Ansam_00330 Ansam_00330   Ansam_00350 Ansam_00350

Ansam_00340 : CDS information

close this sectionLocation

Organism
StrainATCC 31565
Entry nameAnsamitocin
Contig
Start / Stop / Direction73,229 / 76,246 / + [in whole cluster]
9,518 / 6,501 / - [in contig]
Location73229..76246 [in whole cluster]
complement(6501..9518) [in contig]
TypeCDS
Length3,018 bp (1,005 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative bifunctional cytochrome P450/NADPH--cytochrome P450 reductase
Product (GenBank)cytochrome P450
Gene
Gene (GenBank)asm30
EC number
Keyword
Note
Note (GenBank)
  • bifunctional protein
Reference
ACC
PmId
[12060743] The biosynthetic gene cluster of the maytansinoid antitumor agent ansamitocin from Actinosynnema pretiosum. (Proc Natl Acad Sci U S A. , 2002)
[14624546] The post-polyketide synthase modification steps in the biosynthesis of the antitumor agent ansamitocin by Actinosynnema pretiosum. (J Am Chem Soc. , 2003)
comment
[PMID:12060743](2002)
Actinosynnema pretiosum ssp. auranticum ATCC 31565のcosmid libraryから、ansamitocin生合成に必要な2つのgene clustersをクローニング。

<cluster I>
Asm30(1005aa) : Cytochrome P450

配列解析のみ。
ansamitocin形成でC-4/C-5 epoxidationを担うと考えられている。
この反応の代替候補としてAsm11が挙げられている。

---
[PMID:14624546](2003)
Actinosynnema pretiosumのansamitocin生合成gene clusterにある6genesの機能を、遺伝子不活化とmutantの化学分析によって調査。

それらはそれぞれ
halogenase (asm12),
carbamoyltransferase (asm21),
20-O-methyltransferase (asm7),
3-O-acyltransferase (asm19),
epoxidase (asm11),
N-methyltransferase (asm10)
をコードし、ansamitocin形成において6つのPKS後修飾ステップを担う。

insertionによるasm30不活化mutantでもansamitocin P-3を形成できたので、機能不明。
Related Reference
ACC
P14779
PmId
[2544578] ( , )
[1727637] ( , )
comment
Blast 9th, id40%, 0.0
Bacillus megaterium_cyp102A1
Bifunctional P-450/NADPH-P450 reductase
Alternative name: Cytochrome P450(BM-3)

>Including the following 2 domains:
1.Cytochrome P450 102 (EC=1.14.14.1)
2.NADPH--cytochrome P450 reductase (EC=1.6.2.4)

reductase domainはNADP → cytochrome P450への電子伝達に要求される。

---
[PMID:2544578](1989)
P-450BM-3のクローニング、配列解析。
P-450 domainのC末に連結したreductase domainあり。

---
[PMID:1727637](1992)
P450BM-3は、lauric, myristic, and palmitic acids → omega-1, omega-2, and omega-3 hydroxy類似体へ変換し、触媒的に自給自足できるfatty acid hydroxylaseである。多様なfatty acidをmonohydroxylateできるだけでなく、一次代謝産物のいくらかを二次産物、三次産物へとさらに代謝できる。

