Sch475_00190 Sch475_00190   Sch475_00210 Sch475_00210

Sch475_00200 : CDS information

close this sectionLocation

Organism
StrainSCC-2136
Entry nameSch 47554
Contig
Start / Stop / Direction29,818 / 28,019 / - [in whole cluster]
29,818 / 28,019 / - [in contig]
Locationcomplement(28019..29818) [in whole cluster]
complement(28019..29818) [in contig]
TypeCDS
Length1,800 bp (599 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative acyl-CoA carboxylase alpha subunit
Product (GenBank)putative Acyl-CoA carboxylase
Gene
Gene (GenBank)schP1
EC number6.4.1.-
Keyword
Note
  • The N-terminal position was modified from original INSDC entry.
Note (GenBank)
Reference
ACC
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。

SchP1(617aa): Acyl-CoA carboxylase

PKS伸長units malonyl-CoA産生の最初のstepで、acetyl-CoAのcarboxylationを触媒すると提唱されている。
Related Reference
ACC
Q9X4K6
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)
comment
Blast 5th, id90%, 0.0
Streptomyces coelicolor_accA2
Putative acyl-CoA carboxylase complex A subunit

accA1, accA2のcloning, 配列決定している。

accA1のmutantはacetyl- or propionyl-CoA carboxylate活性にほとんど変化がみられなかったことから、complexesの形成に関与していないことが示唆された。しかしながら、accA1と非常に相同性が高いaccA2の欠損株を作れなったことから、in vivoでAccA1の代わりにAccA2が機能していた可能性も考えられた。

accA1, accA2, pccBをE.coliで発現させた結果、propionyl-CoA carboxylase beta-subunitがPccBであり、alpha-subunitがaccA1またはaccA2であることを確認(accA1+pccB, accA2+pccBどちらでも活性がみられた)。

accA2 mutantが作製できなかった点については、もしかすると他のcarboxyl transferasesにも関与しているかもしれないと考察している。
ACC
Q9RGQ6
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)
comment
Blast 6th, 90%, 0.0
Streptomyces coelicolor_accA1
Putative acyl-CoA carboxylase complex A subunit

