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Sequence of A3DJ38_ACET2

EC Number:2.7.1.78

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
polynucleotide 5'-hydroxyl-kinase
A3DJ38
Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
870
98776
Reaction
ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA
Other sequences found for EC No. 2.7.1.78

EC Number:3.1.3.16

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
protein-serine/threonine phosphatase
A3DJ38
Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
870
98776
Reaction
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate
Other sequences found for EC No. 3.1.3.16

EC Number:6.5.1.3

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
RNA ligase (ATP)
A3DJ38
Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
870
98776
Reaction
(ribonucleotide)n-3'-hydroxyl + 5'-(5'-diphosphoadenosine)-(ribonucleotide)m = (ribonucleotide)n+m + AMP
Other sequences found for EC No. 6.5.1.3

General information:

Sequence
show sequence in fasta format
  0 MKLTIPELSL VVLIGSSGSG KSTFAKKHFK PTEVISSDFC RGLVSDDEND QTVTGAAFDV
 60 LHYIVSKRLQ LGKLTVVDAT NVQESARKPL IEIAKDYHCF PVAVVFNLPE KVCQERNKNR
120 TDRQVEEYVI RKHTQQLKKS IKGLQREGFR YVYILNSPEE VEEVVFERQP LWNNKKDEHG
180 PFDIIGDIHG CYDELKMLLE KLGYLIEEVE GGVGSGKYRV THPEGRKVLF LGDLVDRGPK
240 ITEVLKLVMG MVKSGIALCV PGNHDVKLLR KLNGRDVQIT HGLDRTLEQL AKEPQEFIEE
300 VKAFIDGLVS HYVLDDGKLV VAHAGMKEEF QGRGSGKVRE FALYGETTGE TDEYGLPVRY
360 DWASDYRGKA LVVYGHTPQA EVLKVNNTIN IDTGCVFGGK LTAYRYPERE IVDVKALKTY
420 YEPAKPFLPK EDMAERFEAR TDNDILDIND VLGKKIITTR LMSSITIHEE NSIAALEVMS
480 RFAADPHWLI YLPPTMSPCE TSKKEGMLEH PIEAFEYFRT RGVGKVVCEQ KHMGSRAVVI
540 VCKDSQVAEK RFGVLDGTAG ICYTRTGRHF FDDMQLEAEL IDRVRKVLDK SGFWGDFNTD
600 WVCLDCELMP WSAKAQKLLE EQYSAVGISG RVVLDEAVKL LKQASLNKTV SFDVSRQTSG
660 KNADINELLQ RFTERSEMMQ KYVEAYRKYC WPVNSIDDLK LAPFHILATE GKVHSDKNHI
720 WHMDTIAKYC TQDDSLIMAT NHILVDVTDA ESVDKGIKWW EDLTASGGEG MVVKPYDFIV
780 KNGRELLQPA VKCRGREYLR IIYGPEYTMD ENIERLRNRA VGKKRSLALR EFSLGMEALE
840 RFVRNEPLYR VHECVFGVLA LESEPVDPRL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
101243473
Smith P.,Wang L.K.,Nair P.A.,Shuman S.
The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.
Proc. Natl. Acad. Sci. U.S.A.
109
2296-2301
2012
101243474
Wang P.,Chan C.M.,Christensen D.,Zhang C.,Selvadurai K.,Huang R.H.
Molecular basis of bacterial protein Hen1 activating the ligase activity of bacterial protein Pnkp for RNA repair.
Proc. Natl. Acad. Sci. U.S.A.
109
13248-13253
2012
101243475
Wang L.K.,Das U.,Smith P.,Shuman S.
Structure and mechanism of the polynucleotide kinase component of the bacterial Pnkp-Hen1 RNA repair system.
RNA
18
2277-2286
2012
101243476
Das U.,Wang L.K.,Smith P.,Shuman S.
Structural and biochemical analysis of the phosphate donor specificity of the polynucleotide kinase component of the bacterial pnkphen1 RNA repair system.
Biochemistry
52
4734-4743
2013
101243477
Wilson C.M.,Rodriguez M.Jr.,Johnson C.M.,Martin S.L.,Chu T.M.,Wolfinger R.D.,Hauser L.J.,Land M.L.,Klingeman D.M.,Syed M.H.,Ragauskas A.J.,Tschaplinski T.J.,Mielenz J.R.,Brown S.D.
Global transcriptome analysis of Clostridium thermocellum ATCC 27405 during growth on dilute acid pretreated Populus and switchgrass.
Biotechnol. Biofuels
6
179-179
2013
101243478
Wang L.K.,Smith P.,Shuman S.
Structure and mechanism of the 2',3' phosphatase component of the bacterial Pnkp-Hen1 RNA repair system.
Nucleic Acids Res.
41
5864-5873
2013
101243479
Das U.,Wang L.K.,Smith P.,Munir A.,Shuman S.
Structures of bacterial polynucleotide kinase in a michaelis complex with nucleoside triphosphate (NTP)-Mg2+ and 5'-OH RNA and a mixed substrate-product complex with NTP-Mg2+ and a 5'-phosphorylated oligonucleotide.
J. Bacteriol.
196
4285-4292
2014
101243480
Das U.,Wang L.K.,Smith P.,Jacewicz A.,Shuman S.
Structures of bacterial polynucleotide kinase in a Michaelis complex with GTPMg2+ and 5'-OH oligonucleotide and a product complex with GDPMg2+ and 5'-PO4 oligonucleotide reveal a mechanism of general acid-base catalysis and the determinants of phosphoacceptor recognition.
Nucleic Acids Res.
42
1152-1161
2014