DNLJ_SYNAS
ID DNLJ_SYNAS Reviewed; 672 AA.
AC Q2LTN8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; OrderedLocusNames=SYNAS_15650;
GN ORFNames=SYN_02935;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01588};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
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DR EMBL; CP000252; ABC77444.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LTN8; -.
DR SMR; Q2LTN8; -.
DR STRING; 56780.SYN_02935; -.
DR EnsemblBacteria; ABC77444; ABC77444; SYN_02935.
DR KEGG; sat:SYN_02935; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_1_7; -.
DR OMA; HDVEHEI; -.
DR Proteomes; UP000001933; Chromosome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR001679; DNAligase.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR Pfam; PF12826; HHH_2; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR TIGRFAMs; TIGR00575; dnlj; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW Metal-binding; NAD; Reference proteome; Zinc.
FT CHAIN 1..672
FT /note="DNA ligase"
FT /id="PRO_0000313490"
FT DOMAIN 593..672
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT ACT_SITE 118
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 35..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 84..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ SEQUENCE 672 AA; 74509 MW; 21D5C52435B5B4FB CRC64;
MMDAESARKN IEDLKARIEY HNRRYYQLDD PEISDAEYDS LLQELIALEK QFPQWLTEDS
PSRRIGAAPL SKFAPAVHLS PMLSLANAFS EEEILEFDRR LKRFLDSSER LSFVVEPKID
GVAVNLIYSS GVLTTGATRG DGAKGEDVTQ NIRTLHTIPL KIQNGSDERL PEQIEIRGEI
YMETAAFRKL NERRLAAGEP PFANPRNAAA GSLRQLDASI TARRPLKMFC YAVGIVRGRA
FTYHHDVLHA LKKWGFSVNP FIRQVEGIEK CIEFYRELQD LRNELPYEID GMVIKVDDLS
LQTRLGAVSR SPRWAVACKF AATQATTVIR DIIVNVGRTG TLTPVALMTP VKVGGVTVSR
ATLHNQDEID KKDIRIGDTV LVQRAGDVIP EVVKVIVSNR SGREIPFKIP DTCPECGSEV
VRLAGEAAHR CIGLSCPAQL RRHIQHFVSR GGMDIEGLGD KLVSQLVNQK LIHDPADLYY
LSHDALLNLE RMAEKSVSNL LSAIELSKHP SLDKIIFALG IRHVGEHISK ILARRFRTLD
ALINTTENEL LAIRDIGPEV SSSILEFFRN ASNRRVIEKL KKAGVSPLET ISPRSAPLTG
KTFVFTGALS RMTRDEAKQI VESLGGQAAG TVTKKTDYVV AGEAAGSKLQ KAQKAGIAIL
SEEEFLRLAG KI
