Sch475_00510 : CDS information

Location

Organism	Streptomyces sp.
Strain	SCC-2136
Entry name	Sch 47554
Contig	AJ628018
Start / Stop / Direction	67,521 / 69,065 / + [in whole cluster] 67,521 / 69,065 / + [in contig]
Location	67521..69065 [in whole cluster] 67521..69065 [in contig]
Type	CDS
Length	1,545 bp (514 aa)

Annotation

Category	5.1 general function
Product	putative carboxylic acid--CoA ligase putative acyl-CoA synthetase
Product (GenBank)	feruloyl-CoA synthetase
Gene
Gene (GenBank)	schA30
EC number	6.2.1.-
Keyword
Note
Note (GenBank)
Reference	ACC Q2HR07 PmId [17085966] Angucyclines Sch 47554 and Sch 47555 from Streptomyces sp. SCC-2136: cloning, sequencing, and characterization. (Mol Cells. , 2006) comment angucyclines Sch 47554 and Sch 47555の生合成に関連したentire gene clusterのクローニング、シークエンス、配列解析からの特徴づけ。 schA30はtableにも本文にも記載なし。同定された55ORFsのうち、tableにあるのは50.
Related Reference	ACC Q9EY88 PmId [11152072] Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin. (Appl Microbiol Biotechnol. , 2000) comment Blast 5th, id61%, 1e-172 Amycolatopsis sp. HR167_fcs Feruloyl-CoA synthetase Amycolatopsis sp. strain HR167からech (encoding enoyl-CoA hydratase/aldolase), fcs (encoding an unusual feruloyl-CoA synthetase)を含む4 kb断片をクローニングしてシークエンス。この断片をE. coliに導入するとferulic acid → vanillinへ変換できるようになり、feruloyl-CoA synthetase活性、enoyl-CoA hydratase/aldolase活性が検出された。

Sequence

>putative carboxylic acid--CoA ligase [feruloyl-CoA synthetase]
MKDRGTDMRNEGLGSWPARRARKTPHRTALIHGDTTVTYAGLYERTTRLAHALRDSGVRR
GDRIAYLGPNHPSYLETLFAAGTLGAVFVPLNTRLAGPELAYQLTDSGAKALVYGPTFGG
LVAGLPGNSDVRTYVEVGAEYDQLLDMASDEAIDEPVIPDDTCIIMYTSGTTGRPKGAML
THGNLTWNAVNVLVDQDVITDERALVSAPLFHTAGLNMLTLPVLLKGGTCVLVEAFDPAA
TFDLIERHRITFMFGVPTMFEHVARHPRWADADLSSLRMLSCGGSPVPTPLIAAYQERGL
TFLQGYGMTEASPGVLFLDAEHAVTKAGSAGVPHFFSDVRVVRPDLAPADIGETGEVVVR
GPHVMPGYWGLPDETAAVFHDGWFRSGDAARIDEDGYVTIVDRLKDMIISGGENIYPAEI
EDQLLAHPDIVECAVIGVPDEKWGEVPRAVVVPREDVALDPDEVLASLAGRLAKYKIPKS
VVLADELPRTASGKLLKSRVRKRYGTNSQSKEDT

>putative carboxylic acid--CoA ligase [feruloyl-CoA synthetase]
ATGAAGGACAGGGGCACGGACATGCGCAATGAGGGACTGGGGTCGTGGCCCGCACGCCGG
GCCCGCAAGACCCCGCACCGCACCGCCCTGATCCACGGCGACACGACGGTCACCTACGCC
GGGCTGTACGAGCGCACCACCCGCCTCGCACACGCCCTGCGCGACTCCGGGGTGCGCCGC
GGCGACCGGATCGCCTACCTCGGCCCGAACCACCCCTCCTACCTGGAGACGCTGTTCGCC
GCGGGCACCCTCGGGGCGGTCTTCGTACCGCTCAACACCCGCCTCGCCGGACCCGAACTC
GCCTACCAGCTCACGGACTCCGGCGCGAAGGCCCTCGTGTACGGGCCCACGTTCGGCGGC
CTCGTCGCGGGGCTGCCTGGCAACAGCGACGTGCGTACGTACGTCGAAGTGGGCGCCGAA
TACGACCAGTTGCTCGACATGGCCTCCGACGAGGCCATCGACGAACCCGTCATCCCCGAC
GACACCTGCATCATCATGTACACCTCGGGCACGACGGGCCGGCCCAAGGGCGCGATGCTC
ACCCACGGCAATCTGACGTGGAACGCGGTCAACGTCCTGGTCGACCAGGACGTGATCACC
GACGAACGCGCCCTGGTCTCCGCCCCGTTGTTCCACACGGCCGGGCTGAACATGCTGACC
CTGCCGGTCCTCCTCAAGGGCGGTACGTGCGTCCTGGTCGAGGCCTTCGATCCGGCCGCC
ACCTTCGACCTGATCGAGCGGCACCGGATCACCTTCATGTTCGGCGTGCCCACCATGTTC
GAGCACGTGGCCCGCCATCCGCGCTGGGCCGACGCCGACCTGTCCTCCCTGCGGATGCTC
AGCTGCGGCGGCTCACCCGTGCCGACCCCGCTCATCGCCGCCTACCAGGAGCGGGGCCTC
ACCTTCCTCCAGGGCTACGGCATGACGGAGGCCTCGCCCGGCGTGCTCTTCCTGGACGCC
GAGCACGCGGTCACCAAGGCGGGTTCGGCGGGCGTGCCGCACTTCTTCAGCGACGTCCGC
GTCGTACGGCCCGACCTCGCCCCCGCCGACATCGGCGAGACCGGGGAAGTGGTCGTACGC
GGGCCGCATGTCATGCCCGGCTACTGGGGGCTGCCCGACGAGACCGCTGCCGTGTTCCAC
GACGGCTGGTTCCGCAGCGGGGACGCCGCCCGGATCGACGAGGACGGCTACGTCACCATC
GTCGACCGCCTCAAGGACATGATCATCTCGGGCGGCGAGAACATCTACCCCGCCGAGATC
GAGGACCAGCTCCTCGCCCATCCCGACATCGTCGAGTGCGCGGTCATCGGAGTGCCCGAC
GAGAAGTGGGGCGAGGTGCCGCGCGCGGTCGTCGTGCCCCGCGAGGACGTCGCGCTCGAC
CCCGACGAGGTCCTCGCGTCCCTCGCCGGACGCCTCGCCAAGTACAAGATCCCGAAGTCG
GTGGTGCTCGCGGACGAACTGCCGCGCACGGCCTCCGGCAAGCTCCTCAAGTCCCGTGTC
CGCAAGCGGTACGGCACCAACTCCCAGTCGAAGGAAGACACATGA

Feature

BLASTP Database:UniProtKB:2011_09	show BLAST table
InterPro Database:interpro:38.0	IPR000873 AMP-dependent synthetase/ligase (Domain) PF00501 AMP-binding IPR020845 AMP-binding, conserved site (Conserved_site) PS00455 AMP_BINDING IPR025110 Domain of unknown function DUF4009 (Domain) PF13193 DUF4009
SignalP	No significant hit
TMHMM	No significant hit

Sch475_00500 Sch475_00520