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CDS information : Polk_00220


close this sectionLocation

Organism
StrainTü6028
Entry namePolyketomycin
Contig
Start / Stop / Direction28,755 / 30,494 / + [in whole cluster]
28,755 / 30,494 / + [in contig]
Location28755..30494 [in whole cluster]
28755..30494 [in contig]
TypeCDS
Length1,740 bp (579 aa)
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close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative acetyl-CoA carboxylase carboxyltransferase subunit
Product (GenBank)PokAC1
Gene
Gene (GenBank)pokAC1
EC number6.4.1.2
Keyword
Note
Note (GenBank)
  • putative acetyl-CoA carboxylase carboxyl transferase subunit
Reference
ACC
PmId
[19266534] Organisation of the biosynthetic gene cluster and tailoring enzymes in the biosynthesis of the tetracyclic quinone glycoside antibiotic polyketomycin. (Chembiochem. , 2009)
Related Reference
ACC
P0A9Q5
PmId
[1355086] The dedB (usg) open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase. (J Bacteriol. , 1992)
[1355089] The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. (J Biol Chem. , 1992)
[16460018] The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. (Biochemistry. , 2006)
[19965770] A tale of two functions: enzymatic activity and translational repression by carboxyltransferase. (Nucleic Acids Res. , 2010)
ACC
P0ABD5
PmId
[1355089] The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. (J Biol Chem. , 1992)
[15066985] Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity. (J Biol Chem. , 2004)
[16460018] The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. (Biochemistry. , 2006)
[19965770] A tale of two functions: enzymatic activity and translational repression by carboxyltransferase. (Nucleic Acids Res. , 2010)

