Medem_00140 : CDS information

Location

Organism	Streptomyces sp.
Strain	AM-7161
Entry name	Medermycin
Contig	AB103463
Start / Stop / Direction	12,287 / 13,903 / + [in whole cluster] 12,287 / 13,903 / + [in contig]
Location	12287..13903 [in whole cluster] 12287..13903 [in contig]
Type	CDS
Length	1,617 bp (538 aa)

Annotation

Category	5.1 general function
Product	putative acyl-CoA carboxylase beta subunit
Product (GenBank)	decarboxylase
Gene
Gene (GenBank)	med-ORF22
EC number
Keyword
Note
Note (GenBank)	GTG start codon
Reference	ACC Q7WT28 PmId [12855716] Cloning, sequencing and heterologous expression of the medermycin biosynthetic gene cluster of Streptomyces sp. AM-7161: towards comparative analysis of the benzoisochromanequinone gene clusters. (Microbiology. , 2003) comment entire medermycin(med) biosynthetic gene clusterの報告。 Streptomyces coelicolor CH999でmed clusterを発現してmedermycin産生を確認している。 ORF22: Decarboxylase(starter) 配列解析のみ。 acyl-CoA decarboxylase genesに似たJadN, LanPとhomolog.
Related Reference	ACC O86517 PmId [11526020] Role of an essential acyl coenzyme A carboxylase in the primary and secondary metabolism of Streptomyces coelicolor A3(2). (Appl Environ Microbiol. , 2001) [12048195] Kinetic and structural analysis of a new group of Acyl-CoA carboxylases found in Streptomyces coelicolor A3(2). (J Biol Chem. , 2002) comment Blast 10th, id85%, 0.0 Streptomyces coelicolor_SCO5535 Putative carboxyl transferase AccB --- [PMID:11526020](2001) 論文で示されているAL031124は、AL939124で置換されている。このfragmentに含まれるcarboxyl transferaseはこのORFのみ。周りの並びも論文のfigureに一致するので、論文中のAccBがこのentryに相当すると判断した。 propionyl-CoA carboxylase(PCC)のbeta subunit pccBを使って、accBE genesをクローニング。異種性発現でacyl-CoA carboxylase (ACCase)活性を確認。 --- [PMID:12048195](2002) S.coelicolor由来の2つのacyl-CoA carboxylasesを精製されたcomponentで再構成。新しいepsilon subunit(PccE, AccE)があると活性がとても良い。 propionyl-CoA carboxylase(PCC) complex: AccA2 + PccB + PccE acetyl-CoA carboxylase(ACC) complex: AccA2 + AccB + AccE ACCは基質特異性がゆるく、acetyl-, propionyl-, and butyryl-CoAへの特異性定数はほぼ同じ。 PCCはacetyl-CoAを基質として検出できないが、効率的にbutyryl- and propionyl-CoAをcarboxylateし、特にpropionyl-CoAを好んだ。配列解析で、polyketide clustersと関連したcarboxyltransferase AccB homologuesのすぐ下流に、AccE epsilon subunit homologuesが存在するのを見つけている。
Related Reference	ACC Q9X4K7 PmId [10589718] Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). (Microbiology. , 1999) [12048195] Kinetic and structural analysis of a new group of Acyl-CoA carboxylases found in Streptomyces coelicolor A3(2). (J Biol Chem. , 2002) comment Blast 130th, id58%, 1e-165 Streptomyces coelicolor_pccB Propionyl-CoA carboxylase complex B subunit --- [PMID: 10589718](1999) Streptomyces coelicolor A3(2)からaccA1, accA2, pccBをクローニング、シークエンス。 biotin-containing proteins(propionyl-CoA carboxylase alpha subunit): accA1, accA2 propionyl-CoA carboxylase carboxyl transferase subunit: pccB accA1破壊株でacetyl- or propionyl-CoA carboxylase activityに変化なし。 pccB破壊株でpropionyl-CoA carboxylase activity低下。 accA2破壊株は作製できなかったことよりessentialで、生育に必須な他のcarboxyl transferasesと共有されているbiotinylated proteinをコードすることが示唆される。 E.coliでのaccA1+pccB, accA2+pccB 共発現でpropionyl-CoA carboxylase活性確認。 pccBだけでは活性なし。complexで働くことを確認している。 --- [PMID:12048195](2002) S.coelicolor由来の2つのacyl-CoA carboxylasesを精製されたcomponentで再構成。新しいepsilon subunit(PccE, AccE)があると活性がとても良い。 propionyl-CoA carboxylase(PCC) complex: AccA2 + PccB + PccE acetyl-CoA carboxylase(ACC) complex: AccA2 + AccB + AccE ACCは基質特異性がゆるく、acetyl-, propionyl-, and butyryl-CoAへの特異性定数はほぼ同じ。 PCCはacetyl-CoAを基質として検出できないが、効率的にbutyryl- and propionyl-CoAをcarboxylateし、特にpropionyl-CoAを好んだ。配列解析で、polyketide clustersと関連したcarboxyltransferase AccB homologuesのすぐ下流に、AccE epsilon subunit homologuesが存在するのを見つけている。

