DB code: M00208

CATH domain 3.30.1360.10 : Gyrase A; domain 2
2.170.120.12 : RNA Polymerase Alpha Subunit; Chain A, domain 2
1.10.150.20 : DNA polymerase; domain 1
3.90.-.- :
3.90.-.- :
2.30.150.10 : Rna Polymerase Beta Subunit; Chain
2.40.50.100 : OB fold (Dihydrolipoamide Acetyltransferase, E2P)
2.40.270.10 : Dna-directed Rna Polymerase Ii 140kd Polypeptide; Chain
2.40.50.150 : OB fold (Dihydrolipoamide Acetyltransferase, E2P)
1.-.-.- :
3.-.-.- :
2.40.-.- :
-.-.-.- :
-.-.-.- :
-.-.-.- :
-.-.-.- :
1.10.1480.- : Dna-directed Rna Polymerase; Chain
E.C. 2.7.7.6
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.150.20 : DNA polymerase; domain 1 M00055 M00104 M00173 M00175 D00158
2.40.270.10 : Dna-directed Rna Polymerase Ii 140kd Polypeptide; Chain M00207
2.40.50.100 : OB fold (Dihydrolipoamide Acetyltransferase, E2P) M00163 M00222 M00145 M00188 M00189 T00223 M00190 M00191
2.40.50.150 : OB fold (Dihydrolipoamide Acetyltransferase, E2P) M00207
3.30.1360.10 : Gyrase A; domain 2 M00207

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0A7Z4 DNA-directed RNA polymerase subunit alpha
RNAP subunit alpha
EC 2.7.7.6
Transcriptase subunit alpha
RNA polymerase subunit alpha
NP_417754.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492137.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01000 (RNA_pol_A_bac)
PF03118 (RNA_pol_A_CTD)
PF01193 (RNA_pol_L)
[Graphical View]
P0A8V2 DNA-directed RNA polymerase subunit beta
RNAP subunit beta
EC 2.7.7.6
Transcriptase subunit beta
RNA polymerase subunit beta
NP_418414.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491474.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF04563 (RNA_pol_Rpb2_1)
PF04561 (RNA_pol_Rpb2_2)
PF04565 (RNA_pol_Rpb2_3)
PF10385 (RNA_pol_Rpb2_45)
PF00562 (RNA_pol_Rpb2_6)
PF04560 (RNA_pol_Rpb2_7)
[Graphical View]
P0A8T7 DNA-directed RNA polymerase subunit beta''
RNAP subunit beta''
EC 2.7.7.6
Transcriptase subunit beta''
RNA polymerase subunit beta''
NP_418415.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491473.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF04997 (RNA_pol_Rpb1_1)
PF00623 (RNA_pol_Rpb1_2)
PF04983 (RNA_pol_Rpb1_3)
PF05000 (RNA_pol_Rpb1_4)
PF04998 (RNA_pol_Rpb1_5)
[Graphical View]
P0A800 DNA-directed RNA polymerase subunit omega
RNAP omega subunit
EC 2.7.7.6
Transcriptase subunit omega
RNA polymerase omega subunit
NP_418106.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491785.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01192 (RNA_pol_Rpb6)
[Graphical View]

KEGG enzyme name
DNA-directed RNA polymerase
RNA nucleotidyltransferase (DNA-directed)
RNA polymerase I
RNA polymerase II
RNA polymerase III

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A7Z4 RPOA_ECOLI Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
P0A8V2 RPOB_ECOLI Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
P0A8T7 RPOC_ECOLI Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (By similarity).
P0A800 RPOZ_ECOLI Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism
MAP00240 Pyrimidine metabolism
MAP03020 RNA polymerase

