ID   LIGB_PSEMY              Reviewed;         562 AA.
AC   A4XPF7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Pmen_0453;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
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., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP83223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XPF7; -.
DR   SMR; A4XPF7; -.
DR   STRING; 399739.Pmen_0453; -.
DR   EnsemblBacteria; ABP83223; ABP83223; Pmen_0453.
DR   KEGG; pmy:Pmen_0453; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
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; 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   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.
FT   CHAIN           1..562
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000318799"
FT   ACT_SITE        125
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   562 AA;  62570 MW;  6E44B8472004484C CRC64;
     MLAMKRWIAP LLLPLIAQAE PCPDWPDSRA QVEFAALSQQ IAQWDDAYHN QGRSPIADEL
     YDQARERLQR WQQCFAPARQ PLPEPLTGSA GPIAHPVPQT GLRKLNDAAI GEWIGSRDDL
     WIQPKVDGVA VTLVYRQGRL HQAISRGDGR HGQDWSARAR QLPAVPTRLP EALDLVLQGE
     LYWRLEDHLQ ARDGGAGARG KVAGMMARHE LSDTDGAAIG LFVWDWPDGP ASMDERLSQL
     QALGFADSQH YSKPIRSVEE ARQWRQHWYR HRLPFASDGV VLRQGTRPAG ARWQAEAPHW
     AVAWKYPASQ ALAVVQAVDF RIGRSGRITP VLRLQPVDLD DRRISRVALG SVPTWKSLDV
     RPGDQVAIRL AGLTIPRLDS VIWRSPHRAP VEVPRSADYH ALSCWRSSPS CQHQFQARLA
     WLSSKQGLAL SGVGPGTWSS LPLQGLLDWL ELDKAQLQSL PGIGPRRAAQ LQQAFAQARD
     RPLQQWLRAL GAPPGFDAGG LDDWPSLIER QRDDWLRRPG VGPKGADRLL AFFSHPEVQR
     LGRQLQQAGV AGFQPQAGPP RS