ID M4Z4A5_9BRAD Unreviewed; 715 AA. AC M4Z4A5; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 03-AUG-2022, entry version 49. DE RecName: Full=DNA ligase {ECO:0000256|HAMAP-Rule:MF_01588}; DE EC=6.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01588}; DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000256|HAMAP-Rule:MF_01588}; GN Name=ligA {ECO:0000256|HAMAP-Rule:MF_01588}; GN ORFNames=S58_19670 {ECO:0000313|EMBL:BAM87974.1}; OS Bradyrhizobium oligotrophicum S58. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=1245469 {ECO:0000313|EMBL:BAM87974.1, ECO:0000313|Proteomes:UP000011841}; RN [1] {ECO:0000313|EMBL:BAM87974.1, ECO:0000313|Proteomes:UP000011841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S58 {ECO:0000313|EMBL:BAM87974.1, RC ECO:0000313|Proteomes:UP000011841}; RX PubMed=23396330; DOI=10.1128/AEM.00009-13; RA Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A., RA Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T., RA Minamisawa K.; RT "Genome analysis suggests that the soil oligotrophic bacterium Agromonas RT oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen-fixing symbiont RT of Aeschynomene indica."; RL Appl. Environ. Microbiol. 79:2542-2551(2013). 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:0000256|HAMAP-Rule:MF_01588}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01588}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01588}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01588}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP012603; BAM87974.1; -; Genomic_DNA. DR RefSeq; WP_015665101.1; NC_020453.1. DR STRING; 1245469.S58_19670; -. DR EnsemblBacteria; BAM87974; BAM87974; S58_19670. DR KEGG; aol:S58_19670; -. DR PATRIC; fig|1245469.3.peg.2013; -. DR eggNOG; COG0272; Bacteria. DR HOGENOM; CLU_007764_2_0_5; -. DR OrthoDB; 241401at2; -. DR Proteomes; UP000011841; 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; 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 Pfam; PF00533; BRCT; 1. DR Pfam; PF01653; DNA_ligase_aden; 1. DR Pfam; PF03120; DNA_ligase_OB; 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. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01588}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01588}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01588}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01588}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01588}. FT DOMAIN 637..710 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT ACT_SITE 133 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 49..53 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 98..99 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 131 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 154 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 307 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 331 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 436 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 438 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 466 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" SQ SEQUENCE 715 AA; 79814 MW; D581AE92F59E9F4D CRC64; MPKTTKPKKP VDVADLTKAQ AKVEWKRLAI ELETHDRLYY QDDQPKISDA AYDELRRRFN AIEKRFPELV SSESPSQKVG AAPSGRFKKV RHAVPMLSLD NAFAEEDVRD FAGRIARFLK LADDRIDFSA EPKIDGLSMS LRYERGELVT AATRGDGAEG EDVTANIRTL KDVPHKLHGR DLPDICEVRG EVYMTKQAFL ALNERQKEAG DTVFANPRNS AAGSLRQKDP TITASRPLGF FAYAWGEMSE MPAETQSGMI KWFERCGFTT NPLTRLCHSV EELIAFHHQI EEQRAELDYD IDGVVYKVDR IDWQERLGFV SRTPRWGIAH KFPAERAMTV LKDIEIQVGR TGSFTPVGKL EPVGVGGVIV QNVTLHNEDY IKGIGNKGEV LREGRDIRIG DTVVIQRAGD VIPQVVDVVI DKRPADAGEF KLPKTCPCPL HTDVVREEIA TGEEGSRARC TGEFACPFQK IQHLLLFVSR RAFDIDGLGE KQIEFFFEKE WVREPADIFT LAARNARLKL EEIEGYGETS VRNLFNAIDA RREIALERFI YALGMRHVGE TTALALARGY GSWDAFHDAC LKVAKGDEEA IAEMDALDQI GDTVIKSIAA YFGEDHNLGI VERLTKEVKI LDAEKPKRNS PIATKTVVFT GTLEKMTRDE AKATAERLGA KVSGSVSKKT DYVVAGPGAG SKLKDAQKHG VQVLTEDEWL QLIGE //