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00201 C00046 C00013 C00046
E.C.
Compound Magnesium Nucleoside triphosphate RNA(n) Pyrophosphate RNA(n+1)
Type divalent metal (Ca2+, Mg2+) nucleotide nucleic acids phosphate group/phosphate ion nucleic acids
ChEBI 18420
 18420
 		29888
 29888
PubChem 888
 888
 		1023
 21961011
 1023
 21961011
1bdfA01 Unbound Unbound Unbound Unbound Unbound
1bdfB01 Unbound Unbound Unbound Unbound Unbound
1bdfC01 Unbound Unbound Unbound Unbound Unbound
1bdfD01 Unbound Unbound Unbound Unbound Unbound
1bdfA02 Unbound Unbound Unbound Unbound Unbound
1bdfB02 Unbound Unbound Unbound Unbound Unbound
1bdfC02 Unbound Unbound Unbound Unbound Unbound
1bdfD02 Unbound Unbound Unbound Unbound Unbound
1cooA Unbound Unbound Unbound Unbound Unbound
1lb2B Unbound Unbound Unbound Unbound Unbound
1lb2E Unbound Unbound Unbound Unbound Unbound
1xs9D Unbound Unbound Unbound Unbound Unbound
2aukA Unbound Unbound Unbound Unbound Unbound
2aukB Unbound Unbound Unbound Unbound Unbound
2aukC Unbound Unbound Unbound Unbound Unbound
2aukD Unbound Unbound Unbound Unbound Unbound
2aukE Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1bdf

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bdfA01 mutant R45A
1bdfB01 mutant R45A
1bdfC01 mutant R45A
1bdfD01 mutant R45A
1bdfA02
1bdfB02
1bdfC02
1bdfD02
1cooA
1lb2B
1lb2E
1xs9D
2aukA
2aukB
2aukC
2aukD
2aukE

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[17]
p.819-820
[18]
[35]
p.155-160
[36]
p.94-95
[40]
p.714-715

