Sch475_00210 : CDS information

Location

Organism	Streptomyces sp.
Strain	SCC-2136
Entry name	Sch 47554
Contig	AJ628018
Start / Stop / Direction	31,604 / 30,033 / - [in whole cluster] 31,604 / 30,033 / - [in contig]
Location	complement(30033..31604) [in whole cluster] complement(30033..31604) [in contig]
Type	CDS
Length	1,572 bp (523 aa)

Annotation

Category	2.1 modification addition of extender units
Product	putative acyl-CoA carboxylase beta subunit
Product (GenBank)	putative methyl malonyl Co-A decarboxylase
Gene
Gene (GenBank)	schP2
EC number	6.4.1.-
Keyword
Note
Note (GenBank)
Reference	ACC Q2HR49 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。 SchP2(523aa): Methyl malonyl Co-A decarboxylase JadN, LanPに似ており、たぶんmalonyl-CoA decarboxylaseをコードする。
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, id86%, 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, id57%, 1e-168 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 [putative methyl malonyl Co-A decarboxylase]
MTIMEERRPTATHVEELARLKRQVHEGPGERATSAQHARGKLTARERIQLLMDEGTFSEV
EPLRRHRATGFGLEANRPYTDGVITGWGTVHGRTVFVYAHDFRIFGGSLGEAHATKIHKI
MDMAITAGAPLVSLNDGAGARIQEGVSALAGYGGIFQRNTRASGVIPQISVMLGPCAGGA
AYSPALTDFVFMVRETSQMFITGPDVVKAVTGEEITQNGLGGADVHAETSGVAHFAYDDE
ETCIAEVRYLLSMLPQNNRDVPPRVDPDDRADRRTDAVLDLVPVDGNRPYDMTKVIGELV
DDGDYLEVHERWARNIICALARLDGQVVGIVANQPQSMAGVLDIAASEKAARFVQLCDAF
SIPLVTLLDVPGFLPGVDQEHGGVIRHGAKLLYAYCNATVPRISLILRKAYGGAYIVMDS
QSIGADLTYAWPTNEIAVMGAEGAANVVFRRQIAAADDPEAMRARLVKEYKAELMHPYYA
AERGLVDDVIDPAETRTVLIRSLAMLRTKHAELPSRKHGNPPQ

>putative acyl-CoA carboxylase beta subunit [putative methyl malonyl Co-A decarboxylase]
ATGACCATCATGGAGGAGCGGCGGCCGACGGCCACGCACGTCGAGGAGCTGGCCAGGCTC
AAGAGGCAGGTGCACGAGGGTCCCGGCGAACGCGCGACCTCGGCCCAGCACGCCCGCGGC
AAGCTGACAGCCCGTGAACGCATCCAACTCCTCATGGACGAAGGCACGTTCAGCGAGGTG
GAGCCGCTGCGCCGGCACCGGGCGACCGGCTTCGGCCTGGAGGCGAACCGCCCGTACACG
GACGGCGTGATCACCGGCTGGGGCACCGTGCACGGGCGCACGGTCTTCGTGTACGCCCAT
GACTTCCGCATTTTCGGCGGCTCGCTGGGCGAGGCCCACGCCACGAAGATCCACAAGATC
ATGGACATGGCCATCACGGCCGGCGCACCCCTGGTGTCCCTGAACGACGGTGCGGGCGCC
CGCATCCAGGAGGGCGTGTCCGCGCTCGCCGGCTACGGCGGCATCTTCCAGCGCAACACC
CGCGCCTCGGGCGTCATCCCGCAGATCAGCGTGATGCTGGGCCCGTGCGCCGGCGGCGCC
GCGTACTCCCCGGCCCTGACGGACTTCGTGTTCATGGTCCGCGAGACCTCGCAGATGTTC
ATCACAGGACCTGACGTCGTCAAGGCGGTCACCGGCGAGGAGATCACCCAGAACGGCCTG
GGCGGCGCGGACGTCCACGCGGAGACGAGCGGCGTCGCGCACTTCGCGTACGACGACGAG
GAGACCTGCATCGCCGAGGTGCGGTATCTGCTCTCGATGCTGCCGCAGAACAACCGCGAC
GTCCCGCCCCGGGTGGACCCCGACGACCGGGCGGACCGGCGCACCGACGCCGTGCTTGAC
CTGGTCCCCGTGGACGGCAACCGGCCGTACGACATGACGAAGGTGATCGGGGAACTCGTC
GACGACGGGGACTACCTGGAGGTCCACGAGCGCTGGGCCCGCAACATCATCTGCGCACTT
GCCCGGCTCGACGGCCAGGTGGTGGGCATCGTCGCCAACCAGCCGCAGTCCATGGCCGGC
GTCCTCGACATCGCGGCCAGCGAGAAGGCGGCCCGCTTCGTGCAACTGTGCGACGCGTTC
AGCATCCCGCTGGTGACGCTGCTCGACGTGCCGGGCTTTCTGCCGGGCGTGGACCAGGAG
CACGGCGGCGTCATCCGGCACGGCGCGAAACTGCTCTACGCCTACTGCAACGCGACCGTG
CCGCGGATCTCACTGATCCTCAGGAAGGCCTACGGCGGCGCGTACATCGTCATGGACTCG
CAGTCCATCGGCGCCGACCTGACCTACGCCTGGCCGACGAACGAGATCGCGGTGATGGGT
GCGGAAGGCGCCGCCAACGTTGTCTTCCGCAGGCAGATCGCCGCCGCCGACGACCCCGAG
GCGATGCGCGCCAGGCTGGTCAAGGAGTACAAGGCCGAGCTCATGCATCCGTACTACGCG
GCCGAGCGCGGCCTGGTCGACGACGTCATCGACCCCGCCGAGACCCGTACGGTACTCATC
CGCTCCCTGGCGATGCTGCGCACCAAGCACGCGGAACTGCCCTCCCGCAAACACGGCAAC
CCCCCACAGTGA

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

Sch475_00200 Sch475_00220