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Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.6 DNA-directed RNA polymerase
IUBMB Comments
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
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Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase ii, pol ii, t7 rna polymerase, rna polymerase i, pol iii, rna polymerase iii, pol i, rnapii, rnap ii, dna-dependent rna polymerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C RNA formation factors
-
-
-
0
chloroplast soluble RNA polymerase
-
-
-
0
deoxyribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
0
DNA-dependent ribonucleate nucleotidyltransferase
-
-
-
0
DNA-dependent RNA nucleotidyltransferase
-
-
-
0
DNA-dependent RNA polymerase
-
-
-
0
nucleotidyltransferase, ribonucleate
-
-
-
0
Pol II
-
-
-
0
ribonucleate nucleotidyltransferase
-
-
-
0
ribonucleate polymerase
-
-
-
0
ribonucleic acid formation factors, C
-
-
-
0
ribonucleic acid nucleotidyltransferase
-
-
-
0
ribonucleic acid polymerase
-
-
-
0
ribonucleic acid transcriptase
-
-
-
0
ribonucleic polymerase
-
-
-
0
ribonucleic transcriptase
-
-
-
0
RNA formation factors, C
-
-
-
0
RNA nucleotidyltransferase
-
-
-
0
RNA nucleotidyltransferase (DNA-directed)
-
-
-
0
RNA polymerase
RNA polymerase core enzyme
-
-
RNA polymerase I
-
-
-
0
RNA polymerase II
-
-
-
0
RNA polymerase III
-
-
-
0
RNA transcriptase
-
-
-
0
RNAP core enzyme
-
-
RNAP I
-
-
-
0
RNAP II
-
-
-
0
RNAP III
-
-
-
0
transcriptase
-
-
-
0
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
0
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
CAS REGISTRY NUMBER
COMMENTARY hide
9014-24-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme is able to use a variety of DNA templates. DNA from bacteriphage phiPLS27 is transcribed more efficiently than DNA isolated from lamda or herring sperm. DNA isolated from bacteriophage T7 and T7 D111 is utilized more efficiently
-
0
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required, optimal activity at 10 mM MgCl2
Mn2+
-
can partially replace Mg2+, 20% of the activity with Mg2+
additional information
-
KCl, ZnCl2 and CaCl2 can not replace MgCl2 in the assay mixture
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
actinomycin D
-
-
KCl
-
above 10 mM
Streptolydigin
-
-
streptovaracin
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
Tris-HCl buffer
9
-
glycine-NaOH buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
intracellular levels of RNAP, RpoD and PvdS in strains PAO1 and W1485, quantification of RpoD- and PvdS-dependent RNAP holoenzymes, overview
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A2H4G8C7_PSEAI
326
0
35306
TrEMBL
-
C7AUJ4_PSEAI
231
0
25439
TrEMBL
-
A0A2V3FME1_PSEAI
126
0
13648
TrEMBL
-
A0A5E8VRR9_PSEAI
1357
0
150870
TrEMBL
-
A0A485H868_PSEAI
113
0
12748
TrEMBL
-
A0A643I398_PSEAI
1366
0
150845
TrEMBL
-
A0A485I544_PSEAI
149
0
16168
TrEMBL
-
A0A069Q5Y8_PSEAI
1399
0
154383
TrEMBL
-
I1V4P2_PSEAI
225
0
24445
TrEMBL
-
A0A367MCC7_PSEAI
1059
0
117813
TrEMBL
-
A0A5M6GQ97_PSEAI
129
0
15003
TrEMBL
-
Q65A35_PSEAI
360
0
39392
TrEMBL
-
G5DC68_PSEAI
203
0
22210
TrEMBL
-
A0A140S9T0_PSEAI
333
0
36650
TrEMBL
-
G3M0Q8_PSEAI
197
0
21566
TrEMBL
-
A0A2S5IAK0_PSEAI
333
0
36630
TrEMBL
-
A0A485H6U9_PSEAI
1163
0
127194
TrEMBL
-
A0A485I572_PSEAI
779
0
86789
TrEMBL
-
A0A2R3IUH1_PSEAI
1357
0
150866
TrEMBL
-
Q5ZN25_PSEAI
383
0
41873
