Heda_00260 : CDS information

Location

Organism	Streptomyces griseoruber
Strain	ATCC 15422
Entry name	Hedamycin
Contig	AY196994
Start / Stop / Direction	36,538 / 37,497 / + [in whole cluster] 36,538 / 37,497 / + [in contig]
Location	36538..37497 [in whole cluster] 36538..37497 [in contig]
Type	CDS
Length	960 bp (319 aa)

Annotation

Category	1.1 PKS
Product	cyclase/dehydratase/polyketide synthase acyl carrier protein subunit
Product (GenBank)	putative bifunctional cyclase dehydratase and ACP fusion
Gene	hedE
Gene (GenBank)
EC number
Keyword	1st ring type II PKS
Note	multifunctional protein
Note (GenBank)	orf7
Reference	ACC Q67G32 PmId [15271354] The hedamycin locus implicates a novel aromatic PKS priming mechanism. (Chem Biol. , 2004) [19942143] In vivo and in vitro analysis of the hedamycin polyketide synthase. (Chem Biol. , 2009) comment [PMID:15271354](2004) hedamycinの生合成gene clusterの報告。 hedE: Cyclase/dehyd. and ACP fusion --- [PMID:19942143](2009) hedE: bifunctional aromatase/acyl carrier protein HedEはACP and aromatase activityの両方を持つbifunctional proteinである。 aromatase domainは、minimal PKSの鎖長特異性を調節しうる。 hed KS-CLF, KRやHedEのACP domainだけを分離してplasmid構築、産物解析している。 ACP domainだけだと、C-9で還元されC7-C12 cyclizationを受けているdodecaketide (C-24) AD211aが検出されないので、ARO domainはC7-C12 cyclizationを担う。 act KS-CLF, KR + hedEは、act KS-CLF, ACP, KR + act AROと同じ産物を産生。よってHedEはact産生におけるACPとAROを代替できる。 hed KS-CLFは他のACPとの組み合わせではpolyketideは検出されず、よって異種性ACPsに対する識別能力が他より高い。ラベリング実験などから、hed KS-CLFはHedU(type I PKS)のACP domainからprimer unitを最初に受け取り、それからさらなる鎖延伸を触媒するためHedEと結合する、と提唱されている。

PKS/NRPS Module

ACP	239..312

Sequence

>cyclase/dehydratase/polyketide synthase acyl carrier protein subunit [putative bifunctional cyclase dehydratase and ACP fusion]
MGGSWTLEERGEGCTVVLDHHYRAVDDDPARLARIARAVEHNSTVELDNLRRAVLRAGQE
PELLFEFADTETVSGPPEEVYAFLYDAAKWPERIPHVAHVEVREDVLGLQHLRMDTRAPD
GSVHTTVSGRVCEPGRRIVYKQTTLPPVLQAHNGEWLVEETGDGAVRVTARHQVILDPEG
IAGLAEPPESLAAARDAVREALGANSRATMARARAFAEANRPRTPRHHTKGNTAMAELTL
DELKRFLLSAAGDDESVELSGDILHVRLVDLGFDSLAVIDTLGRLERHFGVKLPEEATTE
VETPADLLAAVNRQVAEAA

>cyclase/dehydratase/polyketide synthase acyl carrier protein subunit [putative bifunctional cyclase dehydratase and ACP fusion]
ATGGGCGGCTCCTGGACCTTGGAGGAGCGCGGCGAGGGATGCACCGTCGTCCTCGACCAC
CACTACCGCGCCGTCGACGACGACCCGGCGCGCCTGGCCCGCATCGCGCGGGCCGTGGAG
CACAACAGCACCGTGGAGCTGGACAACCTCCGGCGCGCCGTGCTGCGGGCCGGACAGGAG
CCGGAGCTGCTGTTCGAGTTCGCCGACACCGAGACCGTCTCCGGCCCGCCGGAGGAGGTG
TACGCCTTCCTCTACGACGCCGCGAAATGGCCCGAGCGCATCCCGCACGTCGCGCACGTC
GAGGTACGCGAGGACGTGCTCGGACTGCAGCACCTGCGGATGGACACCCGGGCCCCGGAC
GGGTCCGTGCACACGACGGTCTCCGGCCGGGTCTGCGAGCCGGGCCGGCGGATCGTGTAC
AAGCAGACGACACTGCCGCCCGTGCTCCAGGCGCACAACGGCGAGTGGCTCGTCGAGGAG
ACGGGCGACGGTGCCGTCCGTGTGACGGCCCGGCACCAGGTGATCCTCGACCCGGAGGGG
ATCGCCGGTCTCGCCGAGCCGCCCGAGTCGCTCGCCGCCGCGCGGGATGCTGTCCGTGAG
GCGCTCGGCGCCAACAGCAGGGCGACCATGGCGCGGGCCCGCGCCTTCGCCGAGGCGAAC
CGACCCCGTACCCCCCGCCACCACACGAAAGGGAACACCGCCATGGCCGAACTGACCCTC
GACGAGCTCAAGCGCTTCCTGCTGAGCGCGGCCGGAGACGACGAGAGCGTCGAGCTGTCC
GGCGACATCCTCCACGTCCGCCTGGTCGACCTGGGCTTCGACTCGCTCGCCGTGATCGAC
ACCCTGGGCCGGCTGGAGCGCCACTTCGGCGTCAAACTGCCCGAGGAGGCGACCACCGAG
GTGGAGACCCCGGCGGACCTCCTCGCCGCCGTCAACCGCCAGGTCGCCGAGGCCGCCTGA

ACP	239..312

ACP	715..936

Feature

BLASTP Database:UniProtKB:2011_09	show BLAST table
InterPro Database:interpro:38.0	IPR006162 Phosphopantetheine attachment site (PTM) PS00012 PHOSPHOPANTETHEINE IPR009081 Acyl carrier protein-like (Domain) PS50075 ACP_DOMAIN G3DSA:1.10.1200.10 ACP_like SSF47336 ACP_like PF00550 PP-binding IPR019587 Polyketide cyclase/dehydrase (Family) PF10604 Polyketide_cyc2 IPR023393 START-like domain (Domain) G3DSA:3.30.530.20 G3DSA:3.30.530.20
SignalP	Bacteria, Gram-negative
TMHMM	No significant hit

Heda_00250 Heda_00270