References
[1]
Resource
Comments
Medline ID
PubMed ID 8087855
Journal Cell
Year 1994
Volume 78
Pages 889-96
Authors Blatter EE, Ross W, Tang H, Gourse RL, Ebright RH
Title Domain organization of RNA polymerase alpha subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding.
Related PDB
Related UniProtKB
[2]
Resource
Comments Review
Medline ID
PubMed ID 7613089
Journal Curr Opin Genet Dev
Year 1995
Volume 5
Pages 197-203
Authors Ebright RH, Busby S
Title The Escherichia coli RNA polymerase alpha subunit: structure and function
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7752238
Journal J Mol Biol
Year 1995
Volume 248
Pages 756-67
Authors Kimura M, Ishihama A
Title Functional map of the alpha subunit of Escherichia coli RNA polymerase: insertion analysis of the amino-terminal assembly domain.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7491496
Journal Science
Year 1995
Volume 270
Pages 1495-7
Authors Jeon YH, Negishi T, Shirakawa M, Yamazaki T, Fujita N, Ishihama A, Kyogoku Y
Title Solution structure of the activator contact domain of the RNA polymerase alpha subunit.
Related PDB 1coo
Related UniProtKB P0A7Z4
[5]
Resource
Comments
Medline ID
PubMed ID 8557191
Journal Genes Dev
Year 1996
Volume 10
Pages 16-26
Authors Gaal T, Ross W, Blatter EE, Tang H, Jia X, Krishnan VV, Assa-Munt N, Ebright RH, Gourse RL
Title DNA-binding determinants of the alpha subunit of RNA polymerase: novel DNA-binding domain architecture.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8861963
Journal EMBO J
Year 1996
Volume 15
Pages 4358-67
Authors Murakami K, Fujita N, Ishihama A
Title Transcription factor recognition surface on the RNA polymerase alpha subunit is involved in contact with the DNA enhancer element.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8674985
Journal FEMS Microbiol Lett
Year 1996
Volume 139
Pages 175-80
Authors Kato N, Aiba H, Mizuno T
Title Suppressor mutations in alpha-subunit of RNA polymerase for a mutant of the positive regulator, OmpR, in Escherichia coli.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 9135123
Journal J Mol Biol
Year 1997
Volume 267
Pages 953-62
Authors Jeon YH, Yamazaki T, Otomo T, Ishihama A, Kyogoku Y
Title Flexible linker in the RNA polymerase alpha subunit facilitates the independent motion of the C-terminal activator contact domain.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9398509
Journal J Mol Biol
Year 1997
Volume 274
Pages 1-7
Authors Wood LF, Tszine NY, Christie GE
Title Activation of P2 late transcription by P2 Ogr protein requires a discrete contact site on the C terminus of the alpha subunit of Escherichia coli RNA polymerase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9050843
Journal Proc Natl Acad Sci U S A
Year 1997
Volume 94
Pages 1709-14
Authors Murakami K, Kimura M, Owens JT, Meares CF, Ishihama A
Title The two alpha subunits of Escherichia coli RNA polymerase are asymmetrically arranged and contact different halves of the DNA upstream element.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9326599
Journal Proc Natl Acad Sci U S A
Year 1997
Volume 94
Pages 11274-8
Authors Murakami K, Owens JT, Belyaeva TA, Meares CF, Busby SJ, Ishihama A
Title Positioning of two alpha subunit carboxy-terminal domains of RNA polymerase at promoters by two transcription factors.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 9477962
Journal Biochemistry
Year 1998
Volume 37
Pages 1344-9
Authors Miyake R, Murakami K, Owens JT, Greiner DP, Ozoline ON, Ishihama A, Meares CF
Title Dimeric association of Escherichia coli RNA polymerase alpha subunits, studied by cleavage of single-cysteine alpha subunits conjugated to iron-(S)-1-[p-(bromoacetamido)benzyl]ethylenediaminetetraacetate.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9657722
Journal Science
Year 1998
Volume 281
Pages 262-6
Authors Zhang G, Darst SA
Title Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain.
Related PDB 1bdf
Related UniProtKB P0A7Z4
[14]
Resource
Comments
Medline ID
PubMed ID 10049799
Journal J Struct Biol
Year 1998
Volume 124
Pages 115-22
Authors Darst SA, Polyakov A, Richter C, Zhang G
Title Insights into Escherichia coli RNA polymerase structure from a combination of x-ray and electron crystallography.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9461538
Journal Biochem J
Year 1998
Volume 330
Pages 413-20
Authors Lloyd GS, Busby SJ, Savery NJ
Title Spacing requirements for interactions between the C-terminal domain of the alpha subunit of Escherichia coli RNA polymerase and the cAMP receptor protein
Related PDB
Related UniProtKB
[16]
Resource
Comments Review
Medline ID
PubMed ID 10047577
Journal Curr Opin Struct Biol
Year 1999
Volume 9
Pages 21-8
Authors Jager J, Pata JD
