DNLJ_MOOTA
ID DNLJ_MOOTA Reviewed; 666 AA.
AC Q2RGY0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Moth_2013;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC20309.1; -; Genomic_DNA.
DR RefSeq; WP_011393509.1; NC_007644.1.
DR RefSeq; YP_430852.1; NC_007644.1.
DR AlphaFoldDB; Q2RGY0; -.
DR SMR; Q2RGY0; -.
DR STRING; 264732.Moth_2013; -.
DR EnsemblBacteria; ABC20309; ABC20309; Moth_2013.
DR KEGG; mta:Moth_2013; -.
DR PATRIC; fig|264732.11.peg.2183; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_1_9; -.
DR OMA; HDVEHEI; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; SM00278; HhH1; 4.
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; Zinc.
FT CHAIN 1..666
FT /note="DNA ligase"
FT /id="PRO_0000313309"
FT DOMAIN 588..666
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT ACT_SITE 115
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 34..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 83..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ SEQUENCE 666 AA; 72386 MW; 3D351879F3ADCACE CRC64;
MDLAAARQRV EELRRLIEEH NYRYYVLDQP SISDREYDAL MQELIALEEA YPELRTPDSP
SQRVGGAPRE EFNQVRHPQV LLSLNDAFNE GDLLEFDRRV RDLAGRPVEY VIEAKIDGLA
VALTYRDGLF TLGATRGDGQ VGEEVTANLK TIPALPLRLR RPLPFLVVRG EVYMPKVAFT
ALNAAREEAG EPLFANPRNA AAGSLRQLDP KITASRSLSL FVYQVISLTG AEVATQAGAL
DFLAELGFPV NPYRVVAPDI QAVLEEVKAW TPERRASLPY EIDGLVIKVN DLALHSVLGA
TAKAPRWAMA YKFPAEQATA RVEGIILRVG RTGVLTPTAV LTPVRLAGTT VSRATLHNED
YIREKDIRIG DTVIVQKAGD IIPEVVAVIP ERRTGSEEVF TMPERCPACG AAVVRPPGEA
AHRCTGGLAC PAQVLEGIIH FASRGAMDIQ GLGPAIVAQL LEAGLIHDAA DLYYLKEEDL
LKLERFGQQS ASNLLAAIAA SKKQPLERLI FALGIRNVGQ RAARVLADHF GSLDKLAAAT
VEELTALPDI GPRIAENIRE FFGEPRNRAV LEKLKKAGVR LEALNAAAPA GPLTGKVFVL
TGTLPGMTRQ EAEELITRAG GKVSSSVSRK TDYVVAGEKP GSKLDRAREL GVPVINADGL
RQLLRQ
