Soraph_00050 : CDS information

close this sectionLocation

Organism
StrainSo ce26
Entry nameSoraphen
Contig
Start / Stop / Direction12,671 / 10,080 / - [in whole cluster]
12,671 / 10,080 / - [in contig]
Locationcomplement(10080..12671) [in whole cluster]
complement(10080..12671) [in contig]
TypeCDS
Length2,592 bp (863 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative methoxymalonyl-ACP biosynthesis protein
Product (GenBank)putative methoxymalonyl-CoA synthase
Gene
Gene (GenBank)sorC
EC number
Keyword
  • methoxymalonyl-ACP
Note
Note (GenBank)
  • SorC
Reference
ACC
PmId
[12039053] Characterization of the biosynthetic gene cluster for the antifungal polyketide soraphen A from Sorangium cellulosum So ce26. (Gene. , 2002)
[15289572] Heterologous production of the antifungal polyketide antibiotic soraphen A of Sorangium cellulosum So ce26 in Streptomyces lividans. (Microbiology. , 2004)
[17076505] On the biosynthetic origin of methoxymalonyl-acyl carrier protein, the substrate for incorporation of "glycolate" units into ansamitocin and soraphen A. (J Am Chem Soc. , 2006)
comment
[PMID: 12039053](2002)
Soraphen A biosynthetic gene clusterの報告。
SorC(863aa): Proposed methoxymalonyl-CoA synthase(AT-ACP-MT)

Module 3,7で取り込まれるMethoxymalonyl-CoAを合成する段階。
本ORFSorCのACPドメインを足場として反応が行われる。

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[PMID: 15289572](2004)
sorC破壊株はsoraphen A非産生。

S. lividansでのsor genes異種性発現。
SorABRCDFE株 + cinnamate
SorABRCDFE株 + badA(benzoate-CoA ligase) + benzoate or cinnamate
の組み合わせでSoraphen A産生。
SorABRCDFE株で発現されているのは、the sorA, and the sorB4M, sorRCDFE operons.

SorFは、glyceryl-ACP → hydroxymalonyl-ACPの酸化の際に基質を繋ぎ止めるtype II ACPをコードすると考えられるが、SorFの他にもこの酸化に関与するgenesをひとつの遺伝子でコードするSorCのACP domainが存在する。

---
[PMID: 17076505](2006)
ラベルした基質を用いた実験に基づき、1,3-bisphospho-D-glycerateからmehoxymalonyl-ACPが合成されると結論付けている。
D-[1,2-(13)C2]Glycerateは、ansamitocin P-3生合成は取り込まれないがsoraphen Aには取り込まれる。

sorCは、AT, ACP, MT domainを持つmultifunctional proteinをコードする。

1,3-bisphospho-D-glycetateは、SorC-AT domainの作用でSorC-ACP domainに移される。その結果できた3-phosphoglyceryl-ACPのphosphate ester基の切断はHAD superfamilyのIIIC subgroup(interpro IPR010033)のメンバーに割り当てが考えられているが、SorCはこのメンバーではなく、sor clusterは他に候補を含まないので不明である。

