ID   LIGB_PSEPG              Reviewed;         566 AA.
AC   B0KLZ2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
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};
GN   OrderedLocusNames=PputGB1_5017;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000926; ABZ00902.1; -; Genomic_DNA.
DR   RefSeq; WP_012274527.1; NC_010322.1.
DR   AlphaFoldDB; B0KLZ2; -.
DR   SMR; B0KLZ2; -.
DR   STRING; 76869.PputGB1_5017; -.
DR   EnsemblBacteria; ABZ00902; ABZ00902; PputGB1_5017.
DR   KEGG; ppg:PputGB1_5017; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   Proteomes; UP000002157; 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; 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.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Ligase; NAD.
FT   CHAIN           1..566
FT                   /note="DNA ligase B"
FT                   /id="PRO_1000087957"
FT   ACT_SITE        125
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   566 AA;  62675 MW;  712F0B54C3448FE4 CRC64;
     MPYLLLFAML FALNTPLAWA ASCPDWTPQK AEAEAAQLQA TLTGWDEHYH RQGIALVADE
     LYDQSRQRLV HLQQCFGLAP SPSPLTSARG PLPHPVPHTG VDKLADRQAV ARWMAGKTGV
     WVQPKFDGVA ASLIYRQGQL VQLISRGDGL QGHDWSRHIP QLGAVTRQLP QAIDLHLQGE
     LYLRLNEHVQ AKAGSANARG TVAGLLARKQ LTREQGNTIG LFVWGWPHGP ERQADRLAQL
     AQLGFPDSQH YSIAVDTLED AARWREHWYR SPLPFASDGV ILRLGSRPPA ERWQAKAPYW
     IAAWKYPYVQ ALAEVRDVRF RVGRTGRITP IAHVQPVTLD DRRITQVSLG SLARWQALDI
     RPGDQVAISL AGLTIPRLEH VVHRAVERQP LGAPAPGRHH ALSCWQPSEG CEEQFIARLT
     WLSGKQGLAL PRTGPGTWRR LVDAGLVTSM TDWLQLDAER LQQVPGISSL TAAQLLGSFD
     QARSRPFDQW LRGLGAPIGK HLQLTGGWQE MASRSAGQWQ TVPDIGVKRS RQLVGFFAAA
     EVQAIATRLA ESGIEGFSPP PERIEQ