close this sectionSequence

selected fasta
>putative acetyl-CoA carboxylase carboxyltransferase subunit [PokAC1]
MSAPAETTTPAAWWLCDHCRRPVYAKRLARSSGVCPECGHHRRLSAPERLDQLLDPGSSQ
ALGVPRTADDVLGFTDTRPYHERLAEARDRTGLDDAAIAVRGRIGGCEVAVVAMEFGFMG
GSLSGGVGELITLTAETALAERRPLVIVCASGGARMQEGLISLMQMAKTSQALLALDEAG
IPTVSVITDPVYGGVAASFATLCDVIVAEPGARMGFAGPRVIERTIGERLPENFQRAEFL
REHGQVDVVAPRQELRATLIRLLRALAPPRDTRAGRPRAEQAEPESTGTALGAPDPGLLT
RPEQVPDLDPWQAVRLARNLERPTALDYIALLVDDFQELHGDRLGGDCPATVGGVGLLDG
RPVMVIGQQKGHTAAALRERNFGMPVPAGYRKAARLMRLAAKVGIPVLTLVDTSGAFPGI
EAERGGQAVAIAENLRLMSGLPVPIVAVIVSEGGSGGALGLAVADRVLALSNAVYSVISP
EGCAAILWRDPGAAPHAARELGLHARELLAQGVVDGVVLEPEGGAQSDHRVAAERLAGAV
RPLLEELTVLTTDQLLAGRRARFRGFGSPAPAGRPAPER
selected fasta
>putative acetyl-CoA carboxylase carboxyltransferase subunit [PokAC1]
ATGAGCGCCCCGGCCGAGACGACCACGCCCGCGGCCTGGTGGCTGTGCGACCACTGCCGA
CGGCCTGTCTACGCCAAGCGGCTCGCCCGGTCCTCCGGTGTGTGCCCGGAGTGCGGCCAC
CACCGGAGACTGTCGGCCCCGGAGCGGCTCGACCAGCTGCTCGACCCGGGGTCGTCCCAA
GCCCTGGGCGTGCCGCGCACCGCCGACGACGTCCTCGGCTTCACGGACACCCGGCCCTAC
CACGAGCGACTCGCCGAGGCGCGCGACCGGACCGGACTCGACGACGCCGCGATCGCCGTC
CGCGGCCGGATCGGCGGTTGCGAAGTGGCGGTCGTCGCCATGGAGTTCGGCTTCATGGGC
GGCAGCCTCAGCGGCGGCGTCGGCGAACTCATCACGCTGACCGCCGAGACGGCCCTGGCC
GAACGGCGCCCGCTGGTCATCGTCTGCGCGTCCGGGGGCGCCCGGATGCAGGAGGGCCTG
ATCTCGCTGATGCAGATGGCGAAGACGAGCCAGGCCCTGCTCGCCCTCGACGAGGCCGGC
ATCCCCACCGTCTCCGTCATCACCGACCCGGTGTACGGCGGAGTGGCCGCCTCGTTCGCC
ACGCTCTGCGACGTGATCGTGGCCGAACCGGGAGCCCGCATGGGGTTCGCGGGACCGCGC
GTCATCGAGCGGACCATCGGCGAGCGGCTCCCGGAGAACTTCCAGCGCGCCGAGTTCCTC
CGCGAGCATGGTCAGGTCGACGTGGTCGCACCGCGCCAGGAACTGCGCGCGACCCTGATC
CGGCTGCTCCGCGCGCTGGCTCCACCGCGGGACACCCGGGCGGGACGTCCTCGGGCGGAA
CAGGCCGAGCCGGAGTCCACCGGCACGGCACTCGGCGCACCGGACCCCGGCCTGCTCACC
CGTCCCGAACAGGTCCCCGACCTCGACCCCTGGCAGGCGGTGCGCCTGGCGAGGAACCTC
GAACGCCCCACCGCGCTCGACTACATCGCCCTGCTCGTCGACGACTTCCAGGAACTGCAC
GGTGACCGGCTCGGCGGCGACTGCCCGGCCACCGTCGGAGGAGTCGGCCTCCTCGACGGC
CGGCCCGTGATGGTGATCGGCCAGCAGAAAGGACACACCGCGGCGGCGCTGCGAGAACGG
AACTTCGGCATGCCGGTGCCCGCCGGCTACCGCAAGGCCGCCCGGCTGATGCGCCTGGCC
GCGAAGGTGGGCATCCCGGTGCTCACCCTCGTCGACACCAGCGGTGCCTTCCCCGGCATC
GAGGCGGAGCGCGGGGGCCAGGCCGTGGCCATCGCGGAGAACCTGCGGCTGATGTCCGGG
CTGCCCGTGCCGATCGTTGCTGTGATCGTCTCGGAGGGCGGCAGCGGCGGCGCCCTGGGA
CTCGCCGTCGCCGACCGGGTGCTCGCGCTCAGCAACGCCGTCTACTCGGTGATCAGCCCG
GAGGGATGTGCCGCGATCCTGTGGCGCGATCCCGGGGCGGCACCGCATGCCGCTCGTGAA
CTCGGTCTGCACGCACGGGAGTTGCTTGCACAGGGGGTGGTCGATGGAGTCGTCCTCGAA
CCCGAGGGCGGCGCGCAGAGCGATCACCGCGTCGCGGCGGAGCGCCTCGCCGGCGCCGTA
CGGCCGCTGCTGGAGGAACTGACAGTGCTGACCACCGATCAACTGCTGGCCGGACGACGG
GCCCGCTTCCGCGGCTTCGGCAGCCCGGCACCGGCCGGCCGCCCCGCGCCGGAAAGGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR000022 Carboxyl transferase (Domain)
 [79-503]  1.2e-39 PF01039
PF01039   Carboxyl_trans
IPR000438 Acetyl-CoA carboxylase carboxyl transferase, beta subunit (Family)
 [4-266]  8.90000000000015e-96 TIGR00515
TIGR00515   AccD
IPR001095 Acetyl-CoA carboxylase, alpha subunit (Family)
 [306-568]  5.09999999999992e-96 TIGR00513
TIGR00513   AccA
 [341-352]  1.20000117458134e-29 PR01069 [366-384]  1.20000117458134e-29 PR01069 [387-403]  1.20000117458134e-29 PR01069 [406-419]  1.20000117458134e-29 PR01069 [422-435]  1.20000117458134e-29 PR01069 [450-459]  1.20000117458134e-29 PR01069
PR01069   ACCCTRFRASEA
IPR011762 Acetyl-coenzyme A carboxyltransferase, N-terminal (Domain)
 [33-245]  PS50980
PS50980   COA_CT_NTER
IPR011763 Acetyl-coenzyme A carboxyltransferase, C-terminal (Domain)
 [244-556]  PS50989
PS50989   COA_CT_CTER
SignalP
 [1-46]  0.105 Signal
Bacteria, Gram-negative   
 [1-25]  0.229 Signal
Eukaryota   
 [1-29]  0.321 Signal
Bacteria, Gram-positive   
TMHMM No significant hit