Entry
Name
RNA ligase (ATP);
polyribonucleotide synthase (ATP);
RNA ligase;
polyribonucleotide ligase;
ribonucleic ligase;
poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming)
Class
Ligases;
Forming phosphoric-ester bonds;
Ligases that form phosphoric-ester bonds (only sub-subclass identified to date)
BRITE hierarchy
Sysname
poly(ribonucleotide)-3'-hydroxyl:5'-phospho-poly(ribonucleotide) ligase (ATP)
Reaction(IUBMB)
ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate (overall reaction) [RN:
R07640 ];
(1a) ATP + [RNA ligase]-L-lysine = [RNA ligase]-N6-(5'-adenylyl)-L-lysine + diphosphate;
(1b) [RNA ligase]-N6-(5'-adenylyl)-L-lysine + 5'-phospho-(ribonucleotide)m = 5'-(5'-diphosphoadenosine)-(ribonucleotide)m + [RNA ligase]-L-lysine;
(1c) (ribonucleotide)n-3'-hydroxyl + 5'-(5'-diphosphoadenosine)-(ribonucleotide)m = (ribonucleotide)n+m + AMP
Reaction(KEGG)
Substrate
ATP [CPD:
C00002 ];
(ribonucleotide)n-3'-hydroxyl;
5'-phospho-(ribonucleotide)m;
[RNA ligase]-L-lysine;
[RNA ligase]-N6-(5'-adenylyl)-L-lysine;
5'-(5'-diphosphoadenosine)-(ribonucleotide)m
Product
(ribonucleotide)n+m [CPD:
C00046 ];
AMP [CPD:
C00020 ];
diphosphate [CPD:
C00013 ];
[RNA ligase]-N6-(5'-adenylyl)-L-lysine;
5'-(5'-diphosphoadenosine)-(ribonucleotide)m;
[RNA ligase]-L-lysine
Comment
The enzyme catalyses the ligation of RNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in RNA. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-[RNA]. Finally, the enzyme catalyses a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
History
EC 6.5.1.3 created 1976, modified 2016
Orthology
K18961 Straboviridae RNA ligase 1
K18962 Straboviridae RNA ligase 2
K26449 Alphabaculovirus putative polynucleotide kinase / polynucleotide phosphatase / RNA ligase
Genes
CGR : 2891489(GVI51_M02959)
NCS : NCAS_0A09580(NCAS0A09580)
NDI : NDAI_0G05550(NDAI0G05550)
TPF : TPHA_0I00970(TPHA0I00970)
TBL : TBLA_0C02880(TBLA0C02880)
TDL : TDEL_0D01480(TDEL0D01480)
KAF : KAFR_0A01500(KAFR0A01500)
KNG : KNAG_0B01860(KNAG0B01860)
LBG : 92211092(LODBEIA_P58960)
CAL : CAALFM_C702060WA(LIG1)
CLU : CLUG_02324 CLUG_02325
ASAU : 88174938(PUMCH_003875)
YLI : 2911332(YALI2_D00824g) 2912358(YALI2_E00140g)
NTE : NEUTE1DRAFT121207(NEUTE1DRAFT_121207)
SMP : 10805415(SMAC4_07337)
RTHE : 98125477(VTJ83DRAFT_4353)
TATV : 25777916(TrAtP1_002984)
TASP : 36608937(TrAFT101_006707)
PLJ : 28885318(PLICBS_006888)
CDET : 87938811(CDEST_02308)
BFU : BCIN_11g04740(Bctrl1)
CPW : 9697668(D8B26_007309)
PTRR : 6349699(PtrM4_000780)
ADAC : 96089839(ACET3X_009517)
CDEP : 91084495(L203_100279)
KMG : 30163093(I203_102085)
KNE : 92180163(IAR55_002905)
CCAC : CcaHIS019_0702070(trl1)
PPL : POSPLDRAFT_100403 POSPLDRAFT_101360
ADL : AURDEDRAFT_117966 AURDEDRAFT_171844 AURDEDRAFT_171860 AURDEDRAFT_71532 AURDEDRAFT_85050
ABP : AGABI1DRAFT122028(AGABI1DRAFT_122028) AGABI1DRAFT122582(AGABI1DRAFT_122582)
ABV : AGABI2DRAFT187168(AGABI2DRAFT_187168) AGABI2DRAFT210807(AGABI2DRAFT_210807)
SCM : SCHCO_02671118(SCHCODRAFT_02671118)
PGR : PGTG_07519 PGTG_12509
TBR : TB927.1.3030(KREL2) Tb09.160.2970
TBG : TbgDal_I1840 TbgDal_IX2300
TCR : 506363.110 510155.20 511585.20
LMA : LMJF_01_0590 LMJF_20_1730(REL2)
LIF : LINJ_01_0610 LINJ_20_1700(REL2)
LDO : LDBPK_010610 LDBPK_201700
LMI : LMXM_01_0590 LMXM_20_1730
LMAT : 92516440(LSCM1_06504) 92518047(LSCM1_08197)
LBZ : LBRM_01_0620 LBRM_20_5890
LPAN : LPMP_010590 LPMP_205830(REL2)
LOI : 92362078(LSCM4_06220) 92364159(LSCM4_08356)
LEIS : 94181413(GH5_06072) 94183721(GH5_08523)
LENR : 94173103(CUR178_05914) 94175633(CUR178_08496)
LEIN : 94189388(JIQ42_05766) 94192019(JIQ42_08465)
PHET : 94292062(JKF63_06032) 94293845(JKF63_07840)
» show all
Taxonomy
Reference
Authors
Silber R, Malathi VG, Hurwitz J.
Title
Purification and properties of bacteriophage T4-induced RNA ligase.
Journal
Reference
Authors
Cranston JW, Silber R, Malathi VG, Hurwitz J
Title
Studies on ribonucleic acid ligase. Characterization of an adenosine triphosphate-inorganic pyrophosphate exchange reaction and demonstration of an enzyme-adenylate complex with T4 bacteriophage-induced enzyme.
Journal
J Biol Chem 249:7447-56 (1974)
Reference
Authors
Sugino A, Snoper TJ, Cozzarelli NR
Title
Bacteriophage T4 RNA ligase. Reaction intermediates and interaction of substrates.
Journal
J Biol Chem 252:1732-8 (1977)
Reference
Authors
Romaniuk PJ, Uhlenbeck OC
Title
Joining of RNA molecules with RNA ligase.
Journal
Reference
Authors
Ho CK, Wang LK, Lima CD, Shuman S
Title
Structure and mechanism of RNA ligase.
Journal
Sequence
Reference
Authors
Nandakumar J, Shuman S, Lima CD
Title
RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forward.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.5.1.3
ExPASy - ENZYME nomenclature database: 6.5.1.3
BRENDA, the Enzyme Database: 6.5.1.3
LinkDB
All DBs