ID   LIGB_PSEPK              Reviewed;         566 AA.
AC   Q88D59;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=DNA ligase B {ECO:0000255|HAMAP-Rule:MF_01587};
DE            EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01587};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B {ECO:0000255|HAMAP-Rule:MF_01587};
GN   Name=ligB {ECO:0000255|HAMAP-Rule:MF_01587}; OrderedLocusNames=PP_4968;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Catalyzes the formation of phosphodiester linkages between
CC       5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD
CC       as a coenzyme and as the energy source for the reaction.
CC       {ECO:0000255|HAMAP-Rule:MF_01587}.
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_01587};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01587}.
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DR   EMBL; AE015451; AAN70535.1; -; Genomic_DNA.
DR   RefSeq; NP_747071.1; NC_002947.4.
DR   RefSeq; WP_010955540.1; NC_002947.4.
DR   AlphaFoldDB; Q88D59; -.
DR   SMR; Q88D59; -.
DR   STRING; 160488.PP_4968; -.
DR   EnsemblBacteria; AAN70535; AAN70535; PP_4968.
DR   KEGG; ppu:PP_4968; -.
DR   PATRIC; fig|160488.4.peg.5305; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   PhylomeDB; Q88D59; -.
DR   BioCyc; PPUT160488:G1G01-5312-MON; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_01587; DNA_ligase_B; 1.
DR   InterPro; IPR020923; DNA_ligase_B.
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   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Ligase; NAD; Reference proteome.
FT   CHAIN           1..566
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000313547"
FT   ACT_SITE        125
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   566 AA;  62721 MW;  7BF392E60E52A015 CRC64;
     MPYLLLFALL FVLNTPLARA ASCPHWNPQQ AKAEVAQLRA TLARWDEHYH RQGIALVADE
     LYDQSHERLN HLQQCFAVGT SPSPLASARG PVPHPVPHTG VDKLADRQAV ARWMTGKTGV
     WVQPKVDGVA VSLTYQQGRL VQLTSRGDGV HGHDWSRHIP QLGAVTRQLP EAVDLHLQGE
     LYLRLDEHVQ AKAGSANARG TVAGLLARKQ LTGAQGNAIG LFVWGWPHGP EQQAERLAQL
     ARLGFPDSQL YSIAIDTLED AAHWREHWYR SALPFATDGV ILRQGSRPPA ERWQAKAPYW
     IAAWKYPYAQ ALAEVRDVRF RVGRTGRVTP VLHVQPVTLD DRRITQVSLG SLARWQRLDI
     RPGDQVAISL AGLTIPRLEH VVHRAVERQP ITAPAPDQHH AHSCWQASEG CDEQFIARLT
     WLGGKQGLAL PRTGPGTWRR LVEAGLVTSM TDWLQLDAER LQQAPGISRL TATQMLGSFD
     QARSRPFDQW LRALGVPIGK HLPLTGNWQA LASRSAGQWQ TVPGIGAKRS RQLVEFFAAS
     EVQAIAAQLA EAGIEGFRTP PQRIEQ