hydroxylation活性を確認している。

close this sectionSequence

selected fasta
>putative bifunctional cytochrome P450/NADPH--cytochrome P450 reductase [cytochrome P450]
MVATGTRIPGPKPLPLVGNLLDVLTSDLDTDVDFLDRCHREHGGIVALTFAGQRQVFASS
HELVARMCSDPSWGKAVHPALEQVRDFAGDGLFTARGDEPNWGKAHRLLMPAFGPTAMRD
HFPAMLDIAEQMLVRWRRFGPDHRIDVADDMTRLTLDTIALCAFGARFNSFYRDRAHPFV
DAMVRSLVEAGERAERLPGVQPFLVGRNQRYRDDIATMNRIADGIVAARAALPAGERPDD
LLERMLTCADPVTGERLSARNVRYQLATFLIAGHETTSGLLSFAVHRLLAHPEVLRKAKD
AVDGVLGDRVPAFEDLARLDYLGQVLRETLRLHPTAPAFALAPDEPAELGGHAIGAGEPV
LVMLPTLHRDPAVWRDPDVFDPERFAPERMDEIPACAWMPFGHGARACIGRPFALQEATL
VLALVLQRFDLALADPDHRLTIKQTLTLKPDSLVVRARPRADRPGATATVETVVPHQVPA
THRHGTPLHVFYGSNGGSGEGLARTIAGDGAARGWATSVAPLDDAVRALPASGPVVIVSS
SYNGAPPDNAAHFVRWLTQDGPDLSGVDYLVLGCGNLDWSATYQRVPTLIDEAMAAAGAR
RLRERGATDARADFFGDWERWYEPLWPLLSAECGVEVGEIGPRFRVVESDAADGLGDLAS
AVVLENRELVRGPDAGSKRHLELRLPDGTSYRTGDYLSVLPQNHPDLVRRAVARLGTRAE
RVVTVESSAPTGLVPVGRALRVDELLTRCVDLSAPAGAGVVARLAERCPCPPERAELAAT
TGATLLELLERFPSCAVDLALALELLPAPRTRLYSISSAAEEQRAEVALTVSVTGVTSGY
LSRVRPGDRVAVGIASPPESFRPPADNTVPVVLIAAGTGIAPFRGFLRARAALGGEPGPA
LLLFGCRGPELDDLYAEEFAALGDWLEVDRAYSRHPDGEVRHVQHRLWQRRDRVRELVDA
GARVYLCGDATRVGPAVEEVLGRIGPGAGWLDALRAGGRYATDVF
selected fasta
>putative bifunctional cytochrome P450/NADPH--cytochrome P450 reductase [cytochrome P450]
GTGGTCGCCACCGGCACGCGCATCCCCGGCCCCAAGCCCCTGCCCCTGGTGGGGAACCTG
CTCGACGTCCTCACCTCCGACCTGGACACCGACGTCGACTTCCTCGACCGCTGCCACCGC
GAGCACGGCGGCATCGTCGCGCTGACCTTCGCCGGGCAGCGCCAGGTCTTCGCCTCCAGC
CACGAGCTCGTCGCCCGCATGTGCTCCGACCCGAGCTGGGGCAAGGCCGTGCACCCCGCG
CTGGAGCAGGTCCGCGACTTCGCGGGCGACGGGCTGTTCACCGCGCGCGGCGACGAGCCG
AACTGGGGCAAGGCGCACCGGCTGCTCATGCCCGCCTTCGGCCCCACCGCCATGAGGGAC
CACTTCCCGGCCATGCTCGACATCGCCGAGCAGATGCTCGTGCGCTGGCGGCGGTTCGGC
CCCGACCACCGCATCGACGTCGCCGACGACATGACCCGGCTGACCCTGGACACCATCGCG
CTGTGCGCCTTCGGCGCCCGGTTCAACTCCTTCTACCGCGACCGGGCCCACCCCTTCGTC
GACGCGATGGTCCGCAGCCTCGTGGAGGCGGGCGAGCGCGCCGAGCGGCTGCCGGGCGTG
CAGCCGTTCCTGGTGGGCAGGAACCAGCGGTACCGCGACGACATCGCCACCATGAACCGG
ATCGCCGACGGGATCGTCGCCGCGCGCGCCGCACTGCCCGCAGGGGAGCGGCCGGACGAC
CTGCTGGAGCGGATGCTCACCTGCGCCGACCCGGTCACCGGGGAGCGGCTGTCCGCGCGG