MT domainが同じSorCに含まれていることから、引き続き2-O-methyl-D-glyceryl-ACPへの変換を触媒すると提唱されている。

close this sectionSequence

selected fasta
>putative methoxymalonyl-ACP biosynthesis protein [putative methoxymalonyl-CoA synthase]
MTTALHETNGSPQPNSLQISEPLRLALVAEGSSAELTASMDGLTRTLAAAPGSDVVIRVQ
TPGARPASHRGTLLLDAATKTVVARETAAGAMTPPAVAFLLPGLGDHYLGMARDLYNALP
IFREQVDRCAALLTPELGVDIRTVMHAKARASAAAPGAELDLRRMLGRRGEGPSEEERRL
NQARHAQPALFVVEYALAEQWRAWGVLPDVMLGYSLGEYVAACLAGVLSLEDSLALVARR
AELIESLPAGAMLAVMLSEEELTPQLGAHLSVSAVNGPDFCVVAGPVEEVQRLEARLLDR
RVTLRRVQSSHAFHSRMMEPIAERVTRIVAGFTRRPPRTPYVSNVTGALITAAEATDPAY
WAIHLCRPVRFADGLRALGSEVLLEVGPGQTLSSLATLARKGAGAPSSGGSSTPARTIVA
SMRHAYESESDVSVLLKAVGRLWLSGAAIEGEQPATSAEPAAPADAEAGRGSMAPVVEEI
SPPAEPEAPLTDTEREVAALWQTLLRCEPPTRDANFFRLGGNSLLATRLIDRVSRSLRVK
LPLRRVYQTSTLADMAAAIDGLRGAGARPGAATQGRAAPVTTSAPTAAARPAAAAPDAPR
APLFRLPNGLSVAHQNEAETRHFYDDIFAHRSYVKHGIRIRDGACVLDVGGNIGLFTLFA
HTEAKDVRVFTFEPAPPLFEILSRNVALHGVRATLFNLGLSDRERDAPFTFYPRSAGMSS
FYPDEAEERHNLKAIMDNQRRGGAAEVAQMDGYTEELLDVRFEAVTFTAKLRRLSDVLRE
QRIERVDLMKIDVQKCELEVIEGIDDADWPKFSQIVLEAHDADGRVAKLSSLFERHGFKV
IAEQDELYVGTNIRNIYALREGV
selected fasta
>putative methoxymalonyl-ACP biosynthesis protein [putative methoxymalonyl-CoA synthase]
ATGACTACTGCTCTCCACGAGACGAACGGTTCACCCCAGCCAAACAGCCTGCAAATAAGC
GAGCCTCTCCGGCTCGCGTTGGTTGCTGAAGGGAGCTCGGCTGAGCTCACCGCGAGCATG
GATGGGCTCACGCGCACGCTTGCCGCTGCGCCTGGCTCCGACGTGGTGATCCGGGTCCAA
ACCCCGGGGGCGAGGCCCGCGTCGCATCGCGGGACGCTGCTGCTCGACGCCGCCACGAAG
ACGGTCGTGGCGCGTGAAACCGCGGCGGGGGCAATGACGCCCCCGGCCGTGGCGTTCCTC
CTGCCCGGCCTCGGGGATCATTACCTCGGGATGGCGCGTGATCTTTACAATGCGCTGCCG
ATCTTTCGCGAACAGGTCGATCGCTGCGCCGCGCTCCTCACCCCCGAGCTCGGCGTCGAC
ATCCGCACGGTGATGCACGCGAAGGCGCGCGCGAGCGCTGCGGCGCCGGGCGCCGAGCTC
GACCTGCGGCGCATGCTCGGGCGCAGGGGCGAAGGGCCGAGCGAGGAGGAGCGCCGGCTC
AACCAGGCGCGGCACGCGCAGCCGGCCCTCTTCGTCGTCGAGTACGCCTTAGCGGAGCAA
TGGCGAGCCTGGGGCGTGCTCCCCGACGTCATGCTCGGCTACAGCCTGGGGGAGTACGTG
GCCGCCTGCCTCGCCGGCGTGCTCTCGCTCGAGGACTCACTCGCGCTCGTCGCCCGTCGT
GCGGAGCTGATCGAGTCGCTCCCGGCAGGGGCGATGCTCGCCGTCATGCTCTCGGAGGAG
GAGCTCACTCCGCAGCTCGGCGCGCACCTCTCCGTGTCCGCGGTCAACGGCCCCGATTTC
TGCGTCGTCGCCGGTCCGGTCGAGGAGGTGCAGCGCCTCGAGGCGCGGCTCCTGGACCGC
CGCGTCACCCTCCGGCGCGTCCAGTCGTCACATGCGTTCCACTCCAGGATGATGGAGCCC
ATCGCGGAGCGCGTGACGCGCATCGTGGCGGGCTTCACCCGGCGACCCCCGCGGACACCC
TACGTGTCGAACGTCACCGGCGCGCTGATCACCGCCGCCGAGGCGACCGATCCGGCGTAC
TGGGCGATCCACCTCTGCCGGCCCGTACGGTTCGCGGACGGGCTCCGCGCGCTCGGCAGT
GAGGTCCTCCTGGAGGTCGGACCCGGGCAGACGTTGAGCAGCCTCGCGACGCTCGCCCGG
AAGGGCGCCGGCGCGCCGTCGAGCGGCGGATCATCGACGCCGGCGCGGACGATCGTCGCC
TCGATGCGGCACGCGTACGAGTCGGAGTCGGACGTATCCGTCCTTCTGAAGGCCGTGGGC
CGCCTGTGGCTGAGCGGGGCCGCCATCGAGGGGGAGCAGCCGGCGACCTCCGCGGAGCCG
