSTAPSLAAGGAGGWTVHATEGH
PLAGPLRDALERAGAGPGVLVCLPPDCTDDQLEPALDGVRDALAGAPGTRFVLVQDGRGA
AGLARTLRLEAPHLRVTIVHTPPSADAVDRVVAEVAATGEFAEAYYGADGERRVPTLRAM
PVRAARGDPPLDSSDVLLVTGGGKGITAECALAVAADTGARLAVLGRSDPAEDAELAANL
ARMSDAGATVRYARADVADPVRVAAAVAELTESLGPVTGVLHGAGRNVPAGLAGLDMPEI
HRTLAPKTGGLEAVLAAVDPARLKLLVTFGSIIGRAGLRGEGHYATANDRLAQLTREFAG
RHPDCRTLCMEWSVWSGVGMGERLSVVEGLGREGITAITPDQGVEIMRRLVADPDAPSVV
VISGRTGTIDTVRHDAPELPLLRFTGRPLVRYHGVELVAETELNVGSDPYLADHLLDGNL
LFPAVLGMEAMAQAASAATGREEPPAFEGAEFLRPIVVPPEGSTTIRVAATVVDDGAVQV
AIRTADTDFAADHFTARLVYPDGPLPDGPPDQVGDGLPEVPLDPAADLYGGVLFQGARFQ
RLRRYHRAAARHVDADVAAVPAGGWFAGFLPGGMLLADPGMRDALMHGNQVCVPDATLLP
SGVERLRPAGPGVVGDLRYCATERERDGDTYVYDIAVRDATGAVVERWDGLRLQAVRKGD
GRGPWVPPLLGSYLERELEDLLGVHVAVAVEPDPPAEANGGRGDRTAAAAARASGGAVSV
RRRPDGRPELGDGRPVSASHGSGVTLCVVADEPGAGPLGCDVETVAERAPADWAGLLGDA
AALAKVIAAERAERYATAATRVWAAIESVRKAGLPADAPLTLAPAGAGPWVVVASGGLRI
ATLVTALRDEPDPVVLAVLVEGRS
selected fasta
>polyketide synthase [enediyne polyketide synthase]
ATGAGCAGCACCCGCCTCGCCGTCGTCGGTGCGGCATGCCGCTATCCGGACGCGGCGTCC
CCCCGGGAGCTCTGGGAGAACGCCCTCGCCGGGCGCCGCGCGTTCCGCCGGCTGCCCGAC
GAGCGGATGCGGCTGGAGGACTACTGGGACGCCGATCCCGCCGCCCCCGACCGGTTCTAC
GCCAGCAAGGCCGCCGTCATCGAGGGCTACGAGTTCGACCGCGTCGCCCACCGCATCGCC
GGCAGCACCTACCGCTCCACCGACCTCACCCACTGGCTGGCGCTCGACGTCGCCGGACGG
GCGCTGGCCGACGCGGGCTTCCCGGAGGGCCGGGACCTGCCCCGCGAGCGCACGGGGGTG
ATCGTGGGCAACACCCTCACCGGCGAGTTCACCCGCGCCAACGTGCTGCGGCTGCGCTGG
CCGTACGTGCGGCGCGTGGTGGCCGCCGGGCTCCGCGAGCAGGAAGGCTGGGACGACGAC
CGGCTGGGCGCGTTCCTGGACGACCTGGAGGAGGCGTACAAGGAACCGTTCCCGGCCATC
GACGAGGACTCCCTCGCCGGCGGCCTGTCCAACACCATCGCCGGACGCGTCTGCAACCAC
TTCGACCTCAAGGGCGGCGGCTACACGGTCGACGGCGCGTGCTCGTCCTCGCTGCTGTCG
GTGGCCACGGCCTGCCGGTCGCTGCTCGACCGCGACATCGACGTCGCGGTCGCCGGCGGG
GTGGACCTGTCCATCGACCCGTTCGAGATCATCGGGTTCGCCAAGACGGGCGCGCTGGCC
CGCGGCGAGATGCGCCTCTACGACCGCCGCTCCAACGGCTTCTGGCCGGGGGAGGGCTGC
GGCATGGTCGTGCTGATGCGGGAGGAGGACGCCCGCGCCCAGGGGCGGCGGATCTACGCG
ACCGTCGCCGGCTGGGGCGTCTCGTCCGACGGCCGCGGCGGCATCACCCGGCCGGAGGCC
GACGGCTACCGGCTGGCGCTGAGCCGCGCGTACGAGCGCGCGGGCTTCGGCATCGACACC
GTCGCGCTGTTCGAGGGGCACGGCACGGGCACCGAGGTCGGCGACACGACCGAGCTGACG
GCGCTGTCGCTGGCCCGCCGGGCGGCCGCCCCGCAGGCCGCGCCCGCCGCGGTCGGTTCC
GTCAAGGGGATGATCGGGCACACCAAGGCCGCGGCCGGCGTGGCCGGGCTGATCAAGGCC
