BGC0000149: spirangien O biosynthetic gene cluster from Sorangium cellulosum
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Location: 1,580 - 90,501 nt. (total: 88,922 nt).
This entry is originally from NCBI GenBank AM407731.1.

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core biosynthetic genes
additional biosynthetic genes
transport-related genes
regulatory genes
other genes
resistance
TTA codons
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Gene details
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General
Compounds
Genes
Polyketide
History
NRPS/PKS domains
KnownClusterBlast
General information about the BGC
MIBiG accession BGC0000149
Short description spirangien O biosynthetic gene cluster from Sorangium cellulosum
Status Minimal annotation: no
A minimal annotation only contains information on the BGC loci and one or more linked chemical product(s)

Completeness: complete
Whether the loci encodes everything needed for the pathway producing the compound(s)
Biosynthetic class(es)
  • Polyketide (Other)
Loci NCBI GenBank: AM407731.1
Compounds
  • spirangien O
Species Sorangium cellulosum [taxonomy]
References
Chemical products information
spirangien O
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C41H66O9
Chemical database entries
NPAtlas
List of genes involved in compound(s) production
Identifiers Position Product Functions Evidence Extra
  • CAL58678.1
  • spiA
 1581 - 2372 (-) type II thioesterase
  • Unknown
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  • CAL58679.1
  • spiB
 2442 - 3404 (-) O-methyltransferase
  • Tailoring (Methylation)
Sequence-based prediction
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  • CAL58680.1
  • spiC
 4103 - 5536 (+) cytochrome P450
  • Tailoring (Oxidation)
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  • CAL58681.1
  • spiD
 5550 - 19151 (+) polyketide synthase
  • Scaffold biosynthesis
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  • CAL58682.1
  • spiE
 19148 - 29428 (+) polyketide synthase
  • Scaffold biosynthesis
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  • CAL58683.1
  • spiF
 29434 - 34386 (+) polyketide synthase
  • Scaffold biosynthesis
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  • CAL58684.1
  • spiG
 34751 - 50746 (+) polyketide synthase
  • Scaffold biosynthesis
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  • CAL58685.1
  • spiH
 50766 - 65783 (+) polyketide synthase
  • Scaffold biosynthesis
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  • CAL58686.1
  • spiI
 65780 - 76321 (+) polyketide synthase
  • Scaffold biosynthesis
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  • CAL58687.1
  • spiJ
 76314 - 87053 (+) polyketide synthase
  • Scaffold biosynthesis
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  • CAL58688.1
  • spiK
 87133 - 87924 (+) O-methyltransferase
  • Tailoring (Methylation)
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  • CAL58689.1
  • spiL
 88037 - 89407 (+) cytochrome P450 dependent monooxygenase
  • Tailoring (Monooxygenation)
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  • CAL58690.1
  • spiZ
 89490 - 90128 (-) transcription factor
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Polyketide-specific information
Subclass Other
Starter unit Acetyl-CoA
Cyclic? yes
Release type
  • Hydrolysis
Polyketide-synthases
Genes Properties Modules
spiH
+
spiE
+
spiJ
+
spiI
+
spiG
+
spiD
+
spiF 		Synthase subclass: Modular type I
Module 1
Specificity: Methylmalonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiD
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Dehydratase, Enoylreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 2
Specificity: Methylmalonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiD
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Dehydratase, Enoylreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 3
Specificity: Methylmalonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiE
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: D-OH
Module 4
Specificity: Methylmalonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiE
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Dehydratase, Thiolation (ACP/PCP)
KR-domain stereochemistry: D-OH
Module 5
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiF
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: D-OH
Module 6
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiF
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 7
Specificity: Methylmalonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiG
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Dehydratase, Enoylreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 8
Specificity: Methylmalonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiG
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: D-OH
Module 9
Specificity: Methylmalonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiH
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 10
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiH
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: D-OH
Module 11
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiH
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Dehydratase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 12
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiI
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 13
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiI
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Dehydratase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Module 14
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiJ
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Dehydratase, Thiolation (ACP/PCP)
KR-domain stereochemistry: D-OH
Module 15
Specificity: Malonyl-CoA
Evidence for specificity: Structure-based inference
Genes: spiJ
Core domains: Ketosynthase, Acyltransferase, Ketoreductase, Thiolation (ACP/PCP)
KR-domain stereochemistry: L-OH
Annotation changelog
MIBiG version Submitter Notes
1.0
  • Hidden contributor (ID: 7SR74ARK6JXRBGJRGO2LUHE7, no GDPR consent given).
  • Submitted
2.0
  • Hidden contributor (ID: AAAAAAAAAAAAAAAAAAAAAAAA, no GDPR consent given).
  • Migrated from v1.4
  • Updated compound(s) information (NPAtlas curation)
3.0
  • Hidden contributor (ID: AAAAAAAAAAAAAAAAAAAAAAAA, no GDPR consent given).
  • Remove leading/trailing whitespace in gene identifiers
  • Removed gene annotations, including 'extra' genes, which duplicated NCBI annotations
  • Updated bioactivity data
3.1
  • Hidden contributor (ID: AAAAAAAAAAAAAAAAAAAAAAAA, no GDPR consent given).
  • Update chemical activity to schema version 2.11
Detailed domain annotation
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