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CDS information : R1128_00060


close this sectionLocation

Organism
StrainR1128
Entry nameR1128
Contig
Start / Stop / Direction8,901 / 7,165 / - [in whole cluster]
8,901 / 7,165 / - [in contig]
Locationcomplement(7165..8901) [in whole cluster]
complement(7165..8901) [in contig]
TypeCDS
Length1,737 bp (578 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative acetyl-CoA carboxylase carboxyltransferase subunit
Product (GenBank)acetyl carboxylase
Gene
Gene (GenBank)zhuF
EC number6.4.1.2
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[10931852] Cloning, nucleotide sequence, and heterologous expression of the biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor antagonist. Insights into an unusual priming mechanism. (J Biol Chem. , 2000)
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 [acetyl carboxylase]
MTETAIRPTTGVADWVQCGNCRAAVYGKRWARGLRVCPECAKHHPVGARERLDQLLDPGS
AEPIRNDVRTFDVLGFTDTKPYPARLAAARAATGLDEAVVIVTGRIHGQPLVVAAMDFAF
LGGSLGGAVGELITLAAETALAEHLPLLIVSASGGARMQEGAVALMQMAKTSAALGQLDE
AGVLTISLVTDPTYGGVAASFATLCDVIVAEPGARLGFAGRRVIAQTIREELPPEFQTAE
YLLEHGLIDLIVPRRALRDELARLLRAGAKRPKGGDGEPARRGGLDAGASPYVVDPADLA
AHDPSRQVRAARAIDRPTTLDYIALLCEDFVELRGDRISGDCPAIVAGLARFGGRPVAVI
GHQKGHDAQELRRRNFGMPIPSGYRKAARIMRLADKLGLPVVTFVDTPGAYPGAVAEEQG
QAVAIAENLRLMAGLRVPVVTVVTGEGGSGGALALAVANRVLMFENGIYSVISPEGCAAI
LWQDPAAAGRAARALRVTARELLGLGIVDGVLPEPEGGTGADPLRAADALRDAIAAGLAE
LSPLDGHQLVADRWARFRRYGAERTTDAEITAMKGDPT
selected fasta
>putative acetyl-CoA carboxylase carboxyltransferase subunit [acetyl carboxylase]
ATGACCGAAACCGCCATCCGGCCCACGACCGGCGTCGCCGACTGGGTGCAGTGCGGCAAC
TGCCGCGCCGCCGTGTACGGCAAGCGCTGGGCCCGCGGCCTGCGGGTCTGCCCCGAATGC
GCCAAACACCACCCGGTCGGCGCCCGCGAACGCCTCGACCAGCTCCTCGACCCCGGCTCC
GCCGAGCCGATCCGCAACGACGTGCGCACCTTCGACGTGCTCGGCTTCACCGACACCAAG
CCCTACCCCGCGCGGCTCGCCGCCGCGCGTGCCGCCACCGGGCTCGACGAGGCCGTCGTC
ATCGTGACCGGCCGGATCCACGGCCAGCCGCTCGTCGTCGCCGCGATGGACTTCGCGTTC
CTCGGCGGCAGCCTGGGCGGCGCGGTCGGCGAACTGATCACCCTCGCCGCCGAGACCGCG
CTCGCCGAACACCTGCCGCTGCTGATCGTCAGCGCGTCCGGCGGCGCGCGCATGCAGGAA
GGCGCCGTCGCGCTCATGCAGATGGCCAAGACCAGCGCCGCCCTCGGGCAACTGGACGAG
GCCGGCGTGTTGACCATCTCGCTGGTCACCGACCCCACCTACGGCGGCGTCGCGGCGTCC
TTCGCGACCCTGTGCGACGTCATCGTCGCCGAACCCGGCGCGCGTCTCGGCTTCGCCGGC
CGGCGGGTCATCGCGCAGACCATCCGCGAGGAACTGCCGCCGGAGTTCCAGACCGCCGAA
TACCTCCTCGAACACGGCCTGATCGACCTGATCGTGCCGCGCCGCGCGCTGCGCGACGAA
CTGGCCCGCCTGCTGCGGGCCGGCGCGAAGCGGCCCAAGGGCGGGGACGGGGAACCGGCC
CGACGCGGCGGCCTGGACGCGGGGGCATCGCCGTACGTCGTCGACCCCGCCGACCTCGCC
GCGCACGACCCCAGCCGCCAGGTGCGCGCCGCGCGGGCCATCGACCGGCCCACCACGCTC
GACTACATCGCGCTGCTGTGCGAGGACTTCGTCGAACTGCGCGGCGACCGCATCTCGGGC
GACTGCCCCGCCATCGTCGCCGGCCTGGCCCGCTTCGGCGGCCGACCCGTCGCCGTCATC
GGCCACCAGAAGGGCCACGACGCGCAGGAGCTGCGCCGCCGCAACTTCGGCATGCCGATC
CCGTCGGGCTACCGCAAGGCCGCCCGGATCATGCGGCTCGCCGACAAACTCGGTCTCCCG
GTCGTCACGTTCGTCGACACCCCCGGCGCTTACCCCGGCGCGGTCGCCGAGGAGCAGGGC
CAGGCCGTCGCCATCGCCGAGAACCTGCGCCTGATGGCGGGCCTGCGCGTGCCGGTCGTC
ACCGTCGTCACCGGCGAGGGCGGCAGCGGCGGGGCGCTCGCGCTCGCCGTCGCCAACCGT
GTCCTGATGTTCGAGAACGGCATCTACTCGGTCATCAGCCCCGAGGGCTGCGCGGCCATC
CTGTGGCAGGACCCCGCCGCCGCCGGGCGTGCCGCCCGCGCGCTGAGGGTCACCGCCCGC
GAACTCCTCGGCCTGGGCATCGTCGACGGCGTCCTCCCGGAACCCGAAGGCGGCACCGGA
GCCGACCCGCTGCGCGCCGCCGACGCCCTCCGCGACGCGATCGCGGCCGGCCTCGCGGAG
TTGTCCCCCCTCGACGGCCACCAGTTGGTCGCCGACCGCTGGGCCCGCTTCCGCCGCTAT
GGCGCGGAACGCACCACCGACGCCGAGATCACCGCCATGAAAGGCGACCCGACGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR000022 Carboxyl transferase (Domain)
 [88-232]  3.2e-19 PF01039
PF01039   Carboxyl_trans
IPR000438 Acetyl-CoA carboxylase carboxyl transferase, beta subunit (Family)
 [13-267]  4.49999999999996e-101 TIGR00515
TIGR00515   AccD
IPR001095 Acetyl-CoA carboxylase, alpha subunit (Family)
 [304-395]  4.5e-35 PF03255
PF03255   ACCA
 [303-563]  1.29999999999998e-101 TIGR00513
TIGR00513   AccA
 [335-346]  2.39999798157265e-37 PR01069 [360-378]  2.39999798157265e-37 PR01069 [381-397]  2.39999798157265e-37 PR01069 [400-413]  2.39999798157265e-37 PR01069 [416-429]  2.39999798157265e-37 PR01069 [444-453]  2.39999798157265e-37 PR01069
PR01069   ACCCTRFRASEA
IPR011762 Acetyl-coenzyme A carboxyltransferase, N-terminal (Domain)
 [35-249]  PS50980
PS50980   COA_CT_NTER
IPR011763 Acetyl-coenzyme A carboxyltransferase, C-terminal (Domain)
 [246-549]  PS50989
PS50989   COA_CT_CTER
SignalP
 [1-23]  0.077 Signal
Eukaryota   
TMHMM No significant hit