GTGATGGCGGTCCGCGACCAGGTCCTGCCGCCGACCACCGGCTGCGTCGACCCGCACCCG
CTGCTCGCGGACGACGACGCGGCGCTGCGGGTGCTGCGCAAGGCCGAGCCGTGGCCCGCG
GACGCGCCGGTGCGCGCGGGCGTCACCGCGATGGGCTTCGGCGGCATCAACACCCACATC
GTGCTGGAGGGGGCGGACGAGCGCAGGCGCGTCCCGTTCGACACCCGCACCCGCGCGCTG
GCGGCGTCGGTCCAGGACGCCGAACTGCTGCTGGTCGACGCCGACTCCGCGGACGCGCTG
CGGGCCAGGGTCGCGGAACTGGCCGAGTTCGTGCCGAAACTGGCGTACGCGCAGCTGTCC
GACCTGGCCGCCGTGCTCCAGCGGGACCTGGGCGACCGGCCGTACCGGGCCGCCGTCGTG
GCCTCCTCGCCTGAGCACGCGGAGGCGCGCCTCCGCCGGGTGCTGGCCGTGCTGGAGTCG
GGGGAGAGCGGCCTGCACGCCCCCGACGGCGGCGCGTTCCTCGGCCGGGTGAGCGGGCGG
GGCCGCATCGGCTTCCTGTTCCCCGGCCAGGGCTCGGGCACCGGCACCGCCGGGGGCGCG
CTGCGCCGCCGCTTCGCCGAGGTCGAGGACGTCTACCTGCGGGCGAAGCTGCCCGAGCGG
GGCGACATGATCGCCACGCACGTGGCGCAGCCGCGCATCGTCACCGGCGCGATGGCGGGG
CTGCGGGCGCTGTCCCTGCTGGGCCTGGAGGCGGAGGCCGCGGTCGGCCACAGCCTCGGC
GAGCTGTCCGCGCTGCACTGGGCCGGGGCGATGGACGAGGACGCGCTGCTGCGCGTCGCG
GGGGTGCGCGGCCGGACCATGGCCGAGCACAGCGCGTCCGGGACGATGGCGAGCGCCAGA
TGCTCCGCCGCCGAGGCGGCGGCGCTGGTCGGGGACCGTCCGGTGGTGATCGCCGGTCAC
AACGGCCCCGCCCAGACCGTGCTGGCCGGTTCGGTCGAGGACATCGAGGCGGTGGGCCGC
GACGCGGCGGCGAACGGGGTCAGCTGGGTGCGCCTGCCGGTCTCGCACGCCTTCCACTCC
CCGCTGGTCGCCCCGGCCGCCGACGCCTTCGCCCGCGAGCTCGACGGCGAACGGTTCGGG
CCGGTCGGACGGCGCGTGGTGTCGACCGTCACCGGCGACGGGCTGGCCGCCGGCGCCGAC
GTCCGGGCGCTGCTGCGCCGCCAGATCACCGACCCGGTGCTGTTCGGCCGGGCGGTGGAG
GTCGCGGCCAAGGACGTCGACCTGTTCGTGGAGGTCGGCCCCGGGCGGGTGCTCACCGGG
CTGGCCACCGACATCACCGAGGTGCCCGCCGTCGCGATGGACACCGACGACGAGTCGCTC
GGCGGGTTCCTCACCGTGCTCGCCGCCGCGTACGTGCGCGGCGCGCCCGTCCGGCACGAG
GTCCTGTTCCACGGCAGGCTGGCCCGGCCCCTGGAGATCGGGGCGGAGTTCTCCTTCTTC
GCGAGCCCCTGCGAGACGCCGCCGCCGGTCCGCATCACCGGGACGGGCCGCCGGAGCGGC
CGAGCCGTCCCGGTACCGGACGCGCCTGCGGACGGTGCGGCGGCCGGCGGTGCGGAGGCC
GACGCGGCGGAGCCCTCCATCGACCTGCTGCGGCGGCTGCTGGCCGAGCGCGTGGAGCTG
CCGCCCGAGATGGTGGCCGACGACAGCAGGCCGCTGGACGACCTGCACCTCAGCTCGATC
ACCGTCGGGCAGGTCGTGAACCAGGCGGTGCGGCTGCGGGGCCTGGCGGTGACGCAGGCC
CCGACCAACTTCGCGACCGCCACGCTCCGCGAGCTGGCCGAGACGCTCGACACGCTCGCC
GAGACCGCCCTCCCGGGCGACCTGGAGCCGGGTTCCGCGGTCGCGGGGGCCGCCGCGTGG
GCGCGCGCCTTCTCCCTCGACCTCGACACCGAACCGCTGCCTCGGCCCGCGACGTCCACC
GCCCCCTCCCTCGCGGCGGGCGGCGCCGGCGGGTGGACGGTCCACGCCACCGAAGGGCAT
CCGCTGGCCGGGCCGCTCCGCGACGCGCTGGAGCGGGCGGGCGCCGGTCCCGGCGTCCTG
