ID   LIGB_ENT38              Reviewed;         556 AA.
AC   A4W502;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Ent638_0092;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP58782.1; -; Genomic_DNA.
DR   RefSeq; WP_011915360.1; NC_009436.1.
DR   AlphaFoldDB; A4W502; -.
DR   SMR; A4W502; -.
DR   STRING; 399742.Ent638_0092; -.
DR   PRIDE; A4W502; -.
DR   EnsemblBacteria; ABP58782; ABP58782; Ent638_0092.
DR   KEGG; ent:Ent638_0092; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   OrthoDB; 241401at2; -.
DR   Proteomes; UP000000230; 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; IPR018239; DNA_ligase_AS.
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; 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; NAD.
FT   CHAIN           1..556
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000381947"
FT   ACT_SITE        122
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   556 AA;  62808 MW;  FE753007A2B053A3 CRC64;
     MWKWAGVVVM VWSSYGTAIC PAWSHAKAEQ EIAGLNAQIS RWNDAYWQEG KSDVSDEIYD
     QLNTRLKQWQ QCFNHEPATE DIPPANGTLR HPFAHTGVHK VSGKEELRQW MHSRRDLWVQ
     PKVDGVAVTL VYRKGKLVQA ISRGDGVKGE DWTARVQAIP SVPLNVKGVL SESVLQGEIF
     LRCERHIQQQ MGGMNARAKV AGMMMRQNNK TVLENLGVFI WAWPDGPQSM PQRLSELTKA
     GFTLTAQYTR AVSTADEVEK NRKEWLTSSL PFVTDGIVVR SSIEPVGEQW LPGEGDWVVA
     WKYSPVSQVA EVNAIQFAIG RTGKISVVAV LESIQLDDKR VKRVNLGSVS RWQALDIAPG
     DQILVSLAGQ GIPRVDKVVW RGNDRKKPAP PASQYHSLTC FYASPECLEQ FFARLVWLSS
     KQILNMEGLG DSSWRLLHQT YHFEHIFSWL AVTQEQIEKT SGLNPARRLQ LWHRFELARH
     HPFKKWIKAL GIPLPQAAAD ALSVHSWRQL QDKDAVSWNQ LPGIGTEKAR KLVEFVHDSQ
     ITRLATWLGE QGIDGF