GCGGCGCCGGCGGACGCCGAGGCCGGCCGCGGCTCTATGGCGCCGGTGGTCGAAGAGATC
TCGCCGCCCGCGGAGCCCGAGGCGCCATTGACGGACACGGAGCGCGAGGTCGCCGCCCTC
TGGCAGACCCTCCTGCGGTGCGAGCCGCCGACGCGCGACGCCAACTTCTTCCGGCTCGGG
GGCAACTCGCTCCTCGCGACGCGCCTCATCGATCGGGTGTCCAGGTCGCTGCGCGTGAAG
CTGCCGCTCCGGCGCGTCTACCAAACATCAACGCTGGCGGACATGGCGGCGGCGATCGAC
GGCTTGCGAGGCGCCGGCGCTCGCCCCGGCGCGGCCACGCAAGGCCGCGCCGCGCCGGTC
ACGACCAGCGCTCCTACCGCCGCGGCGCGCCCCGCGGCGGCGGCGCCGGACGCGCCCCGG
GCGCCGCTCTTCCGCCTGCCGAACGGCCTCTCCGTCGCTCATCAGAACGAGGCCGAGACG
CGGCACTTCTACGATGACATCTTCGCGCACCGCTCGTACGTGAAGCACGGCATTCGCATT
CGCGACGGGGCGTGCGTCCTCGACGTGGGCGGCAACATCGGCCTCTTCACGCTGTTCGCC
CACACCGAGGCGAAGGACGTCCGCGTCTTCACCTTCGAGCCGGCGCCTCCGCTCTTCGAG
ATCCTGAGCCGCAACGTCGCGCTGCACGGCGTCCGGGCGACCCTGTTCAATCTCGGCCTG
TCGGATCGCGAGCGCGACGCGCCGTTCACCTTCTATCCGCGGAGCGCCGGCATGTCCTCG
TTCTACCCGGACGAGGCGGAGGAGCGGCACAACCTCAAGGCGATCATGGACAACCAGCGC
CGGGGCGGCGCCGCAGAGGTCGCTCAGATGGACGGGTACACGGAGGAGCTGCTCGACGTC
CGGTTCGAGGCCGTCACCTTCACGGCCAAGCTCCGGCGCCTGAGCGACGTCCTCCGCGAG
CAGCGCATCGAGCGGGTCGATCTCATGAAGATCGACGTTCAGAAGTGCGAGCTCGAGGTC
ATCGAGGGGATCGACGACGCCGACTGGCCCAAGTTCTCGCAGATCGTGCTCGAGGCGCAC
GACGCCGACGGTCGCGTCGCGAAGCTCTCGTCCTTGTTCGAGCGCCACGGCTTCAAGGTC
ATCGCCGAGCAGGACGAGCTCTACGTCGGGACGAACATCCGCAACATCTACGCCCTTCGA
GAGGGAGTTTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001227 Acyl transferase domain (Domain)
 [92-247]  1.99999999999999e-64 G3DSA:3.40.366.10 [311-399]  1.99999999999999e-64 G3DSA:3.40.366.10
G3DSA:3.40.366.10   Ac_transferase_reg
IPR006162 Phosphopantetheine attachment site (PTM)
 [518-533]  PS00012
PS00012   PHOSPHOPANTETHEINE
IPR006342 Methyltransferase FkbM (Domain)
 [648-840]  1.2e-18 PF05050
PF05050   Methyltransf_21
 [646-820]  3.90000000000001e-29 TIGR01444
TIGR01444   FkbM_fam
IPR009081 Acyl carrier protein-like (Domain)
 [486-561]  4.00000300869883e-17 SSF47336
SSF47336   ACP_like
 [496-559]  4.5e-11 PF00550
PF00550   PP-binding
 [493-560]  PS50075
PS50075   ACP_DOMAIN
 [484-563]  7.79999999999999e-24 G3DSA:1.10.1200.10
G3DSA:1.10.1200.10   ACP_like
IPR014043 Acyl transferase (Domain)
 [99-392]  5.10000000000004e-51 PF00698
PF00698   Acyl_transf_1
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase (Domain)
 [96-418]  9.19998414420354e-57 SSF52151
SSF52151   Acyl_Trfase/lysoPlipase
IPR016036 Malonyl-CoA ACP transacylase, ACP-binding (Domain)
 [248-310]  3.29999802154459e-11 SSF55048
SSF55048   Malonyl_transacylase_ACP-bd
IPR020801 Polyketide synthase, acyl transferase domain (Domain)
 [100-426]  1.90000694315261e-92 SM00827
SM00827   PKS_AT
SignalP No significant hit
TMHMM No significant hit
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