GTCTGCCTGCCCCCCGACTGCACCGACGACCAGCTGGAACCGGCCCTGGACGGGGTGCGG
GACGCGCTGGCGGGCGCGCCGGGCACCCGGTTCGTCCTGGTCCAGGACGGGCGCGGCGCG
GCCGGGCTCGCCCGGACCCTCCGCCTGGAGGCGCCGCACCTGCGCGTCACGATCGTGCAC
ACCCCGCCGTCCGCGGACGCCGTCGACCGGGTCGTCGCCGAGGTGGCGGCGACCGGGGAG
TTCGCCGAGGCGTACTACGGCGCCGACGGCGAGCGCCGCGTCCCCACGCTGCGGGCGATG
CCCGTGCGCGCGGCGCGCGGCGACCCGCCGCTGGACTCCTCGGACGTGCTGCTGGTGACG
GGCGGCGGCAAGGGGATCACCGCGGAGTGCGCGCTCGCCGTCGCCGCCGACACCGGCGCC
CGGCTCGCCGTGCTCGGCCGCTCCGACCCCGCCGAGGACGCCGAACTGGCGGCGAACCTG
GCGCGGATGTCCGACGCCGGGGCGACCGTCCGCTACGCCCGCGCCGACGTCGCCGACCCG
GTCCGGGTCGCCGCCGCGGTCGCGGAGCTGACCGAGTCGCTCGGCCCGGTCACCGGCGTC
CTGCACGGGGCGGGACGGAACGTTCCGGCCGGTCTCGCCGGGCTGGACATGCCGGAGATC
CACCGCACCCTCGCGCCCAAGACGGGCGGGCTGGAGGCGGTGCTCGCCGCCGTCGACCCC
GCCCGGCTGAAGCTGCTCGTCACGTTCGGCAGCATCATCGGACGCGCCGGGCTGCGCGGG
GAGGGCCACTACGCCACCGCCAACGACCGGCTCGCGCAGCTGACCCGCGAGTTCGCCGGC
CGGCATCCGGACTGCCGGACGCTCTGCATGGAGTGGTCGGTGTGGTCGGGCGTCGGCATG
GGCGAGCGGCTGTCGGTGGTCGAGGGCCTCGGCCGCGAGGGCATCACCGCCATCACCCCC
GACCAGGGCGTCGAGATCATGCGGCGGCTCGTCGCCGATCCGGACGCCCCGTCCGTCGTG
GTGATCAGCGGCCGCACCGGGACGATCGACACCGTGCGCCACGACGCGCCGGAGCTGCCG
CTGTTGCGGTTCACGGGGCGGCCGCTCGTCCGGTACCACGGCGTCGAGCTGGTCGCCGAG
ACCGAGCTCAACGTCGGCTCCGACCCGTACCTGGCCGACCACCTGCTGGACGGGAACCTG
CTGTTCCCGGCCGTCCTCGGGATGGAGGCGATGGCCCAGGCGGCGTCCGCCGCCACCGGC
CGGGAGGAGCCGCCCGCCTTCGAGGGGGCGGAGTTCCTGCGGCCGATCGTCGTCCCGCCC
GAGGGCAGCACCACGATCCGCGTCGCCGCGACCGTCGTCGACGACGGCGCGGTCCAGGTC
GCGATCCGCACGGCCGACACCGACTTCGCCGCCGACCACTTCACCGCGCGGCTGGTGTAC
CCGGACGGACCGCTCCCGGACGGCCCCCCGGACCAGGTCGGCGACGGCCTGCCCGAGGTC
CCGCTCGACCCGGCCGCGGACCTGTACGGCGGCGTCCTGTTCCAGGGCGCCCGCTTCCAG
CGGCTGCGCCGGTACCACCGGGCCGCGGCCCGGCACGTGGACGCCGACGTCGCCGCGGTC
CCCGCCGGGGGCTGGTTCGCCGGGTTCCTGCCCGGCGGCATGCTGCTGGCCGACCCCGGC
ATGCGGGACGCGCTGATGCACGGCAACCAGGTGTGCGTCCCGGACGCGACCCTGCTGCCG
TCCGGCGTCGAACGGCTGCGGCCCGCGGGTCCCGGCGTCGTCGGCGACCTGCGGTACTGC
GCCACCGAACGGGAGCGGGACGGCGACACGTACGTGTACGACATCGCCGTCCGGGACGCG
ACCGGCGCCGTCGTCGAACGGTGGGACGGGCTGCGCCTCCAGGCCGTCCGGAAGGGGGAC
GGGCGCGGCCCGTGGGTGCCCCCGCTGCTCGGCTCGTACCTGGAACGTGAACTGGAGGAC
CTCCTCGGCGTGCACGTCGCGGTCGCCGTGGAGCCCGACCCGCCCGCCGAGGCGAACGGG
GGGCGGGGCGACCGGACGGCGGCGGCCGCCGCCCGCGCGAGCGGCGGCGCGGTGTCCGTG
CGGCGCCGCCCGGACGGCCGTCCCGAACTGGGCGACGGCCGGCCGGTCTCCGCCTCGCAC