Title Getting a grip: polymerases and their substrate complexes.
Related PDB
Related UniProtKB
[17]
Resource
Comments Comments in: Cell 1999;98(6):687-90.
Medline ID
PubMed ID 10499798
Journal Cell
Year 1999
Volume 98
Pages 811-24
Authors Zhang G, Campbell EA, Minakhin L, Richter C, Severinov K, Darst SA
Title Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution.
Related PDB
Related UniProtKB
[18]
Resource
Comments Review
Medline ID
PubMed ID 10744988
Journal Curr Opin Microbiol
Year 2000
Volume 3
Pages 118-25.
Authors Severinov K
Title RNA polymerase structure-function: insights into points of transcriptional regulation.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 10892647
Journal Cell
Year 2000
Volume 101
Pages 601-11
Authors Naryshkin N, Revyakin A, Kim Y, Mekler V, Ebright RH
Title Structural organization of the RNA polymerase-promoter open complex.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 10915625
Journal Science
Year 2000
Volume 289
Pages 619-25
Authors Korzheva N, Mustaev A, Kozlov M, Malhotra A, Nikiforov V, Goldfarb A, Darst SA
Title A structural model of transcription elongation.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 10920271
Journal J Biochem(Tokyo)
Year 2000
Volume 128
Pages 337-44
Authors Otomo T, Yamazaki T, Murakami K, Ishihama A, Kyogoku Y
Title Structural study of the N-terminal domain of the alpha subunit of Escherichia coli RNA polymerase solubilized with non-denaturing detergents.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 10821700
Journal Biochemistry
Year 2000
Volume 39
Pages 6243-9
Authors Fujita N, Endo S, Ishihama A
Title Structural requirements for the interdomain linker of alpha subunit of Escherichia coli RNA polymerase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 10747024
Journal EMBO J
Year 2000
Volume 19
Pages 1555-66
Authors Meng W, Savery NJ, Busby SJ, Thomas MS
Title The Escherichia coli RNA polymerase alpha subunit linker: length requirements for transcription activation at CRP-dependent promoters.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 10986259
Journal J Bacteriol
Year 2000
Volume 182
Pages 5539-50
Authors Fritsch PS, Urbanowski ML, Stauffer GV
Title Role of the RNA polymerase alpha subunits in MetR-dependent activation of metE and metH: important residues in the C-terminal domain and orientation requirements within RNA polymerase.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 11073923
Journal J Bacteriol
Year 2000
Volume 182
Pages 6774-82
Authors Holcroft CC, Egan SM
Title Interdependence of activation at rhaSR by cyclic AMP receptor protein, the RNA polymerase alpha subunit C-terminal domain, and rhaR.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 10821859
Journal J Biol Chem
Year 2000
Volume 275
Pages 16057-63
Authors Wada T, Yamazaki T, Kyogoku Y
Title The structure and the characteristic DNA binding property of the C-terminal domain of the RNA polymerase alpha subunit from Thermus thermophilus.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 10972822
Journal Mol Microbiol
Year 2000
Volume 37
Pages 1032-40
Authors Lee DJ, Wing HJ, Savery NJ, Busby SJ
Title Analysis of interactions between Activating Region 1 of Escherichia coli FNR protein and the C-terminal domain of the RNA polymerase alpha subunit: use of alanine scanning and suppression genetics.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 10908318
Journal Nucleic Acids Res
Year 2000
Volume 28
Pages 2643-50
Authors Shao X, Grishin NV
Title Common fold in helix-hairpin-helix proteins.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 11554759
Journal Biochem Biophys Res Commun
Year 2001
Volume 287
Pages 519-21
Authors Ruiz R, Ramos JL
Title Residues 137 and 153 of XylS influence contacts with the C-terminal domain of the RNA polymerase alpha subunit.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 11240128
Journal FEBS Lett
Year 2001
Volume 491
Pages 207-11
Authors Ruiz R, Ramos JL, Egan SM
Title Interactions of the XylS regulators with the C-terminal domain of the RNA polymerase alpha subunit influence the expression level from the cognate Pm promoter.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 11237595
Journal J Mol Biol
Year 2001
Volume 306
Pages 213-25
Authors Yasuno K, Yamazaki T, Tanaka Y, Kodama TS, Matsugami A, Katahira M, Ishihama A, Kyogoku Y
Title Interaction of the C-terminal domain of the E. coli RNA polymerase alpha subunit with the UP element: recognizing the backbone structure in the minor groove surface.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 11212907
Journal Mol Gen Genet
Year 2001
Volume 264
Pages 531-8
Authors Sujatha S, Ishihama A, Chatterji D