Sequence

>putative acyl-CoA carboxylase beta subunit [decarboxylase]
MPTTESRPSTTDNPDDRTDRTDRSVSALRDELHVLRERALRGPSERATEAQHAKGKLTAR
ERIELLLDPGSFNEVEQLRRHRAQGFGLEARKPYTDGVITGWGTVEGRTVFVYAHDFRIF
GGALGEAHATKIHKIMDMAIAAGAPLVSLNDGAGARIQEGVSALAGYGGIFQRNTRASGV
IPQISVMLGPCAGGAAYSPALTDFVFMVRETSQMFITGPDVVKAVTGEEITQNGLGGADV
HAETSGVAHFAYDDEETCIAEVRYLLSMLPQNNRENPPAVVPDDSPDRATPALLDLVPAD
AVRSYDVRAVIEELVDDEEHMEVHSGWAANLVCTLARLDGRVVGIVANQPSVMAGVLDID
ASEKGARFVQMCDAFSIPIVTLVDVPGFLPGVGQEHHGVIRRGAKLLYAYCNATVPRISV
ILRKAYGGAYIVMDSQSIGADLTYAWPTNEIAVMGAEGAANVIFRRQIAEAPDPEAERLQ
KIKEYRTELMHPYYAVERGLVDDVIDPSDTRRVLVRGLEMLRAKHAELPSRKHGNPPQ

>putative acyl-CoA carboxylase beta subunit [decarboxylase]
GTGCCGACGACAGAGAGCCGACCATCGACCACCGACAACCCCGACGACAGGACCGACAGG
ACCGACCGCTCCGTCTCCGCTCTCCGTGACGAGCTGCACGTCCTGCGCGAGCGGGCGCTG
CGTGGCCCGAGTGAGCGCGCGACCGAGGCGCAGCACGCGAAGGGCAAGCTGACGGCGCGT
GAGCGCATCGAGCTGCTGCTCGACCCGGGTTCCTTCAACGAGGTCGAGCAGTTGCGCCGG
CACCGCGCCCAGGGCTTCGGCCTGGAGGCGAGGAAGCCGTACACCGACGGTGTGATCACC
GGCTGGGGCACGGTCGAGGGCCGGACGGTCTTCGTGTACGCGCACGACTTCCGGATCTTC
GGCGGTGCGCTGGGCGAGGCCCACGCGACGAAGATCCACAAGATCATGGACATGGCCATC
GCGGCCGGTGCCCCGCTGGTCTCGCTGAACGACGGCGCCGGTGCCCGTATCCAGGAGGGC
GTCTCCGCGCTCGCCGGCTACGGCGGCATCTTCCAGCGCAACACCCGGGCCTCGGGTGTC
ATCCCGCAGATCTCGGTGATGCTCGGCCCGTGCGCCGGCGGCGCGGCCTACAGCCCCGCC
CTCACCGACTTCGTGTTCATGGTCCGTGAGACCTCGCAGATGTTCATCACCGGCCCGGAC
GTCGTCAAGGCGGTCACCGGTGAGGAGATCACCCAGAACGGCCTCGGCGGCGCGGACGTG
CACGCCGAGACCTCGGGCGTCGCGCACTTCGCGTACGACGACGAGGAGACCTGCATCGCC
GAGGTCCGCTACCTCCTGTCGATGCTCCCGCAGAACAACCGCGAGAACCCGCCCGCCGTC
GTACCGGACGACTCCCCGGACCGTGCCACCCCCGCCCTCCTCGACCTGGTGCCCGCAGAC
GCCGTCCGCTCGTACGACGTCCGGGCCGTGATCGAGGAACTCGTCGACGACGAGGAGCAC
ATGGAGGTGCACAGCGGCTGGGCCGCCAACCTGGTGTGCACCCTCGCCCGGCTGGACGGC
CGGGTCGTCGGCATCGTCGCCAACCAGCCCTCCGTGATGGCGGGCGTCCTGGACATCGAC
GCCTCCGAGAAGGGGGCCCGCTTCGTGCAGATGTGCGACGCCTTCAGCATCCCGATCGTC
ACGCTCGTCGACGTACCGGGATTCCTCCCCGGCGTCGGCCAGGAGCACCACGGCGTCATC
AGAAGGGGCGCCAAGCTGCTCTACGCCTACTGCAACGCGACCGTGCCCCGGATCTCCGTG
ATCCTGCGCAAGGCCTACGGCGGCGCCTACATCGTCATGGACTCCCAGTCCATCGGCGCC
GACCTCACCTACGCCTGGCCCACCAACGAGATCGCGGTCATGGGCGCCGAGGGCGCCGCC
AACGTCATCTTCCGCCGGCAGATCGCGGAGGCCCCGGACCCCGAGGCGGAACGCCTGCAG
AAGATCAAGGAGTACAGGACCGAACTGATGCATCCCTACTACGCCGTCGAGCGCGGCCTC
GTCGACGATGTCATCGACCCCTCCGACACACGCCGGGTGCTCGTCCGCGGACTGGAGATG
CTCCGCGCCAAGCACGCCGAACTCCCCTCGCGCAAACACGGAAACCCGCCGCAGTGA

Feature

BLASTP Database:UniProtKB:2011_09	show BLAST table
InterPro Database:interpro:38.0	IPR000022 Carboxyl transferase (Domain) PF01039 Carboxyl_trans IPR011762 Acetyl-coenzyme A carboxyltransferase, N-terminal (Domain) PS50980 COA_CT_NTER IPR011763 Acetyl-coenzyme A carboxyltransferase, C-terminal (Domain) PS50989 COA_CT_CTER
SignalP	No significant hit
TMHMM	No significant hit

Medem_00130 Medem_00150