AACGTGCGCTACCAGCTGGCCACGTTCCTGATCGCCGGGCACGAGACCACCTCCGGCCTG
CTCTCCTTCGCCGTGCACCGGCTGCTGGCGCACCCCGAGGTGCTGCGCAAGGCCAAGGAC
GCGGTGGACGGGGTCCTGGGCGACCGCGTGCCCGCGTTCGAGGACCTGGCCCGGCTCGAC
TACCTCGGGCAGGTGCTGCGCGAGACCCTGCGGCTGCACCCGACCGCGCCCGCGTTCGCC
CTGGCCCCCGACGAGCCCGCAGAGCTGGGCGGCCACGCGATCGGCGCGGGCGAGCCGGTG
CTGGTGATGCTGCCGACGCTGCACCGGGACCCGGCGGTGTGGCGCGACCCCGACGTGTTC
GACCCGGAGCGGTTCGCGCCCGAGCGGATGGACGAGATCCCGGCCTGCGCGTGGATGCCG
TTCGGGCACGGGGCGCGGGCGTGCATCGGGCGGCCGTTCGCCCTGCAGGAGGCGACCCTC
GTGCTGGCGCTGGTGCTCCAGCGGTTCGACCTCGCGCTCGCCGACCCCGACCACCGGCTG
ACGATCAAGCAGACGTTGACCCTCAAGCCGGACTCGCTGGTGGTCCGCGCCCGGCCGCGC
GCCGACCGCCCTGGCGCCACCGCGACCGTCGAAACCGTTGTGCCGCACCAGGTTCCGGCC
ACCCATCGGCACGGAACCCCGCTGCACGTGTTCTACGGGTCGAACGGCGGCAGCGGCGAG
GGCCTGGCGCGCACGATCGCCGGTGACGGTGCGGCTCGCGGGTGGGCGACTTCCGTCGCG
CCCCTTGACGACGCGGTGCGCGCCCTGCCCGCGTCGGGACCGGTGGTGATCGTCAGCTCC
TCCTACAACGGCGCCCCGCCGGACAACGCGGCCCACTTCGTGCGGTGGCTCACGCAGGAC
GGGCCCGACCTGTCCGGAGTGGACTACCTGGTGCTCGGCTGCGGCAACCTGGACTGGTCG
GCCACCTACCAGCGCGTGCCCACCCTGATCGACGAGGCCATGGCGGCGGCGGGCGCCCGG
CGGCTGCGCGAGCGCGGGGCCACCGACGCCCGCGCGGACTTCTTCGGCGACTGGGAGCGC
TGGTACGAGCCGCTGTGGCCGCTGCTGTCGGCCGAGTGCGGGGTCGAGGTGGGCGAGATC
GGGCCGCGCTTCCGGGTGGTCGAGTCGGACGCGGCCGACGGCCTCGGCGATCTCGCGTCG
GCGGTCGTGCTGGAGAACCGGGAGCTGGTGCGCGGACCGGACGCCGGGTCCAAGCGGCAC
CTGGAGCTGCGGCTGCCCGACGGCACGTCCTACCGCACCGGCGACTACCTGTCCGTGCTG
CCGCAGAACCACCCCGACCTGGTGCGGCGGGCGGTGGCGCGGCTGGGCACGCGCGCGGAG
CGGGTCGTGACGGTCGAGTCGAGCGCGCCCACCGGGCTGGTGCCGGTCGGGCGCGCGCTG
CGCGTGGACGAGCTGCTGACCCGGTGCGTCGACCTGTCCGCGCCCGCGGGCGCCGGGGTC
GTCGCGCGCCTGGCCGAGCGCTGCCCCTGCCCGCCGGAGCGCGCCGAGCTGGCCGCCACG
ACCGGGGCGACGCTGCTGGAGCTGCTGGAGCGCTTCCCCTCGTGCGCGGTCGACCTGGCG
CTGGCCCTGGAACTGCTGCCCGCGCCCAGGACCCGCCTGTACTCGATCAGCTCGGCGGCC
GAGGAGCAGCGGGCCGAGGTGGCGCTCACCGTGTCGGTCACCGGCGTGACCTCCGGCTAC
CTGAGCCGGGTGCGACCCGGCGACCGCGTGGCCGTCGGGATCGCGTCACCGCCGGAGTCG
TTCCGCCCGCCCGCCGACAACACCGTCCCCGTGGTGCTGATCGCCGCGGGCACCGGGATC
GCGCCGTTCCGGGGGTTCCTGCGGGCGCGGGCCGCGCTCGGCGGCGAACCGGGCCCGGCG
CTGCTGCTGTTCGGCTGCCGGGGGCCCGAGCTGGACGACCTGTACGCGGAGGAGTTCGCC
GCGCTCGGCGACTGGCTGGAGGTGGACCGGGCCTACTCGCGCCACCCCGATGGCGAGGTC