GGTTCGGGCGTCACCCTCTGCGTCGTCGCGGACGAGCCCGGCGCGGGCCCGCTCGGCTGC
GACGTCGAGACGGTCGCGGAGCGGGCCCCGGCGGACTGGGCCGGGCTGCTCGGCGACGCC
GCCGCGCTGGCGAAGGTGATCGCCGCGGAGCGCGCCGAGCGGTACGCGACCGCCGCCACC
CGAGTCTGGGCGGCGATCGAGAGCGTCCGCAAGGCGGGCCTGCCGGCCGACGCCCCGCTG
ACCCTCGCGCCGGCCGGCGCCGGGCCGTGGGTGGTCGTGGCCTCCGGCGGCCTGCGGATC
GCGACCCTCGTCACCGCCCTGCGGGACGAGCCGGACCCGGTCGTGCTCGCGGTACTCGTG
GAAGGACGGTCGTAA
[1] KS4..414
[1] AT618..846
[1] acetyl-CoA malonyl-CoA756..760
[1] ACP934..1028
[1] KR1217..1397
[1] DH1467..1622
[1] PPT1722..1937
[1] KS10..1242
[1] AT1852..2538
[1] acetyl-CoA malonyl-CoA2266..2280
[1] ACP2800..3084
[1] KR3649..4191
[1] DH4399..4866
[1] PPT5164..5811

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
[583-687] 6e-36 G3DSA:3.40.366.10 [755-851] 6e-36 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR009081 Acyl carrier protein-like (Domain)
[944-1021] 4.69999810630989e-06 SSF47336
SSF47336   ACP_like
IPR013968 Polyketide synthase, KR (Domain)
[1217-1397] 1.5e-28 PF08659
PF08659   KR
IPR014030 Beta-ketoacyl synthase, N-terminal (Domain)
[4-291] 5.19999999999996e-52 PF00109
PF00109   ketoacyl-synt
IPR014031 Beta-ketoacyl synthase, C-terminal (Domain)
[299-414] 2.1e-30 PF02801
PF02801   Ketoacyl-synt_C
IPR014043 Acyl transferase (Domain)
[618-846] 2.6e-26 PF00698
PF00698   Acyl_transf_1
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
[582-863] 1.10000150671643e-40 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
[692-755] 5.29999657550189e-13 SSF55048
SSF55048   Malonyl_transacylase_ACP-bd
IPR016038 Thiolase-like, subgroup (Domain)
[7-127] 1.09999999999999e-61 G3DSA:3.40.47.10 [161-303] 1.09999999999999e-61 G3DSA:3.40.47.10 [304-468] 5.10000000000004e-45 G3DSA:3.40.47.10
G3DSA:3.40.47.10   Thiolase-like_subgr
IPR016039 Thiolase-like (Domain)
[4-298] 2.60000517657733e-60 SSF53901 [258-471] 1.49999648196323e-53 SSF53901
SSF53901   Thiolase-like
IPR016040 NAD(P)-binding domain (Domain)
[1216-1436] 6.50000000000001e-26 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
SignalP No significant hit
TMHMM No significant hit
Madu_00430 Madu_00430   Madu_00450 Madu_00450
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