ID M4Z4A5_9BRAD Unreviewed; 715 AA. AC M4Z4A5; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 25-OCT-2017, entry version 33. 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; Rhizobiales; 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}; 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 RT Agromonas oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen- RT fixing symbiont of Aeschynomene indica."; RL Appl. Environ. Microbiol. 79:2542-2551(2013). CC -!- FUNCTION: DNA ligase that catalyzes the formation of CC phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl CC groups in double-stranded DNA using NAD as a coenzyme and as the CC energy source for the reaction. It is essential for DNA CC replication and repair of damaged DNA. {ECO:0000256|HAMAP- CC Rule:MF_01588}. CC -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl CC + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) CC + AMP + beta-nicotinamide D-nucleotide. {ECO:0000256|HAMAP- CC Rule:MF_01588}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC 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 CC of 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 EnsemblBacteria; BAM87974; BAM87974; S58_19670. DR KEGG; aol:S58_19670; -. DR PATRIC; fig|1245469.3.peg.2013; -. DR KO; K01972; -. DR OrthoDB; POG091H024G; -. 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; cd00027; BRCT; 1. DR CDD; cd00114; LIGANc; 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; 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 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 Complete proteome {ECO:0000313|Proteomes:UP000011841}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01588}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01588}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_01588}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01588}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01588}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01588}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01588}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01588}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01588}. FT DOMAIN 637 710 BRCT. {ECO:0000259|PROSITE:PS50172}. FT NP_BIND 49 53 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT NP_BIND 98 99 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT ACT_SITE 133 133 N6-AMP-lysine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01588}. FT METAL 436 436 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. FT METAL 438 438 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. FT METAL 466 466 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 131 131 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 154 154 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 191 191 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 307 307 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 331 331 NAD. {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 //