CGCCACGTGCAGCACCGGCTGTGGCAGCGGCGGGACCGGGTGCGCGAGCTGGTGGACGCC
GGGGCGCGCGTGTACCTCTGCGGCGACGCGACGCGGGTGGGACCCGCGGTGGAGGAGGTG
CTGGGGCGCATCGGTCCCGGCGCCGGGTGGCTGGACGCGCTCCGCGCCGGGGGGCGGTAC
GCGACGGACGTGTTCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR001128 Cytochrome P450 (Family)
[7-461] 4.59999999999996e-114 G3DSA:1.10.630.10
G3DSA:1.10.630.10   Cyt_P450
[9-451] 1.69999999999998e-79 PF00067
PF00067   p450
[272-289] 1.20000117458134e-10 PR00385 [324-335] 1.20000117458134e-10 PR00385 [399-408] 1.20000117458134e-10 PR00385 [408-419] 1.20000117458134e-10 PR00385
PR00385   P450
[8-460] 1.19999063421924e-112 SSF48264
SSF48264   Cytochrome_P450
IPR001433 Oxidoreductase FAD/NAD(P)-binding (Domain)
[873-969] 3.1e-12 PF00175
PF00175   NAD_binding_1
IPR002401 Cytochrome P450, E-class, group I (Family)
[261-278] 3.39999972437717e-25 PR00463 [281-307] 3.39999972437717e-25 PR00463 [323-341] 3.39999972437717e-25 PR00463 [363-387] 3.39999972437717e-25 PR00463 [398-408] 3.39999972437717e-25 PR00463 [408-431] 3.39999972437717e-25 PR00463
PR00463   EP450I
IPR003097 FAD-binding, type 1 (Domain)
[661-837] 5.40000000000002e-24 PF00667
PF00667   FAD_binding_1
IPR008254 Flavodoxin/nitric oxide synthase (Domain)
[488-626] PS50902
PS50902   FLAVODOXIN_LIKE
[490-612] 6.40000000000001e-14 PF00258
PF00258   Flavodoxin_1
IPR017927 Ferredoxin reductase-type FAD-binding domain (Domain)
[656-864] PS51384
PS51384   FAD_FR
IPR017938 Riboflavin synthase-like beta-barrel (Domain)
[629-858] 4.50001022902825e-49 SSF63380
SSF63380   Riboflavin_synthase_like_b-brl
IPR017972 Cytochrome P450, conserved site (Conserved_site)
[401-410] PS00086
PS00086   CYTOCHROME_P450
IPR023173 NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain-3 (Domain)
[691-807] 3e-20 G3DSA:1.20.990.10
G3DSA:1.20.990.10   NADPH_Cyt_P450_Rdtase_dom3
IPR023206 Bifunctional cytochrome P450/NADPH--cytochrome P450 reductase (Family)
[1-1005] PIRSF000209
PIRSF000209   Bifunctional_P450_P450R
SignalP No significant hit
TMHMM No significant hit
Ansam_00330 Ansam_00330   Ansam_00350 Ansam_00350
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