close this sectionSequence

selected fasta
>putative acyl-CoA carboxylase alpha subunit [putative Acyl-CoA carboxylase]
MSAALLGLRQARIRKVLIANRGEIAVRVARACRDAGIASVAVYAEPDRDALHVRAADEAF
ALGGDTPATSYLDMAKVLQAAKDSGADAIHPGYGFLSENADFAQAVLDAQLIWIGPPPQA
IRDLGDKAHIAQRAGAPLVAGTPDPVSGSDEVVAFAEEHGLPIAIKAAFGGGGRGLKVAR
TLEEVPELYDSAVREAVAAFGRGECFVERYLDKPRHVETQCLADSHGNVVVVSTRDCSLQ
RRHQKLVEEAPAPFLSDEQVAELYSSSKAILKEAGYVGAGTVEFLVGTDGTISFLEVNTR
LQVEHPVTEEVAGIDLVREMFRIADGEELGYGDPELRGHSFEFRINGEDPGRGFLPAPGT
VTTFAPPSGPGVRLDAGVESGSVIGPAWDSLLAKLIVTGATREQALQRAARALAEFNVEG
MATAIPFHRAVVKDPALRPELTGSTDPFTVHTRWIETEFVNDIKPFAAPADTEVEDEPGR
ETVVVEVGGKRLEVSLPVSLGMSLARTGLAAGAKPKRRAAKKSGPAASGDTLASPMQGTI
VKVAVEEGQEVKEGDLVVVLEAMKMEQPLNAHRSGTVKALSAEVGASVTSGALICEINS
selected fasta
>putative acyl-CoA carboxylase alpha subunit [putative Acyl-CoA carboxylase]
ATGAGCGCCGCCCTCCTAGGCCTCCGTCAGGCCCGCATACGCAAGGTGTTGATCGCCAAC
CGTGGCGAAATCGCTGTTCGTGTCGCCCGGGCGTGCCGAGACGCCGGTATCGCGAGCGTG
GCGGTGTACGCCGAGCCGGACCGGGACGCACTGCATGTGCGGGCCGCGGACGAGGCGTTC
GCGCTGGGCGGTGACACCCCCGCGACCAGCTACCTCGACATGGCCAAGGTGCTGCAGGCC
GCCAAGGACTCCGGCGCGGACGCCATCCACCCCGGTTACGGCTTCCTTTCCGAGAACGCC
GACTTCGCCCAGGCCGTCCTGGACGCCCAGCTGATCTGGATCGGCCCGCCGCCGCAGGCG
ATTCGCGACCTGGGTGACAAGGCCCATATCGCCCAGCGCGCCGGCGCCCCGCTGGTCGCC
GGCACCCCCGACCCGGTCTCGGGCTCGGACGAGGTCGTCGCCTTCGCGGAGGAGCACGGG
CTGCCGATCGCCATCAAGGCCGCCTTCGGTGGCGGTGGCCGCGGTCTGAAGGTCGCCCGC
ACCCTGGAAGAAGTCCCCGAGCTGTACGACTCGGCCGTCCGCGAGGCGGTGGCCGCCTTC
GGCCGCGGTGAGTGCTTCGTCGAGCGCTACCTCGACAAGCCCCGGCACGTGGAGACCCAG
TGCCTGGCCGACTCCCACGGCAACGTGGTCGTCGTCTCCACCCGCGACTGCTCACTGCAG
CGCCGCCACCAGAAGCTGGTCGAGGAGGCGCCCGCGCCGTTCCTCTCCGACGAGCAGGTC
GCCGAGCTGTACTCCTCTTCGAAGGCCATCCTCAAGGAGGCCGGCTATGTCGGCGCCGGG
ACCGTGGAGTTCCTGGTCGGCACGGACGGCACGATCTCCTTCCTGGAGGTCAACACCCGC
CTGCAGGTGGAGCACCCGGTGACCGAGGAGGTCGCCGGCATCGACCTCGTCCGCGAGATG
TTCCGCATCGCCGACGGTGAGGAGCTCGGCTACGGCGACCCGGAACTGCGCGGCCACTCC
TTCGAGTTCCGCATCAACGGCGAGGACCCGGGCCGCGGCTTCCTGCCCGCTCCCGGCACG
GTGACCACCTTCGCCCCGCCGTCCGGCCCGGGCGTGCGGCTGGACGCGGGCGTGGAGAGC
GGCAGCGTCATCGGCCCGGCCTGGGACTCCCTCCTCGCCAAGCTCATCGTCACCGGCGCC
ACCCGCGAGCAGGCCCTGCAACGGGCCGCCCGCGCGCTCGCCGAGTTCAACGTCGAGGGC
ATGGCGACCGCGATCCCCTTCCACCGCGCGGTCGTCAAGGACCCCGCCCTTCGCCCCGAA
CTGACCGGCTCCACCGACCCGTTCACGGTCCACACCCGCTGGATCGAGACCGAGTTCGTC
AACGACATCAAGCCCTTCGCCGCTCCCGCGGACACCGAGGTCGAAGACGAGCCGGGCCGC
GAGACCGTCGTCGTCGAGGTCGGCGGCAAACGCCTGGAAGTCTCCCTGCCCGTCTCCCTG
GGCATGTCGCTGGCCCGCACCGGCCTCGCAGCCGGCGCCAAGCCCAAACGCCGCGCGGCC
AAGAAGTCCGGCCCCGCCGCCTCCGGCGACACCCTCGCCTCCCCCATGCAGGGCACCATC
GTCAAGGTCGCCGTCGAAGAGGGCCAGGAGGTCAAGGAAGGCGACCTCGTCGTCGTCCTG
GAGGCCATGAAGATGGAGCAGCCCCTCAACGCCCACCGCTCGGGCACCGTCAAGGCCCTG
TCCGCCGAAGTCGGCGCCTCCGTCACCTCCGGCGCCCTCATCTGCGAAATCAATTCCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR000089 Biotin/lipoyl attachment (Domain)
[530-597] 14.116 PS50968
PS50968   BIOTINYL_LIPOYL
[532-597] 1.6e-17 PF00364
PF00364   Biotin_lipoyl
IPR001882 Biotin-binding site (Binding_site)
[554-571] PS00188
PS00188   BIOTIN
IPR005479 Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain (Domain)
[294-301] PS00867
PS00867   CPSASE_2
[128-329] 1.6e-72 PF02786
PF02786   CPSase_L_D2
IPR005481 Carbamoyl-phosphate synthase, large subunit, N-terminal (Domain)
[13-121] 9.6e-41 PF00289
PF00289   CPSase_L_chain
IPR005482 Biotin carboxylase, C-terminal (Domain)
[342-455] 1.7e-33 PF02785
PF02785   Biotin_carb_C
[342-456] 4.5e-52 SM00878
SM00878   Biotin carboxylase C-terminal domain
IPR011053 Single hybrid motif (Domain)
[515-598] 1.6e-20 SSF51230
SSF51230   Single hybrid motif
IPR011054 Rudiment single hybrid motif (Domain)
[337-459] 8.6e-38 SSF51246
SSF51246   Rudiment single hybrid motif
IPR011761 ATP-grasp fold (Domain)
[128-325] 40.207 PS50975
PS50975   ATP_GRASP
IPR011764 Biotin carboxylation domain (Domain)
[12-452] 53.188 PS50979
PS50979   BC
IPR013815 ATP-grasp fold, subdomain 1 (Domain)
[137-210] 4.5e-19 G3DSA:3.30.1490.20
G3DSA:3.30.1490.20   no description
IPR013816 ATP-grasp fold, subdomain 2 (Domain)
[212-457] 1.1e-84 G3DSA:3.30.470.20
G3DSA:3.30.470.20   no description
IPR016185 Pre-ATP-grasp fold (Domain)
[12-124] 1.5e-47 SSF52440
SSF52440   PreATP-grasp domain
[13-134] 1.7e-42 G3DSA:3.40.50.20
G3DSA:3.40.50.20   no description
SignalP
[1-31] 0.353 Signal
Bacteria, Gram-positive   
TMHMM No significant hit
Sch475_00190 Sch475_00190   Sch475_00210 Sch475_00210
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