TrEMBL
-
A0A2K4XKZ8_PSEAI
1399
0
154397
TrEMBL
-
A0A485I7S7_PSEAI
577
0
63998
TrEMBL
-
A0A485BPF4_PSEAI
1289
0
143041
TrEMBL
-
A0A2V3F4A3_PSEAI
75
0
8310
TrEMBL
-
A0A072ZBF8_PSEAI
1357
0
150852
TrEMBL
-
A0A485H4C5_PSEAI
234
0
26874
TrEMBL
-
Q65A33_PSEAI
360
0
39570
TrEMBL
-
A0A2S5IAM8_PSEAI
1399
0
154771
TrEMBL
-
Q59AE9_PSEAI
261
0
28965
TrEMBL
-
A0A2S5I8T5_PSEAI
87
0
9746
TrEMBL
-
Q65A25_PSEAI
309
0
33729
TrEMBL
-
A0A2R3IRH2_PSEAI
1399
0
154369
TrEMBL
-
A0A2V3FLB2_PSEAI
1314
0
145817
TrEMBL
-
A0A067YF44_PSEAI
196
0
21528
TrEMBL
-
Q5ZH00_PSEAI
364
0
40200
TrEMBL
-
A0A367MEM0_PSEAI
228
0
25678
TrEMBL
-
A0A659BUB3_PSEAI
1357
0
150842
TrEMBL
-
A0A5P2U4V2_PSEAI
232
0
25526
TrEMBL
-
A0A0F6RPU4_PSEAI
1399
0
154369
TrEMBL
-
A0A485I7U0_PSEAI
929
0
103031
TrEMBL
-
A0A289ZHL5_PSEAI
220
0
23806
TrEMBL
-
A0A2V3FPF7_PSEAI
184
0
20561
TrEMBL
-
A0A485BLV0_PSEAI
80
0
9174
TrEMBL
-
A0A6B0QNX1_PSEAI
1399
0
154397
TrEMBL
-
Q9FAG8_PSEAI
270
0
30030
TrEMBL
-
A0A6H3G6B9_PSEAI
147
0
16126
TrEMBL
-
A0A2U9A291_PSEAI
305
0
33018
TrEMBL
-
A0A069Q227_PSEAI
88
0
9775
TrEMBL
-
A0A6G7LG73_PSEAI
497
0
56068
TrEMBL
-
A0A485I8N4_PSEAI
285
0
31481
TrEMBL
-
Q9EU01_PSEAI
270
0
30003
TrEMBL
-
A0A485F246_PSEAI
1224
0
135624
TrEMBL
-
A0A485H6B0_PSEAI
344
0
37705
TrEMBL
-
A0A5E9K5L9_PSEAI
1360
0
151209
TrEMBL
-
Q65A34_PSEAI
360
0
39594
TrEMBL
-
A0A659B970_PSEAI
333
0
36636
TrEMBL
-
A0A6H1QNK4_PSEAI
497
0
56041
TrEMBL
-
A0A485H4E7_PSEAI
912
0
101212
TrEMBL
-
A0A6H3FWZ3_PSEAI
1351
0
149367
TrEMBL
-
A0A2S5IAL6_PSEAI
1357
0
150980
TrEMBL
-
A0A367LX41_PSEAI
94
0
10294
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
148000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
157000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
45000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
87000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
-
beta',beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R584A
-
site-directed mutagenesis, the RNAP holoenzyme containing this sigma70 mutant binds preferentially to promoters bearing a specifically mutated -35 element
additional information
-
phenotypes of several sigma70 mutants and of diverse rsd mutants, genetic screening for isolating enhanced-function Rsd mutants, overview. Interaction of Rsd and AlgQ mutants with region 2 and 4 of sigma70, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
each freeze-thaw cycle results in significant loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, -20°C or -70°C, 50% w/v glycerol, stable for more than 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RNAP purification from iron-starved Pseudomonas aeruginosa cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Allan, B.; Kropinski, A.M.
DNA-dependent RNA polymerase from Pseudomonas aeruginosa
Biochem. Cell Biol.
65
776-782
1987
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Tiburzi, F.; Imperi, F.; Visca, P.
Intracellular levels and activity of PvdS, the major iron starvation sigma factor of Pseudomonas aeruginosa
Mol. Microbiol.
67
213-227
2008
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Yuan, A.H.; Gregory, B.D.; Sharp, J.S.; McCleary, K.D.; Dove, S.L.; Hochschild, A.
Rsd family proteins make simultaneous interactions with regions 2 and 4 of the primary sigma factor
Mol. Microbiol.
70
1136-1151
2008
Pseudomonas aeruginosa
Manually annotated by BRENDA team
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