Title Functional complementation between mutations at two distant positions in Escherichia coli RNA polymerase as revealed by second-site suppression.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 11266593
Journal Protein Sci
Year 2001
Volume 10
Pages 46-54
Authors Kannan N, Chander P, Ghosh P, Vishveshwara S, Chatterji D
Title Stabilizing interactions in the dimer interface of alpha-subunit in Escherichia coli RNA polymerase: a graph spectral and point mutation study.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 11290327
Journal Cell
Year 2001
Volume 104
Pages 901-12
Authors Campbell EA, Korzheva N, Mustaev A, Murakami K, Nair S, Goldfarb A, Darst SA
Title Structural mechanism for Rifampicin inhibition of bacterial RNA polymerase.
Related PDB
Related UniProtKB
[35]
Resource
Comments Review
Medline ID
PubMed ID 11297923
Journal Curr Opin Struct Biol
Year 2001
Volume 11
Pages 155-62
Authors Darst SA
Title Bacterial RNA polymerase.
Related PDB
Related UniProtKB
[36]
Resource
Comments Review
Medline ID
PubMed ID 11839495
Journal Curr Opin Struct Biol
Year 2002
Volume 12
Pages 89-97
Authors Cramer P
Title Multisubunit RNA polymerases.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 11914063
Journal Biochemistry
Year 2002
Volume 41
Pages 4186-92
Authors Schmidt BD, Meares CF
Title Proteolytic DNA for mapping protein-DNA interactions.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 12016306
Journal Science
Year 2002
Volume 296
Pages 1280-4
Authors Murakami KS, Masuda S, Darst SA
Title Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 12016307
Journal Science
Year 2002
Volume 296
Pages 1285-90
Authors Murakami KS, Masuda S, Campbell EA, Muzzin O, Darst SA
Title Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex.
Related PDB
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 12000971
Journal Nature
Year 2002
Volume 417
Pages 712-9
Authors Vassylyev DG, Sekine S, Laptenko O, Lee J, Vassylyeva MN, Borukhov S, Yokoyama S
Title Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 12368266
Journal Genes Dev
Year 2002
Volume 16
Pages 2557-65
Authors Lloyd GS, Niu W, Tebbutt J, Ebright RH, Busby SJ
Title Requirement for two copies of RNA polymerase alpha subunit C-terminal domain for synergistic transcription activation at complex bacterial promoters.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 12142422
Journal J Bacteriol
Year 2002
Volume 184
Pages 4520-8
Authors Finney AH, Blick RJ, Murakami K, Ishihama A, Stevens AM
Title Role of the C-terminal domain of the alpha subunit of RNA polymerase in LuxR-dependent transcriptional activation of the lux operon during quorum sensing.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 11866515
Journal J Mol Biol
Year 2002
Volume 316
Pages 517-29
Authors McLeod SM, Aiyar SE, Gourse RL, Johnson RC
Title The C-terminal domains of the RNA polymerase alpha subunits: contact site with Fis and localization during co-activation with CRP at the Escherichia coli proP P2 promoter.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 12202833
Journal Science
Year 2002
Volume 297
Pages 1562-6
Authors Benoff B, Yang H, Lawson CL, Parkinson G, Liu J, Blatter E, Ebright YW, Berman HM, Ebright RH
Title Structural basis of transcription activation: the CAP-alpha CTD-DNA complex.
Related PDB 1lb2
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 15458404
Journal Mol Microbiol
Year 2004
Volume 54
Pages 45-59
Authors Dangi B, Gronenborn AM, Rosner JL, Martin RG
Title Versatility of the carboxy-terminal domain of the alpha subunit of RNA polymerase in transcriptional activation: use of the DNA contact site as a protein contact site for MarA.
Related PDB 1xs9
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 16154587
Journal J Mol Biol
Year 2005
Volume 353
Pages 138-54
Authors Chlenov M, Masuda S, Murakami KS, Nikiforov V, Darst SA, Mustaev A
Title Structure and function of lineage-specific sequence insertions in the bacterial RNA polymerase beta' subunit.
Related PDB 2auk
Related UniProtKB

Comments
The same E.C. number (2.7.7.6) appears in M00104, and M00207.
This enzyme seems to be composed of several subunits (alpha, beta, beta', and omega). However, the tertiary structures have been reported for the subunits, alpha, omega, and beta'. The structure of the beta' subunit have been partially solved.
Among these subunits, the beta' subunit seems to contain a catalytic site, which involves a Mg++ binding site.
Moreover, this enzyme is a bacterial RNA polymerase. However, the other bacterial RNA polymerases, such as one from Thermus aquaticus (Swiss-prot;Q9KWU8, Q9KWU7, Q9EVV4 & Q9KWU6), have got different domain compositions in the beta and beta' subunits from this polymerase enzyme (see [46]).

Created Updated
2003-07-22 2009-06-03